[1]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND INVOLVEMENT IN JUVENILE PARKINSON DISEASE. TISSUE=Fetal brain, and Skeletal muscle; DOI=10.1038/33416; PubMed=9560156 [NCBI, ExPASy, EBI, Israel, Japan] Kitada T., Asakawa S., Hattori N., Matsumine H., Yamamura Y., Minoshima S., Yokochi M., Mizuno Y., Shimizu N.; "Mutations in the parkin gene cause autosomal recessive juvenile parkinsonism."; Nature 392:605-608(1998).
[2]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 4). D'Agata V., Scapagnini G., Cavallaro S.; "Functional and molecular diversity of parkin."; Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. DOI=10.1038/nature02055; PubMed=14574404 [NCBI, ExPASy, EBI, Israel, Japan] Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.; "The DNA sequence and analysis of human chromosome 6."; Nature 425:805-811(2003).
[4]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5). TISSUE=Testis; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).
[5]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 312-361. Zou H.Q., Chan P.; Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
[6]	SUBCELLULAR LOCATION. DOI=10.1002/1531-8249(199905)45:5<668::AID-ANA19>3.0.CO;2-Z; PubMed=10319893 [NCBI, ExPASy, EBI, Israel, Japan] Shimura H., Hattori N., Kubo S., Yoshikawa M., Kitada T., Matsumine H., Asakawa S., Minoshima S., Yamamura Y., Shimizu N., Mizuno Y.; "Immunohistochemical and subcellular localization of Parkin protein: absence of protein in autosomal recessive juvenile parkinsonism patients."; Ann. Neurol. 45:668-672(1999).
[7]	FUNCTION IN UBIQUITINATION. DOI=10.1074/jbc.C000447200; PubMed=10973942 [NCBI, ExPASy, EBI, Israel, Japan] Imai Y., Soda M., Takahashi R.; "Parkin suppresses unfolded protein stress-induced cell death through its E3 ubiquitin-protein ligase activity."; J. Biol. Chem. 275:35661-35664(2000).
[8]	FUNCTION, AND CHARACTERIZATION OF VARIANTS PD PRO-42 AND ARG-240. DOI=10.1038/77060; PubMed=10888878 [NCBI, ExPASy, EBI, Israel, Japan] Shimura H., Hattori N., Kubo S., Mizuno Y., Asakawa S., Minoshima S., Shimizu N., Iwai K., Chiba T., Tanaka K., Suzuki T.; "Familial Parkinson disease gene product, parkin, is a ubiquitin-protein ligase."; Nat. Genet. 25:302-305(2000).
[9]	INTERACTION WITH UBE2L6 AND SEPT5, AND UBIQUITINATION OF SEPT5. DOI=10.1073/pnas.240347797; PubMed=11078524 [NCBI, ExPASy, EBI, Israel, Japan] Zhang Y., Gao J., Chung K.K.K., Huang H., Dawson V.L., Dawson T.M.; "Parkin functions as an E2-dependent ubiquitin-protein ligase and promotes the degradation of the synaptic vesicle-associated protein, CDCrel-1."; Proc. Natl. Acad. Sci. U.S.A. 97:13354-13359(2000).
[10]	UBIQUITINATION OF GPR37. DOI=10.1016/S0092-8674(01)00407-X; PubMed=11439185 [NCBI, ExPASy, EBI, Israel, Japan] Imai Y., Soda M., Inoue H., Hattori N., Mizuno Y., Takahashi R.; "An unfolded putative transmembrane polypeptide, which can lead to endoplasmic reticulum stress, is a substrate of Parkin."; Cell 105:891-902(2001).
[11]	INTERACTION, UBIQUITINATION OF SNCAIP, CHARACTERIZATION OF VARIANTS PARK2 ARG-240; CYS-256; TRP-275 AND ASN-415, AND MUTAGENESIS OF CYS-337; CYS-421 AND CYS-431. DOI=10.1038/nm1001-1144; PubMed=11590439 [NCBI, ExPASy, EBI, Israel, Japan] Chung K.K.K., Zhang Y., Lim K.L., Tanaka Y., Huang H., Gao J., Ross C.A., Dawson V.L., Dawson T.M.; "Parkin ubiquitinates the alpha-synuclein-interacting protein, synphilin-1: implications for Lewy-body formation in Parkinson disease."; Nat. Med. 7:1144-1150(2001).
[12]	UBIQUITINATION OF AN O-GLYCOSYLATED ISOFORM OF SNCAIP, SUBCELLULAR LOCATION, AND CHARACTERIZATION OF VARIANTS PD PRO-42 AND ARG-240. DOI=10.1126/science.1060627; PubMed=11431533 [NCBI, ExPASy, EBI, Israel, Japan] Shimura H., Schlossmacher M.G., Hattori N., Frosch M.P., Trockenbacher A., Schneider R., Mizuno Y., Kosik K.S., Selkoe D.J.; "Ubiquitination of a new form of alpha-synuclein by parkin from human brain: implications for Parkinson's disease."; Science 293:263-269(2001).
[13]	PRESENCE OF ATYPICAL RING FINGER DOMAINS. PubMed=12446796 [NCBI, ExPASy, EBI, Israel, Japan] Marin I., Ferrus A.; "Comparative genomics of the RBR family, including the Parkinson's disease-related gene parkin and the genes of the ariadne subfamily."; Mol. Biol. Evol. 19:2039-2050(2002).
