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UniProtKB/Swiss-Prot entry Q96RR4


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name KKCC2_HUMAN
Primary accession number Q96RR4
Secondary accession numbers A8K7Q7 O94883 Q8IUG2 Q8IUG3 Q8N3I4 Q8WY03 Q8WY04 Q8WY05 Q8WY06 Q96RP1 Q96RP2 Q96RR3 Q9BWE9 Q9UER3 Q9UES2 Q9Y5N2
Integrated into Swiss-Prot on December 7, 2004
Sequence was last modified on December 1, 2001 (Sequence version 1)
Annotations were last modified on    June 16, 2009 (Entry version 71)
Name and origin of the protein
Protein name Calcium/calmodulin-dependent protein kinase kinase 2
Synonyms EC 2.7.11.17
Calcium/calmodulin-dependent protein kinase kinase beta
CaM-kinase kinase beta
CaM-KK beta
CaMKK beta
Gene name
Name: CAMKK2
Synonyms: CAMKKB, KIAA0787
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1; 2; 3; 4; 5 AND 6), FUNCTION, AND VARIANT THR-85.
DOI=10.1074/jbc.M011720200; PubMed=11395482 [NCBI, ExPASy, EBI, Israel, Japan]
Hsu L.-S., Chen G.-D., Lee L.-S., Chi C.-W., Cheng J.-F., Chen J.-Y.;
"Human Ca2+/calmodulin-dependent protein kinase kinase beta gene encodes multiple isoforms that display distinct kinase activity.";
J. Biol. Chem. 276:31113-31123(2001).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT THR-85.
TISSUE=Brain cortex;
DOI=10.1074/jbc.273.48.31880; PubMed=9822657 [NCBI, ExPASy, EBI, Israel, Japan]
Anderson K.A., Means R.L., Huang Q.-H., Kemp B.E., Goldstein E.G., Selbert M.A., Edelman A.M., Fremeau R.T., Means A.R.;
"Components of a calmodulin-dependent protein kinase cascade. Molecular cloning, functional characterization and cellular localization of Ca2+/calmodulin-dependent protein kinase kinase beta.";
J. Biol. Chem. 273:31880-31889(1998).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION IN PHOSPHORYLATION OF CAMK1D, AND VARIANT THR-85.
DOI=10.1016/S0014-5793(03)00817-2; PubMed=12935886 [NCBI, ExPASy, EBI, Israel, Japan]
Ishikawa Y., Tokumitsu H., Inuzuka H., Murata-Hori M., Hosoya H., Kobayashi R.;
"Identification and characterization of novel components of a Ca2+/calmodulin-dependent protein kinase cascade in HeLa cells.";
FEBS Lett. 550:57-63(2003).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 7).
TISSUE=Brain;
DOI=10.1093/dnares/5.5.277; PubMed=9872452 [NCBI, ExPASy, EBI, Israel, Japan]
Nagase T., Ishikawa K., Suyama M., Kikuno R., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. XI. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro.";
DNA Res. 5:277-286(1998).
[5]
SEQUENCE REVISION.
DOI=10.1093/dnares/9.3.99; PubMed=12168954 [NCBI, ExPASy, EBI, Israel, Japan]
Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
"Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones.";
DNA Res. 9:99-106(2002).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANT THR-85.
TISSUE=Stomach;
DOI=10.1038/ng1285; PubMed=14702039 [NCBI, ExPASy, EBI, Israel, Japan]
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human cDNAs.";
Nat. Genet. 36:40-45(2004).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 233-588 (ISOFORM 5).
TISSUE=Placenta;
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).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 117-588 (ISOFORM 2), FUNCTION IN PHOSPHORYLATION OF CAMK1, AND TISSUE SPECIFICITY.
DOI=10.1159/000025324; PubMed=9662074 [NCBI, ExPASy, EBI, Israel, Japan]
Hsu L.-S., Tsou A.-P., Chi C.-W., Lee C.-H., Chen J.-Y.;
"Cloning, expression and chromosomal localization of human Ca2+/calmodulin-dependent protein kinase kinase.";
J. Biomed. Sci. 5:141-149(1998).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 254-588 (ISOFORM 7).
TISSUE=Amygdala;
DOI=10.1186/1471-2164-8-399; PubMed=17974005 [NCBI, ExPASy, EBI, Israel, Japan]
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Blocker H., Heubner D., Hoerlein A., Michel G., Wedler H., Kohrer K., Ottenwalder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 338-533 (ISOFORM 2).
Barrow I.K.-P., Boguski M.S., Touchman J.W., Spencer F.;
"Full-insert sequence of mapped XREF EST.";
Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-495 AND SER-511, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-522 (ISOFORM 3), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-479 (ISOFORM 5), AND MASS SPECTROMETRY.
DOI=10.1016/j.molcel.2008.07.007; PubMed=18691976 [NCBI, ExPASy, EBI, Israel, Japan]
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[12]
VARIANTS [LARGE SCALE ANALYSIS] ASN-10; THR-85; TYR-123; LEU-127; THR-182 AND HIS-492.
DOI=10.1038/nature05610; PubMed=17344846 [NCBI, ExPASy, EBI, Israel, Japan]
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G., Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.;
"Patterns of somatic mutation in human cancer genomes.";
Nature 446:153-158(2007).
Comments
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
AB081337; BAC19841.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF287630; AAK64600.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF287631; AAK64601.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF321385; AAL37215.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF321386; AAL37216.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF321387; AAL37217.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF321388; AAL37218.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF321401; AAK91830.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF321390; AAK91830.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF321391; AAK91830.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF321392; AAK91830.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF321393; AAK91830.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF321394; AAK91830.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF321395; AAK91830.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF321396; AAK91830.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF321397; AAK91830.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF321398; AAK91830.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF321399; AAK91830.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF321400; AAK91830.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF321575; AAK91830.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF321576; AAK91830.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF321577; AAK91830.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF321578; AAK91830.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF321402; AAK91829.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF321390; AAK91829.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF321391; AAK91829.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF321392; AAK91829.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF321393; AAK91829.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF321394; AAK91829.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF321395; AAK91829.