[14]	INTERACTION WITH STUB1 AND HSP70, AND UBIQUITINATION OF STUB1. DOI=10.1016/S1097-2765(02)00583-X; PubMed=12150907 [NCBI, ExPASy, EBI, Israel, Japan] Imai Y., Soda M., Hatakeyama S., Akagi T., Hashikawa T., Nakayama K., Takahashi R.; "CHIP is associated with Parkin, a gene responsible for familial Parkinson's disease, and enhances its ubiquitin ligase activity."; Mol. Cell 10:55-67(2002).
[15]	INTERACTION WITH SYT11, CHARACTERIZATION OF VARIANT PD GLY-289, AND MUTAGENESIS OF CYS-418. DOI=10.1093/hmg/ddg269; PubMed=12925569 [NCBI, ExPASy, EBI, Israel, Japan] Huynh D.P., Scoles D.R., Nguyen D., Pulst S.M.; "The autosomal recessive juvenile Parkinson disease gene product, parkin, interacts with and ubiquitinates synaptotagmin XI."; Hum. Mol. Genet. 12:2587-2597(2003).
[16]	INTERACTION WITH PACRG. DOI=10.1074/jbc.M309655200; PubMed=14532270 [NCBI, ExPASy, EBI, Israel, Japan] Imai Y., Soda M., Murakami T., Shoji M., Abe K., Takahashi R.; "A product of the human gene adjacent to parkin is a component of Lewy bodies and suppresses Pael receptor-induced cell death."; J. Biol. Chem. 278:51901-51910(2003).
[17]	FUNCTION, INTERACTION WITH FBXW7 AND CUL1, AND UBIQUITINATION OF CYCLIN E. DOI=10.1016/S0896-6273(03)00084-9; PubMed=12628165 [NCBI, ExPASy, EBI, Israel, Japan] Staropoli J.F., McDermott C., Martinat C., Schulman B., Demireva E., Abeliovich A.; "Parkin is a component of an SCF-like ubiquitin ligase complex and protects postmitotic neurons from kainate excitotoxicity."; Neuron 37:735-749(2003).
[18]	INVOLVEMENT IN CANCER. DOI=10.1038/sj.onc.1207072; PubMed=14614460 [NCBI, ExPASy, EBI, Israel, Japan] Denison S.R., Wang F., Becker N.A., Schuele B., Kock N., Phillips L.A., Klein C., Smith D.I.; "Alterations in the common fragile site gene Parkin in ovarian and other cancers."; Oncogene 22:8370-8378(2003).
[19]	FUNCTION, AND INVOLVEMENT IN CANCER. DOI=10.1073/pnas.0931262100; PubMed=12719539 [NCBI, ExPASy, EBI, Israel, Japan] Cesari R., Martin E.S., Calin G.A., Pentimalli F., Bichi R., McAdams H., Trapasso F., Drusco A., Shimizu M., Masciullo V., D'Andrilli G., Scambia G., Picchio M.C., Alder H., Godwin A.K., Croce C.M.; "Parkin, a gene implicated in autosomal recessive juvenile parkinsonism, is a candidate tumor suppressor gene on chromosome 6q25-q27."; Proc. Natl. Acad. Sci. U.S.A. 100:5956-5961(2003).
[20]	REVIEW. DOI=10.1038/sj.embor.7400188; PubMed=15229644 [NCBI, ExPASy, EBI, Israel, Japan] Kahle P.J., Haass C.; "How does parkin ligate ubiquitin to Parkinson's disease?"; EMBO Rep. 5:681-685(2004).
[21]	FUNCTION, UBIQUITINATION, AND S-NITROSYLATION. DOI=10.1126/science.1093891; PubMed=15105460 [NCBI, ExPASy, EBI, Israel, Japan] Chung K.K.K., Thomas B., Li X., Pletnikova O., Troncoso J.C., Marsh L., Dawson V.L., Dawson T.M.; "S-nitrosylation of parkin regulates ubiquitination and compromises parkin's protective function."; Science 304:1328-1331(2004).
[22]	INTERACTION WITH LRRK2. DOI=10.1073/pnas.0508052102; PubMed=16352719 [NCBI, ExPASy, EBI, Israel, Japan] Smith W.W., Pei Z., Jiang H., Moore D.J., Liang Y., West A.B., Dawson V.L., Dawson T.M., Ross C.A.; "Leucine-rich repeat kinase 2 (LRRK2) interacts with parkin and mutant LRRK2 induces neuronal degeneration."; Proc. Natl. Acad. Sci. U.S.A. 102:18676-18681(2005).
[23]	INTERACTION WITH RANBP2. DOI=10.1074/jbc.M504994200; PubMed=16332688 [NCBI, ExPASy, EBI, Israel, Japan] Um J.W., Min D.S., Rhim H., Kim J., Paik S.R., Chung K.C.; "Parkin ubiquitinates and promotes the degradation of RanBP2."; J. Biol. Chem. 281:3595-3603(2006).
[24]	INTERACTION WITH SUMO1, AND SUBCELLULAR LOCATION. DOI=10.1002/jnr.21041; PubMed=16955485 [NCBI, ExPASy, EBI, Israel, Japan] Um J.W., Chung K.C.; "Functional modulation of parkin through physical interaction with SUMO-1."; J. Neurosci. Res. 84:1543-1554(2006).
[25]	STRUCTURE BY NMR OF 1-76, AND INTERACTION WITH PSMD4. DOI=10.1038/sj.embor.embor764; PubMed=12634850 [NCBI, ExPASy, EBI, Israel, Japan] Sakata E., Yamaguchi Y., Kurimoto E., Kikuchi J., Yokoyama S., Yamada S., Kawahara H., Yokosawa H., Hattori N., Mizuno Y., Tanaka K., Kato K.; "Parkin binds the Rpn10 subunit of 26S proteasomes through its ubiquitin-like domain."; EMBO Rep. 4:301-306(2003).
[26]	STRUCTURE BY NMR OF 307-384 IN COMPLEX WITH ZINC IONS, CHARACTERIZATION OF VARIANT PARK2 PRO-351, MUTAGENESIS OF CYS-332 AND CYS-365, AND MASS SPECTROMETRY. DOI=10.1073/pnas.0610548104; PubMed=17360614 [NCBI, ExPASy, EBI, Israel, Japan] Beasley S.A., Hristova V.A., Shaw G.S.; "Structure of the Parkin in-between-ring domain provides insights for E3-ligase dysfunction in autosomal recessive Parkinson's disease."; Proc. Natl. Acad. Sci. U.S.A. 104:3095-3100(2007).
[27]	REVIEW ON VARIANTS. DOI=10.1093/hmg/ddh089; PubMed=14976155 [NCBI, ExPASy, EBI, Israel, Japan] Mata I.F., Lockhart P.J., Farrer M.J.; "Parkin genetics: one model for Parkinson's disease."; Hum. Mol. Genet. 13:R127-R133(2004).
[28]	VARIANT PARK2 ARG-240. DOI=10.1006/bbrc.1998.9134; PubMed=9731209 [NCBI, ExPASy, EBI, Israel, Japan] Hattori N., Matsumine H., Asakawa S., Kitada T., Yoshino H., Elibol B., Brookes A.J., Yamamura Y., Kobayashi T., Wang M., Yoritaka A., Minoshima S., Shimizu N., Mizuno Y.; "Point mutations (Thr240Arg and Gln311Stop) in the Parkin gene."; Biochem. Biophys. Res. Commun. 249:754-758(1998).
[29]	ERRATUM. Hattori N., Matsumine H., Asakawa S., Kitada T., Yoshino H., Elibol B., Brookes A.J., Yamamura Y., Kobayashi T., Wang M., Yoritaka A., Minoshima S., Shimizu N., Mizuno Y.; Biochem. Biophys. Res. Commun. 251:666-666(1998).
[30]	VARIANTS PARK2 ASN-161; CYS-256; TRP-275 AND ASN-415, AND VARIANTS ASN-167; LEU-380 AND ASN-394. DOI=10.1093/hmg/8.4.567; PubMed=10072423 [NCBI, ExPASy, EBI, Israel, Japan] Abbas N., Luecking C.B., Ricard S., Duerr A., Bonifati V., De Michele G., Bouley S., Vaughan J.R., Gasser T., Marconi R., Broussolle E., Brefel-Courbon C., Harhangi B.S., Oostra B.A., Fabrizio E., Bohme G.A., Pradier L., Wood N.W., Filla A., Meco G., Denefle P., Agid Y., Brice A.; "A wide variety of mutations in the parkin gene are responsible for autosomal recessive parkinsonism in Europe."; Hum. Mol. Genet. 8:567-574(1999).
[31]	VARIANT ASN-167. PubMed=10511432 [NCBI, ExPASy, EBI, Israel, Japan] Satoh J., Kuroda Y.; "Association of codon 167 Ser/Asn heterozygosity in the parkin gene with sporadic Parkinson's disease."; NeuroReport 10:2735-2739(1999).
[32]	VARIANT PARK2 PHE-431. DOI=10.1002/1531-8249(200008)48:2<245::AID-ANA15>3.3.CO;2-U; PubMed=10939576 [NCBI, ExPASy, EBI, Israel, Japan] Maruyama M., Ikeuchi T., Saito M., Ishikawa A., Yuasa T., Tanaka H., Hayashi S., Wakabayashi K., Takahashi H., Tsuji S.; "Novel mutations, pseudo-dominant inheritance, and possible familial affects in patients with autosomal recessive juvenile parkinsonism."; Ann. Neurol. 48:245-250(2000).
[33]	VARIANTS ASN-167; TRP-366 AND LEU-380. DOI=10.1159/000008203; PubMed=10965160 [NCBI, ExPASy, EBI, Israel, Japan] Hu C.-J., Sung S.-M., Liu H.-C., Lee C.-C., Tsai C.-H., Chang J.-G.; "Polymorphisms of the parkin gene in sporadic Parkinson's disease among Chinese in Taiwan."; Eur. Neurol. 44:90-93(2000).
[34]	VARIANTS PD ASN-161; ASN-211; CYS-256; TRP-275; ASN-280; GLY-289; GLU-328; CYS-334; ASN-415 AND ASP-430. DOI=10.1056/NEJM200005253422103; PubMed=10824074 [NCBI, ExPASy, EBI, Israel, Japan] Luecking C.B., Duerr A., Bonifati V., Vaughan J.R., De Michele G., Gasser T., Harhangi B.S., Meco G., Denefle P., Wood N.W., Agid Y., Brice A.; "Association between early-onset Parkinson's disease and mutations in the parkin gene."; N. Engl. J. Med. 342:1560-1567(2000).
[35]	VARIANTS PD ARG-211; TRP-275 AND ASP-430. DOI=10.1086/318791; PubMed=11179010 [NCBI, ExPASy, EBI, Israel, Japan] Periquet M., Luecking C.B., Vaughan J.R., Bonifati V., Duerr A., De Michele G., Horstink M., Farrer M., Illarioshkin S.N., Pollak P., Borg M., Brefel-Courbon C., Denefle P., Meco G., Gasser T., Breteler M.M., Wood N.W., Agid Y., Brice A.; "Origin of the mutations in the parkin gene in Europe: exon rearrangements are independent recurrent events, whereas point mutations may result from founder effects."; Am. J. Hum. Genet. 68:617-626(2001).
[36]	VARIANT PARK2 GLU-82. DOI=10.1093/hmg/10.16.1649; PubMed=11487568 [NCBI, ExPASy, EBI, Israel, Japan] Hedrich K., Kann M., Lanthaler A.J., Dalski A., Eskelson C., Landt O., Schwinger E., Vieregge P., Lang A.E., Breakefield X.O., Ozelius L.J., Pramstaller P.P., Klein C.; "The importance of gene dosage studies: mutational analysis of the parkin gene in early-onset parkinsonism."; Hum. Mol. Genet. 10:1649-1656(2001).