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF321396; AAK91829.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF321397; AAK91829.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF321398; AAK91829.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF321399; AAK91829.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF321400; AAK91829.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF321575; AAK91829.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF321576; AAK91829.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF321577; AAK91829.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF321578; AAK91829.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF140507; AAD31507.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AB081336; BAC19840.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AB018330; BAA34507.2; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK292072; BAF84761.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC000318; AAH00318.2; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC026060; AAH26060.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF101264; AAD04566.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL834322; CAD38990.1; ALT_SEQ; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF091074; AAC72943.1; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00170509; -.
IPI00172426; -.
IPI00172500; -.
IPI00172501; -.
IPI00290239; -.
IPI00292156; -.
IPI00479420; -.
PIR JE0191; JE0191.
RefSeq NP_006540.3; -.
NP_705719.2; -.
NP_705720.1; -.
NP_757363.1; -.
NP_757364.1; -.
NP_757365.1; -.
NP_757380.1; -.
UniGene Hs.297343
3D structure databases
HSSP O14965; 1OL6. [HSSP ENTRY / PDB]
ModBase Q96RR4.
Protein-protein interaction databases
IntAct Q96RR4; 5.
PTM databases
PhosphoSite Q96RR4; -.
Enzyme and pathway databases
BRENDA 2.7.11.17; 247.
Organism-specific databases
GeneCards GC12M120138; -.
H-InvDB HIX0011079; -.
HGNC HGNC:1470; CAMKK2.
GenAtlas CAMKK2.
HPA HPA017389; -.
PharmGKB PA26052; -.
HUGE KIAA0787.
Gene expression databases
ArrayExpress Q96RR4; -.
Bgee Q96RR4; -.
CleanEx HS_CAMKK2; -.
GermOnline ENSG00000110931; Homo sapiens.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-SubCell).
GO:0005524; Molecular function: ATP binding (inferred from electronic annotation from UniProtKB-KW).
GO:0005509; Molecular function: calcium ion binding (inferred from direct assay from UniProtKB).
GO:0005516; Molecular function: calmodulin binding (traceable author statement from UniProtKB).
GO:0004683; Molecular function: calmodulin-dependent protein kinase activity (inferred from electronic annotation from EC).
GO:0004713; Molecular function: protein tyrosine kinase activity (traceable author statement from UniProtKB).
GO:0019722; Biological process: calcium-mediated signaling (traceable author statement from UniProtKB).
GO:0000165; Biological process: MAPKKK cascade (traceable author statement from UniProtKB).
GO:0045941; Biological process: positive regulation of transcription (traceable author statement from UniProtKB).
GO:0046777; Biological process: protein amino acid autophosphorylation (inferred from direct assay from UniProtKB).
GO:0045859; Biological process: regulation of protein kinase activity (traceable author statement from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR000719; Prot_kinase_core.
IPR017441; Protein_kinase_ATP_BS.
IPR017442; Se/Thr_pkinase-rel.
IPR008271; Ser_thr_pkin_AS.
IPR002290; Ser_thr_pkinase.
Graphical view of domain structure.
Pfam PF00069; Pkinase; 1.
Pfam graphical view of domain structure.
ProDom PD000001; Prot_kinase; 1.
[Domain structure / List of seq. sharing at least 1 domain]
SMART SM00220; S_TKc; 1.
SMART graphical view of domain structure.
PROSITE PS00107; PROTEIN_KINASE_ATP; 1.
PS50011; PROTEIN_KINASE_DOM; 1.
PS00108; PROTEIN_KINASE_ST; 1.
PROSITE graphical view of domain structure (profiles).
Proteomic databases
PRIDE Q96RR4; -.
Genome annotation databases
Ensembl ENSG00000110931; Homo sapiens. [Contig view]
GeneID 10645; -.
KEGG hsa:10645; -.
Phylogenomic databases
HOVERGEN Q96RR4; -.
Other
NextBio 40461; -.
ProtoNet Q96RR4.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Alternative splicing; ATP-binding; Calmodulin-binding; Cytoplasm; Kinase; Nucleotide-binding; Phosphoprotein; Polymorphism; Serine/threonine-protein kinase; Transferase.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   588  588     Calcium/calmodulin-dependent protein kinase kinase 2. PRO_0000086144
DOMAIN   165   446  282     Protein kinase. 
NP_BIND   171   179  9     ATP (By similarity). 
REGION   204   226  23     RP domain. 
REGION   472   477  6     Autoinhibitory domain (By similarity). 
REGION   475   500  26     Calmodulin-binding (By similarity). 
ACT_SITE   312   312        Proton acceptor (By similarity). 
BINDING   194   194        ATP (By similarity). 
MOD_RES   129   129        Phosphoserine (By similarity). 
MOD_RES   133   133        Phosphoserine (By similarity). 
MOD_RES   495   495        Phosphoserine. 
MOD_RES   511   511        Phosphoserine. 
VAR_SEQ   442   484        Missing (in isoform 4, isoform 5 and isoform 6). VSP_012142
VAR_SEQ   520   532        KPTRECESLSELK -> QGSEDNLQGTDPP (in isoform 3 and isoform 5). VSP_012143
VAR_SEQ   533   554        EARQRRQPPGHRPAPRGGGGSA -> GTKKKKGLDSMTSTVAAGWLDRRV (in isoform 7). VSP_012148
VAR_SEQ   533   541        EARQRRQPP -> PVGEEEVLL (in isoform 3 and isoform 5). VSP_012144
VAR_SEQ   533   533        E -> T (in isoform 2 and isoform 6). VSP_012146
VAR_SEQ   534   554        Missing (in isoform 2 and isoform 6). VSP_012147
VAR_SEQ   542   554        Missing (in isoform 3 and isoform 5). VSP_012145
VAR_SEQ   555   588        Missing (in isoform 2, isoform 3, isoform 5, isoform 6 and isoform 7). VSP_012149
VARIANT   10    10  1     S -> N (in dbSNP:rs28360477 [NCBI]). VAR_032788 
VARIANT   85    85  1     S -> T (in dbSNP:rs3817190 [NCBI]). VAR_020532 
VARIANT   123   123  1     C -> Y. VAR_040610 
VARIANT   127   127  1     P -> L (in a lung neuroendocrine carcinoma sample; somatic mutation). VAR_040611 
VARIANT   182   182  1     A -> T (in a colorectal adenocarcinoma sample; somatic mutation). VAR_040612 
VARIANT   363   363  1     R -> C (in dbSNP:rs1132780 [NCBI]). VAR_020533 
VARIANT   492   492  1     R -> H. VAR_040613 
CONFLICT   206   206        G -> A (in Ref. 2; AAD31507). 
CONFLICT   331   331        F -> I (in Ref. 6; BAF84761). 
CONFLICT   347   347        T -> Y (in Ref. 2; AAD31507). 
CONFLICT   371   371        L -> K (in Ref. 2; AAD31507). 
CONFLICT   554   554        A -> H (in Ref. 1; AAK91829). 
CONFLICT   557   557        R -> N (in Ref. 1; AAK91829). 
Sequence information
Length: 588 AA [This is the length of the unprocessed precursor] Molecular weight: 64732 Da [This is the MW of the unprocessed precursor] CRC64: D4C4583561341166 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSSCVSSQPS SNRAAPQDEL GGRGSSSSES QKPCEALRGL SSLSIHLGME SFIVVTECEP 