[37]	VARIANT PARK2 TYR-212. DOI=10.1016/S0304-3940(00)01733-X; PubMed=11163284 [NCBI, ExPASy, EBI, Israel, Japan] Pineda-Trujillo N., Carvajal-Carmona L.G., Buritica O., Moreno S., Uribe C., Pineda D., Toro M., Garcia F., Arias W., Bedoya G., Lopera F., Ruiz-Linares A.; "A novel Cys212Tyr founder mutation in parkin and allelic heterogeneity of juvenile parkinsonism in a population from North West Colombia."; Neurosci. Lett. 298:87-90(2001).
[38]	VARIANTS PD GLU-82; CYS-256; TRP-275; GLU-328 AND 441-ARG. DOI=10.1002/ajmg.10525; PubMed=12116199 [NCBI, ExPASy, EBI, Israel, Japan] French Parkinson's disease genetics study group; European consortium on genetic susceptibility on Parkinson's disease; West A., Periquet M., Lincoln S., Luecking C.B., Nicholl D., Bonifati V., Rawal N., Gasser T., Lohmann E., Deleuze J.-F., Maraganore D., Levey A., Wood N.W., Duerr A., Hardy J., Brice A., Farrer M.; "Complex relationship between parkin mutations and Parkinson disease."; Am. J. Med. Genet. 114:584-591(2002).
[39]	ERRATUM. French Parkinson's disease genetics study group; European consortium on genetic susceptibility on Parkinson's disease; West A., Periquet M., Lincoln S., Luecking C.B., Nicholl D., Bonifati V., Rawal N., Gasser T., Lohmann E., Deleuze J.-F., Maraganore D., Levey A., Wood N.W., Duerr A., Hardy J., Brice A., Farrer M.J.; Am. J. Med. Genet. 114:992-992(2002).
[40]	VARIANTS PARK2 LEU-37 AND PRO-351. DOI=10.1002/ana.10179; PubMed=12112109 [NCBI, ExPASy, EBI, Israel, Japan] Kann M., Jacobs H., Mohrmann K., Schumacher K., Hedrich K., Garrels J., Wiegers K., Schwinger E., Pramstaller P.P., Breakefield X.O., Ozelius L.J., Vieregge P., Klein C.; "Role of parkin mutations in 111 community-based patients with early-onset parkinsonism."; Ann. Neurol. 51:621-625(2002).
[41]	VARIANTS PD ASN-211; TRP-275; ASP-430 AND LEU-437. DOI=10.1136/jmg.39.7.489; PubMed=12114481 [NCBI, ExPASy, EBI, Israel, Japan] Nichols W.C., Pankratz N., Uniacke S.K., Pauciulo M.W., Halter C., Rudolph A., Conneally P.M., Foroud T.; "Linkage stratification and mutation analysis at the parkin locus identifies mutation positive Parkinson's disease families."; J. Med. Genet. 39:489-492(2002).
[42]	VARIANT PD MET-15, AND VARIANTS LEU-380 AND ASN-394. DOI=10.1136/jnnp.73.5.582; PubMed=12397156 [NCBI, ExPASy, EBI, Israel, Japan] Munoz E., Tolosa E., Pastor P., Marti M.J., Valldeoriola F., Campdelacreu J., Oliva R.; "Relative high frequency of the c.255delA parkin gene mutation in Spanish patients with autosomal recessive parkinsonism."; J. Neurol. Neurosurg. Psych. 73:582-584(2002).
[43]	VARIANTS PD PRO-42; VAL-192; CYS-256; TRP-275; ASP-430 AND LEU-437. PubMed=11971093 [NCBI, ExPASy, EBI, Israel, Japan] Hedrich K., Marder K., Harris J., Kann M., Lynch T., Meija-Santana H., Pramstaller P.P., Schwinger E., Bressman S.B., Fahn S., Klein C.; "Evaluation of 50 probands with early-onset Parkinson's disease for parkin mutations."; Neurology 58:1239-1246(2002).
[44]	VARIANT PD PRO-46. PubMed=12362318 [NCBI, ExPASy, EBI, Israel, Japan] Xu Y., Liu Z., Wang Y., Tao E., Chen G., Chen B.; "A new point mutation on exon 2 of parkin gene in Parkinson's disease."; Zhonghua Yi Xue Yi Chuan Xue Za Zhi 19:409-411(2002).
[45]	VARIANTS PD GLN-33; TYR-253; CYS-256; TRP-275; ASN-280; ASP-430 AND LEU-437, AND VARIANTS GLU-82; LEU-380 AND ASN-394. DOI=10.1002/ana.10524; PubMed=12730996 [NCBI, ExPASy, EBI, Israel, Japan] Oliveira S.A., Scott W.K., Martin E.R., Nance M.A., Watts R.L., Hubble J.P., Koller W.C., Pahwa R., Stern M.B., Hiner B.C., Ondo W.G., Allen F.H. Jr., Scott B.L., Goetz C.G., Small G.W., Mastaglia F., Stajich J.M., Zhang F., Booze M.W., Winn M.P., Middleton L.T., Haines J.L., Pericak-Vance M.A., Vance J.M.; "Parkin mutations and susceptibility alleles in late-onset Parkinson's disease."; Ann. Neurol. 53:624-629(2003).
[46]	VARIANTS PD VAL-192; ASN-211; MET-240 AND LEU-437, AND VARIANT ASN-167. PubMed=12629236 [NCBI, ExPASy, EBI, Israel, Japan] Foroud T., Uniacke S.K., Liu L., Pankratz N., Rudolph A., Halter C., Shults C., Marder K., Conneally P.M., Nichols W.C.; "Heterozygosity for a mutation in the parkin gene leads to later onset Parkinson disease."; Neurology 60:796-801(2003).
[47]	VARIANTS HIS-100; SER-271 AND SER-339. PubMed=12781599 [NCBI, ExPASy, EBI, Israel, Japan] Chen R., Gosavi N.S., Langston J.W., Chan P.; "Parkin mutations are rare in patients with young-onset parkinsonism in a US population."; Parkinsonism Relat. Disord. 9:309-312(2003).

Comments

FUNCTION: Functions within a multiprotein E3 ubiquitin ligase complex, catalyzing the covalent attachment of ubiquitin moieties onto substrate proteins. These substrates include SYT11, CCNE1, GPR37, STUB1, a 22 kDa O-linked glycosylated isoform of SNCAIP and SEPT5. May play a more general role in the ubiquitin proteasomal pathway by participating in the removal and/or detoxification of abnormally folded or damaged protein. Loss of this ubiquitin ligase activity appears to be the mechanism underlying pathogenesis of PARK2. May protect neurons against alpha synuclein toxicity, proteasomal dysfunction, GPR37 accumulation, and kainate-induced excitotoxicity. May play a role in controlling neurotransmitter trafficking at the presynaptic terminal and in calcium-dependent exocytosis. Regulates cyclin E during neuronal apoptosis. May represent a tumor suppressor gene.
PATHWAY: Protein modification; protein ubiquitination .
SUBUNIT: Forms an E3 ubiquitin ligase complex with UBE2L3 or UBE2L6. Part of a SCF-like complex, consisting of PARK2, CUL1 and FBXW7. Interacts with SNCAIP. Binds to the C2A and C2B domains of SYT11. Interacts and regulates the turnover of SEPT5. Part of a complex, including STUB1, HSP70 and GPR37. The amount of STUB1 in the complex increases during ER stress. STUB1 promotes the dissociation of HSP70 from PARK2 and GPR37, thus facilitating PARK2-mediated GPR37 ubiquitination. HSP70 transiently associates with unfolded GPR37 and inhibits the E3 activity of PARK2, whereas, STUB1 enhances the E3 activity of PARK2 through promotion of dissociation of HSP70 from PARK2-GPR37 complexes. Interacts with PSMD4 and PACRG. Interacts with LRRK2. Interacts with RANBP2. Interacts with SUMO1 but not SUMO2, which promotes nuclear localization and autoubiquitination.
INTERACTION:
P49792:RANBP2; NbExp=6; IntAct=EBI-716346, EBI-973138;
SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Co-localizes with SYT11 in neutrites. Co-localizes with SNCAIP in brainstem Lewy bodies.

ALTERNATIVE PRODUCTS: 5 named isoforms [FASTA] produced by alternative splicing.

Name	1
Isoform ID	O60260-1
This is the isoform sequence displayed in this entry.

Name	2
Isoform ID	O60260-2
Features which should be applied to build the isoform sequence: VSP_011707.

Name	3
Isoform ID	O60260-3
Features which should be applied to build the isoform sequence: VSP_011706, VSP_011709, VSP_011710.

Name	4
Isoform ID	O60260-4
Features which should be applied to build the isoform sequence: VSP_011705.

Name	5
Isoform ID	O60260-5
Features which should be applied to build the isoform sequence: VSP_011708, VSP_011711, VSP_011712.