        70         80         90        100        110        120 
GCAVDLGLAR DRPLEADGQE VPLDSSGSQA RPHLSGRKLS LQERSQGGLA AGGSLDMNGR 

       130        140        150        160        170        180 
CICPSLPYSP VSSPQSSPRL PRRPTVESHH VSITGMQDCV QLNQYTLKDE IGKGSYGVVK 

       190        200        210        220        230        240 
LAYNENDNTY YAMKVLSKKK LIRQAGFPRR PPPRGTRPAP GGCIQPRGPI EQVYQEIAIL 

       250        260        270        280        290        300 
KKLDHPNVVK LVEVLDDPNE DHLYMVFELV NQGPVMEVPT LKPLSEDQAR FYFQDLIKGI 

       310        320        330        340        350        360 
EYLHYQKIIH RDIKPSNLLV GEDGHIKIAD FGVSNEFKGS DALLSNTVGT PAFMAPESLS 

       370        380        390        400        410        420 
ETRKIFSGKA LDVWAMGVTL YCFVFGQCPF MDERIMCLHS KIKSQALEFP DQPDIAEDLK 

       430        440        450        460        470        480 
DLITRMLDKN PESRIVVPEI KLHPWVTRHG AEPLPSEDEN CTLVEVTEEE VENSVKHIPS 

       490        500        510        520        530        540 
LATVILVKTM IRKRSFGNPF EGSRREERSL SAPGNLLTKK PTRECESLSE LKEARQRRQP 

       550        560        570        580 
PGHRPAPRGG GGSALVRGSP CVESCWAPAP GSPARMHPLR PEEAMEPE 

Q96RR4 in FASTA format

View entry in raw text format (no links)
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BLAST logo BLAST submission on ExPASy/SIB
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Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
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