TISSUE SPECIFICITY: Highly expressed in the brain including the substantia nigra. Expressed in heart, testis and skeletal muscle. Expression is down-regulated or absent in tumor biopsies, and absent in the brain of PARK2 patients. Overexpression protects dopamine neurons from kainate-mediated apoptosis.
DOMAIN: The ubiquitin-like domain binds the PSMD4 subunit of 26S proteasomes.
PTM: Auto-ubiquitinates in an E2-dependent manner leading to its own degradation.
PTM: S-nitrosylated. The inhibition of PARK2 ubiquitin E3 ligase activity by S-nitrosylation could contribute to the degenerative process in PD by impairing the ubiquitination of PARK2 substrates.
DISEASE: Defects in PARK2 are a cause of Parkinson disease (PD) [MIM:168600]. PD is a complex, multifactorial disorder that typically manifests after the age of 50 years, although early-onset cases (before 50 years) are known. PD generally arises as a sporadic condition but is occasionally inherited as a simple mendelian trait. Although sporadic and familial PD are very similar, inherited forms of the disease usually begin at earlier ages and are associated with atypical clinical features. PD is characterized by bradykinesia, resting tremor, muscular rigidity and postural instability, as well as by a clinically significant response to treatment with levodopa. The pathology of PD involves the loss of dopaminergic neurons in the substantia nigra and the presence of Lewy bodies (intraneuronal accumulations of aggregated proteins), in surviving neurons in various areas of the brain.
DISEASE: Defects in PARK2 are the cause of autosomal recessive early onset Parkinson disease 2 (PARK2) [MIM:600116]; also known as early-onset parkinsonism with diurnal fluctuation (EPDF) or autosomal recessive juvenile Parkinson disease (PDJ). PARK2 is symptomatically different in several aspects from idiopathic Parkinson disease, although classic symptoms such as bradykinesia, rigidity and tremor are present. Additional clinical features include early DOPA-induced dyskinesia, diurnal fluctuation of the symptoms, sleep benefit, dystonia and hyper-reflexia. PARK2 is usually characterized by onset before 40, with a mean age at onset of 23.2 years. Pathologically, PARK2 patients show loss of dopaminergic neurons in the substantia nigra, similar to that seen in Parkinson disease; however, Lewy bodies (intraneuronal accumulations of aggregated proteins) are absent.
DISEASE: Defects in PARK2 may be involved in the development and/or progression of ovarian cancer.
MISCELLANEOUS: The parkin locus (PRKN), adjacent to the 6q telomere is hyper-recombinable and lies within FRA6E, the third most common fragile site in tumor tissue.
SIMILARITY: Belongs to the RBR family. Parkin subfamily.
SIMILARITY: Contains 1 IBR-type zinc finger.
SIMILARITY: Contains 2 RING-type zinc fingers.
SIMILARITY: Contains 1 ubiquitin-like domain.
WEB RESOURCE: Name=GeneReviews; URL="http://www.genetests.org/query?gene=PARK2";.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AB009973; BAA25751.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF381282; AAM21457.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF381283; AAM21458.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF381286; AAM21461.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AL445215; CAH73681.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AL035697; CAH73681.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AL132982; CAH73681.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AP000886; CAH73681.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AP000887; CAH73681.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AP001576; CAH73681.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AP001577; CAH73681.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AP001578; CAH73681.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AP003699; CAH73681.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AL035697; CAI21385.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AL132982; CAI21385.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AL445215; CAI21385.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AP000886; CAI21385.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AP000887; CAI21385.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AP001576; CAI21385.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AP001577; CAI21385.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AP001578; CAI21385.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AP003699; CAI21385.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AL132982; CAI23601.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AL035697; CAI23601.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AL445215; CAI23601.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AP000886; CAI23601.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AP000887; CAI23601.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AP001576; CAI23601.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AP001577; CAI23601.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AP001578; CAI23601.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AP003699; CAI23601.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC022014; AAH22014.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY564225; AAS88422.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

IPI

IPI00005254; -.
IPI00332282; -.
IPI00470427; -.
IPI00470428; -.
IPI00470429; -.

RefSeq

NP_004553.2; -.

UniGene

Hs.132954

3D structure databases

PDB

1IYF; NMR; -; A=1-76.	[ExPASy / RCSB / EBI]
2JMO; NMR; -; A=308-384.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1IYF; -.
2JMO; -.

ModBase

O60260.

Protein-protein interaction databases

IntAct

O60260; 8.

PTM databases

PhosphoSite

O60260; -.

Enzyme and pathway databases

Pathway_Interaction_DB

alphasynuclein_pathway; Alpha-synuclein signaling.

Organism-specific databases

GC06M161740; -.

HIX0023029; -.

HGNC:8607; PARK2.

CAB016257; -.

168600; phenotype. [NCBI / EBI]
600116; phenotype. [NCBI / EBI]
602544; gene. [NCBI / EBI]

Orphanet

2828; Parkinson disease, genetic types.

PharmGKB

PA32942; -.

Gene expression databases

O60260; -.

O60260; -.

HS_PARK2; -.

ENSG00000185345; Homo sapiens.

Ontologies

GO:0005794;	Cellular component: Golgi apparatus (inferred from direct assay from UniProtKB).
GO:0005634;	Cellular component: nucleus (inferred from electronic annotation from UniProtKB-SubCell).
GO:0048471;	Cellular component: perinuclear region of cytoplasm (inferred from direct assay from UniProtKB).
GO:0005515;	Molecular function: protein binding (inferred from physical interaction from UniProtKB).
GO:0004842;	Molecular function: ubiquitin-protein ligase activity (inferred from direct assay from UniProtKB).
GO:0008270;	Molecular function: zinc ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0007417;	Biological process: central nervous system development (traceable author statement from ProtInc).
GO:0042787;	Biological process: protein ubiquitination during ubiquitin-dependent protein catabolic process (inferred from direct assay from UniProtKB).
QuickGo view.

Family and domain databases

InterPro

IPR003977; Parkin.
IPR016010; Parkin_C.
IPR000626; Ubiquitin.
IPR019954; Ubiquitin_CS.
IPR019955; Ubiquitin_supergroup.
IPR002867; Znf_C6HC.
IPR017907; Znf_RING_CS.
Graphical view of domain structure.

PANTHER

PTHR11685:SF2; Parkin; 1.

Pfam

PF01485; IBR; 1.
PF00240; ubiquitin; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF037880; Parkin; 1.

PRINTS

PR01475; PARKIN.

SMART

SM00647; IBR; 2.
SM00213; UBQ; 1.
SMART graphical view of domain structure.

PROSITE

PS00299; UBIQUITIN_1; FALSE_NEG.
PS50053; UBIQUITIN_2; 1.
PS00518; ZF_RING_1; FALSE_NEG.
PS50089; ZF_RING_2; FALSE_NEG.
PROSITE graphical view of domain structure (profiles).

Proteomic databases

PRIDE

O60260; -.

Genome annotation databases

Ensembl

ENSG00000185345; Homo sapiens. [Contig view]

GeneID

5071; -.

KEGG

hsa:5071; -.

Phylogenomic databases

HOVERGEN

O60260; -.

OMA

O60260; SAEFFFK.

Other

19538; -.

PARK2; Homo sapiens.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Alternative splicing; Cytoplasm; Disease mutation; Ligase; Metal-binding; Nucleus; Parkinson disease; Parkinsonism; Polymorphism; Repeat; S-nitrosylation; Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 465`	`465`	`E3 ubiquitin-protein ligase parkin.`	`PRO_0000058576`
`DOMAIN`	`1 76`	`76`	`Ubiquitin-like.`
`ZN_FING`	`238 293`	`56`	`RING-type 1; atypical.`
`ZN_FING`	`313 377`	`65`	`IBR-type.`
`ZN_FING`	`418 449`	`32`	`RING-type 2.`
`REGION`	`204 238`	`35`	`SYT11 binding 1.`
`REGION`	`257 293`	`37`	`SYT11 binding 2.`
`VAR_SEQ`	`1 191`		`Missing (in isoform 4).`	`VSP_011705`
`VAR_SEQ`	`1 79`		`Missing (in isoform 3).`	`VSP_011706`
`VAR_SEQ`	`179 206`		`Missing (in isoform 2).`	`VSP_011707`
`VAR_SEQ`	`290 290`		`V -> VGTGDTVVLRGALGGFRRGV (in isoform 5).`	`VSP_011708`
`VAR_SEQ`	`291 297`		`AGCPNSL -> VCLLPGM (in isoform 3).`	`VSP_011709`
`VAR_SEQ`	`298 465`		`Missing (in isoform 3).`	`VSP_011710`
`VAR_SEQ`	`362 368`		`FAFCREC -> YGQRRTK (in isoform 5).`	`VSP_011711`
`VAR_SEQ`	`369 465`		`Missing (in isoform 5).`	`VSP_011712`
`VARIANT`	`15 15`	`1`	`V -> M (in PD).`	`VAR_019733`
`VARIANT`	`33 33`	`1`	`R -> Q (in PD).`	`VAR_019734`
`VARIANT`	`37 37`	`1`	`P -> L (in PARK2).`	`VAR_019735`
`VARIANT`	`42 42`	`1`	`R -> P (in PD; early-onset; induces a conformational change in the PSMD4-binding site of Ubl resulting in impaired proteasomal binding).`	`VAR_019736`
`VARIANT`	`46 46`	`1`	`A -> P (in PD; early-onset; sporadic).`	`VAR_019737`
`VARIANT`	`82 82`	`1`	`A -> E (in PARK2 and PD).`	`VAR_019738`
`VARIANT`	`92 92`	`1`	`A -> V (in PARK2).`	`VAR_019739`
`VARIANT`	`100 100`	`1`	`Q -> H.`	`VAR_019740`
`VARIANT`	`161 161`	`1`	`K -> N (in PARK2 and PD).`	`VAR_019741`
`VARIANT`	`167 167`	`1`	`S -> N (in dbSNP:rs1801474 [NCBI]).`	`VAR_019742`
`VARIANT`	`192 192`	`1`	`M -> L (in dbSNP:rs9456735 [NCBI]).`	`VAR_054107`
`VARIANT`	`192 192`	`1`	`M -> V (in PD; early and late onset; dbSNP:rs9456735 [NCBI]).`	`VAR_019743`
`VARIANT`	`211 211`	`1`	`K -> N (in PD; early and late onset).`	`VAR_019744`
`VARIANT`	`211 211`	`1`	`K -> R (in PD; early onset).`	`VAR_019745`
`VARIANT`	`212 212`	`1`	`C -> Y (in PARK2).`	`VAR_019746`
`VARIANT`	`240 240`	`1`	`T -> M (in PD; late onset).`	`VAR_019747`
`VARIANT`	`240 240`	`1`	`T -> R (in PARK2; impairs the ability to ubiquitinate SNCAIP; loss of UBE2L3 binding).`	`VAR_019748`
`VARIANT`	`253 253`	`1`	`C -> Y (in PD; late onset).`	`VAR_019749`
`VARIANT`	`256 256`	`1`	`R -> C (in PARK2 and PD; early and late onset; impairs the ability to ubiquitinate SNCAIP; dbSNP:rs34424986 [NCBI]).`	`VAR_019750`
`VARIANT`	`271 271`	`1`	`R -> S.`	`VAR_019751`
`VARIANT`	`275 275`	`1`	`R -> W (in PARK2 and PD; early and late onset; impairs the ability to ubiquitinate SNCAIP).`	`VAR_019752`
`VARIANT`	`280 280`	`1`	`D -> N (in PD).`	`VAR_019753`
`VARIANT`	`284 284`	`1`	`G -> R (in PARK2).`	`VAR_019754`
`VARIANT`	`289 289`	`1`	`C -> G (in PD; fails to ubiquitinate SYT11; loses ability to bind SYT11).`	`VAR_019755`
`VARIANT`	`328 328`	`1`	`G -> E (in PD).`	`VAR_019756`
`VARIANT`	`334 334`	`1`	`R -> C (in PD).`	`VAR_019757`
`VARIANT`	`339 339`	`1`	`A -> S.`	`VAR_019758`
`VARIANT`	`351 351`	`1`	`T -> P (in PARK2; impairs folding of IBR domain).`	`VAR_019759`
`VARIANT`	`366 366`	`1`	`R -> W.`	`VAR_019760`
`VARIANT`	`380 380`	`1`	`V -> L (in dbSNP:rs1801582 [NCBI]).`	`VAR_019761`
`VARIANT`	`394 394`	`1`	`D -> N (in dbSNP:rs1801334 [NCBI]).`	`VAR_019762`
`VARIANT`	`415 415`	`1`	`T -> N (in PARK2 and PD; impairs the ability to ubiquitinate SNCAIP; does not affect turnover of CDCRE1).`	`VAR_019763`
`VARIANT`	`430 430`	`1`	`G -> D (in PD; early onset).`	`VAR_019764`
`VARIANT`	`431 431`	`1`	`C -> F (in PARK2).`	`VAR_019765`
`VARIANT`	`437 437`	`1`	`P -> L (in PD; early and late onset).`	`VAR_019766`
`VARIANT`	`441 441`	`1`	`C -> R (in PD).`	`VAR_019767`
`MUTAGEN`	`332 332`		`C->S: Impairs folding of IBR domain.`
`MUTAGEN`	`337 337`		`C->A: Impairs the ability to ubiquitinate SNCAIP.`
`MUTAGEN`	`365 365`		`C->S: Impairs protein folding.`
`MUTAGEN`	`418 418`		`C->R: Fails to ubiquitinate SYT11. Does not loose ability to bind SYT11.`
`MUTAGEN`	`421 421`		`C->A: Impairs the ability to ubiquitinate SNCAIP.`
`MUTAGEN`	`431 431`		`C->A: Impairs the ability to ubiquitinate SNCAIP.`
`CONFLICT`	`223 223`		`S -> P (in Ref. 1 and 2).`
`CONFLICT`	`289 290`		`CV -> MI (in Ref. 2; AAM21461).`
`CONFLICT`	`339 339`		`A -> V (in Ref. 5).`
`STRAND`	`2 7`	`6`
`TURN`	`8 10`	`3`
`STRAND`	`11 17`	`7`
`STRAND`	`19 21`	`3`
`HELIX`	`23 33`	`11`
`STRAND`	`38 45`	`8`
`STRAND`	`48 50`	`3`
`TURN`	`52 55`	`4`
`HELIX`	`57 60`	`4`
`STRAND`	`63 70`	`8`
`STRAND`	`318 320`	`3`
`STRAND`	`334 336`	`3`
`STRAND`	`354 356`	`3`
`TURN`	`366 369`	`4`
`STRAND`	`377 379`	`3`

Sequence information

Length: 465 AA [This is the length of the unprocessed precursor]

Molecular weight: 51641 Da [This is the MW of the unprocessed precursor]

CRC64: 9A8BB802A3FC84C3 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MIVFVRFNSS HGFPVEVDSD TSIFQLKEVV AKRQGVPADQ LRVIFAGKEL RNDWTVQNCD 

        70         80         90        100        110        120 
LDQQSIVHIV QRPWRKGQEM NATGGDDPRN AAGGCEREPQ SLTRVDLSSS VLPGDSVGLA 

       130        140        150        160        170        180 
VILHTDSRKD SPPAGSPAGR SIYNSFYVYC KGPCQRVQPG KLRVQCSTCR QATLTLTQGP 

       190        200        210        220        230        240 
SCWDDVLIPN RMSGECQSPH CPGTSAEFFF KCGAHPTSDK ETSVALHLIA TNSRNITCIT 

       250        260        270        280        290        300 
CTDVRSPVLV FQCNSRHVIC LDCFHLYCVT RLNDRQFVHD PQLGYSLPCV AGCPNSLIKE 

       310        320        330        340        350        360 
LHHFRILGEE QYNRYQQYGA EECVLQMGGV LCPRPGCGAG LLPEPDQRKV TCEGGNGLGC 

       370        380        390        400        410        420 
GFAFCRECKE AYHEGECSAV FEASGTTTQA YRVDERAAEQ ARWEAASKET IKKTTKPCPR 

       430        440        450        460 
CHVPVEKNGG CMHMKCPQPQ CRLEWCWNCG CEWNRVCMGD HWFDV

O60260 in FASTA format

View entry in raw text format (no links)
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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools