[1]	PROTEIN SEQUENCE (ISOFORM 5). PubMed=4108501 [NCBI, ExPASy, EBI, Israel, Japan] Carnegie P.R.; "Amino acid sequence of the encephalitogenic basic protein from human myelin."; Biochem. J. 123:57-67(1971).
[2]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 6). TISSUE=Embryonic spinal cord; PubMed=2427738 [NCBI, ExPASy, EBI, Israel, Japan] Roth H.J., Kronquist K.E., Pretorius P.J., Crandall B.F., Campagnoni A.T.; "Isolation and characterization of a cDNA coding for a novel human 17.3K myelin basic protein (MBP) variant."; J. Neurosci. Res. 16:227-238(1986).
[3]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 5). PubMed=2425357 [NCBI, ExPASy, EBI, Israel, Japan] Kamholz J., de Ferra F., Puckett C., Lazzarini R.A.; "Identification of three forms of human myelin basic protein by cDNA cloning."; Proc. Natl. Acad. Sci. U.S.A. 83:4962-4966(1986).
[4]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3; 4; 5 AND 6). TISSUE=Embryonic spinal cord; PubMed=2442403 [NCBI, ExPASy, EBI, Israel, Japan] Roth H.J., Kronquist K.E., de Rosbo N., Crandall B.F., Campagnoni A.T.; "Evidence for the expression of four myelin basic protein variants in the developing human spinal cord through cDNA cloning."; J. Neurosci. Res. 17:321-328(1987).
[5]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 3; 4; 5 AND 6). PubMed=2472816 [NCBI, ExPASy, EBI, Israel, Japan] Streicher R., Stoffel W.; "The organization of the human myelin basic protein gene. Comparison with the mouse gene."; Biol. Chem. Hoppe-Seyler 370:503-510(1989).
[6]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1 AND 2), AND TISSUE SPECIFICITY. TISSUE=Brain; PubMed=7504278 [NCBI, ExPASy, EBI, Israel, Japan] Pribyl T.M., Campagnoni C.W., Kampf K., Kashima T., Handley V.W., McMahon J., Campagnoni A.T.; "The human myelin basic protein gene is included within a 179-kilobase transcription unit: expression in the immune and central nervous systems."; Proc. Natl. Acad. Sci. U.S.A. 90:10695-10699(1993).
[7]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 3), FUNCTION, DIMERIZATION, AND MUTAGENESIS. DOI=10.1016/0161-5890(95)00066-6; PubMed=8544862 [NCBI, ExPASy, EBI, Israel, Japan] Nye S.H., Pelfrey C.M., Burkwit J.J., Voskuhl R.R., Lenardo M.J., Mueller J.P.; "Purification of immunologically active recombinant 21.5 kDa isoform of human myelin basic protein."; Mol. Immunol. 32:1131-1141(1995).
[8]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6). Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.; "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."; Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[9]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 7). TISSUE=Amygdala; The German cDNA consortium; Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
[10]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). TISSUE=Brain; Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno F.R.; Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
[11]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. DOI=10.1038/nature03983; PubMed=16177791 [NCBI, ExPASy, EBI, Israel, Japan] Nusbaum C., Zody M.C., Borowsky M.L., Kamal M., Kodira C.D., Taylor T.D., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Abouelleil A., Allen N.R., Anderson S., Bloom T., Bugalter B., Butler J., Cook A., DeCaprio D., Engels R., Garber M., Gnirke A., Hafez N., Hall J.L., Norman C.H., Itoh T., Jaffe D.B., Kuroki Y., Lehoczky J., Lui A., Macdonald P., Mauceli E., Mikkelsen T.S., Naylor J.W., Nicol R., Nguyen C., Noguchi H., O'Leary S.B., Piqani B., Smith C.L., Talamas J.A., Topham K., Totoki Y., Toyoda A., Wain H.M., Young S.K., Zeng Q., Zimmer A.R., Fujiyama A., Hattori M., Birren B.W., Sakaki Y., Lander E.S.; "DNA sequence and analysis of human chromosome 18."; Nature 437:551-555(2005).
[12]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 5). TISSUE=Brain, Lung, and Skin; 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).
[13]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 135-192. DOI=10.1016/0888-7543(90)90443-X; PubMed=1689270 [NCBI, ExPASy, EBI, Israel, Japan] Boylan K.B., Ayres T.M., Popko B., Takahashi N., Hood L.E., Prusiner S.B.; "Repetitive DNA (TGGA)n 5' to the human myelin basic protein gene: a new form of oligonucleotide repetitive sequence showing length polymorphism."; Genomics 6:16-22(1990).
[14]	PROTEIN SEQUENCE OF 135-178 AND 224-304 (ISOFORM 3), AND MASS SPECTROMETRY. PubMed=2426402 [NCBI, ExPASy, EBI, Israel, Japan] Scoble H.A., Whitaker J.N., Biemann K.; "Analysis of the primary sequence of human myelin basic protein peptides 1-44 and 90-170 by fast atom bombardment mass spectrometry."; J. Neurochem. 47:614-616(1986).
[15]	PROTEIN SEQUENCE OF 148-304 (ISOFORM 5), AND CITRULLINATION OF C8. TISSUE=Brain; PubMed=2466844 [NCBI, ExPASy, EBI, Israel, Japan] Wood D.D., Moscarello M.A.; "The isolation, characterization, and lipid-aggregating properties of a citrulline containing myelin basic protein."; J. Biol. Chem. 264:5121-5127(1989).
[16]	PROTEIN SEQUENCE OF 156-172 AND 302-304, AND CHARACTERIZATION OF C8. TISSUE=Brain; DOI=10.1006/abbi.1995.1449; PubMed=7574672 [NCBI, ExPASy, EBI, Israel, Japan] Boulias C., Pang H., Mastronardi F., Moscarello M.A.; "The isolation and characterization of four myelin basic proteins from the unbound fraction during CM52 chromatography."; Arch. Biochem. Biophys. 322:174-182(1995).
[17]	PROTEIN SEQUENCE OF 179-223 (ISOFORM 5), AND MASS SPECTROMETRY. PubMed=6201481 [NCBI, ExPASy, EBI, Israel, Japan] Gibson B.W., Gilliom R.D., Whitaker J.N., Biemann K.; "Amino acid sequence of human myelin basic protein peptide 45-89 as determined by mass spectrometry."; J. Biol. Chem. 259:5028-5031(1984).
[18]	PROTEIN SEQUENCE OF 179-222 (ISOFORM 5), AND SEQUENCE REVISION. Shapira R., McKneally S.S., Chou F., Kibler R.F.; "Encephalitogenic fragment of myelin basic protein. Amino acid sequence of bovine, rabbit, guinea pig, monkey, and human fragments."; J. Biol. Chem. 246:4630-4640(1971).
[19]	PROTEIN SEQUENCE OF 246-269 (ISOFORM 3), AND ENCEPHALITOGENIC PEPTIDE. PubMed=4099924 [NCBI, ExPASy, EBI, Israel, Japan] Lennon V.A., Wilks A.V., Carnegie P.R.; "Immunologic properties of the main encephalitogenic peptide from the basic protein of human myelin."; J. Immunol. 105:1223-1230(1970).
[20]	PARTIAL PROTEIN SEQUENCE. TISSUE=Brain; DOI=10.1006/bbrc.1993.1540; PubMed=7685161 [NCBI, ExPASy, EBI, Israel, Japan] Proost P., Van Damme J., Opdenakker G.; "Leukocyte gelatinase B cleavage releases encephalitogens from human myelin basic protein."; Biochem. Biophys. Res. Commun. 192:1175-1181(1993).
[21]	METHYLATION AT ARG-241. PubMed=5128665 [NCBI, ExPASy, EBI, Israel, Japan] Baldwin G.S., Carnegie P.R.; "Isolation and partial characterization of methylated arginines from the encephalitogenic basic protein of myelin."; Biochem. J. 123:69-74(1971).
[22]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-96, AND MASS SPECTROMETRY. TISSUE=Epithelium; DOI=10.1016/j.cell.2006.09.026; PubMed=17081983 [NCBI, ExPASy, EBI, Israel, Japan] Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."; Cell 127:635-648(2006).
[23]	STRUCTURE BY NMR OF 135-148, AND ACETYLATION. PubMed=7544282 [NCBI, ExPASy, EBI, Israel, Japan] Mendz G.L., Barden J.A., Martenson R.E.; "Conformation of a tetradecapeptide epitope of myelin basic protein."; Eur. J. Biochem. 231:659-666(1995).
[24]	3D-STRUCTURE MODELING OF 135-279 (ISOFORM 5). DOI=10.1074/jbc.272.7.4269; PubMed=9020143 [NCBI, ExPASy, EBI, Israel, Japan] Ridsdale R.A., Beniac D.R., Tompkins T.A., Moscarello M.A., Harauz G.; "Three-dimensional structure of myelin basic protein. II. Molecular modeling and considerations of predicted structures in multiple sclerosis."; J. Biol. Chem. 272:4269-4275(1997).
[25]	X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 218-237 IN COMPLEX WITH HLA-DRA; HLA-DRB1 AND TCRB. DOI=10.1006/jmbi.2000.4198; PubMed=11080454 [NCBI, ExPASy, EBI, Israel, Japan] Li Y., Li H., Martin R., Mariuzza R.A.; "Structural basis for the binding of an immunodominant peptide from myelin basic protein in different registers by two HLA-DR2 proteins."; J. Mol. Biol. 304:177-188(2000).
[26]	X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 45-57 IN COMPLEX WITH HLA-DRA AND HLA-DRB1. DOI=10.1038/sj.emboj.7600771; PubMed=16079912 [NCBI, ExPASy, EBI, Israel, Japan] Li Y., Huang Y., Lue J., Quandt J.A., Martin R., Mariuzza R.A.; "Structure of a human autoimmune TCR bound to a myelin basic protein self-peptide and a multiple sclerosis-associated MHC class II molecule."; EMBO J. 24:2968-2979(2005).

Comments

FUNCTION: The classic group of MBP isoforms (isoform 4-isoform 14) are with PLP the most abundant protein components of the myelin membrane in the CNS. They have a role in both its formation and stabilization. The smaller isoforms might have an important role in remyelination of denuded axons in multiple sclerosis. The non-classic group of MBP isoforms (isoform 1-isoform 3/Golli-MBPs) may preferentially have a role in the early developing brain long before myelination, maybe as components of transcriptional complexes, and may also be involved in signaling pathways in T-cells and neural cells. Differential splicing events combined with optional post-translational modifications give a wide spectrum of isomers, with each of them potentially having a specialized function. Induces T-cell proliferation.
SUBUNIT: Homodimer; isoform 3 exists as a homodimer.
SUBCELLULAR LOCATION: Myelin membrane; Peripheral membrane protein; Cytoplasmic side. Note=Cytoplasmic side of myelin.

ALTERNATIVE PRODUCTS: 7 named isoforms [FASTA] produced by alternative splicing. Additional isoforms seem to exist.

Name	1
Synonyms	Golli-MBP1, HOG7
Isoform ID	P02686-1
This is the isoform sequence displayed in this entry.

Name	2
Synonyms	Golli-MBP2, HOG5
Isoform ID	P02686-2
Features which should be applied to build the isoform sequence: VSP_003311.

Name	3
Synonyms	MBP1, 21.5 kDa
Isoform ID	P02686-3
Note: Met-1 is removed. Contains N-acetylalanine at position 2. Mutagenesis of Cys-81 to Ser prevents dimerization.
Features which should be applied to build the isoform sequence: VSP_003308, VSP_003309.

Name	4
Synonyms	MBP2, 20.2 kDa
Isoform ID	P02686-4
Note: Met-1 is removed. Contains N-acetylalanine at position 2.
Features which should be applied to build the isoform sequence: VSP_003308, VSP_003309, VSP_003310.

Name	5
Synonyms	MBP3, 18.5 kDa
Isoform ID	P02686-5
Note: Met-1 is removed. Contains N-acetylalanine at position 2.
Features which should be applied to build the isoform sequence: VSP_003308.

Name	6
Synonyms	MBP4, 17.2 kDa
Isoform ID	P02686-6
Note: Met-1 is removed. Contains N-acetylalanine at position 2.
Features which should be applied to build the isoform sequence: VSP_003308, VSP_003310.

Name	7
Isoform ID	P02686-7
Features which should be applied to build the isoform sequence: VSP_003308, VSP_019259, VSP_019260.

TISSUE SPECIFICITY: MBP isoforms are found in both the central and the peripheral nervous system, whereas Golli-MBP isoforms are expressed in fetal thymus, spleen and spinal cord, as well as in cell lines derived from the immune system.
DEVELOPMENTAL STAGE: Expression begins abruptly in 14-16 week old fetuses. Even smaller isoforms seem to be produced during embryogenesis; some of these persisting in the adult. Expression of isoform MBP2 is more evident at 16 weeks and its relative proportion declines thereafter.
PTM: Several charge isomers of MBP; C1 (the most cationic, least modified, and most abundant form), C2, C3, C4, C5, C6, C7, C8-A and C8-B (the least cationic form); are produced as a result of optional PTM, such as phosphorylation, deamidation of glutamine or asparagine, arginine citrullination and methylation. C8-A and C8-B contain each two mass isoforms termed C8-A(H), C8-A(L), C8-B(H) and C8-B(L), (H) standing for higher and (L) for lower molecular weight. C3, C4 and C5 are phosphorylated. The ratio of methylated arginine residues decreases during aging, making the protein more cationic.
PTM: The N-terminal alanine is acetylated (isoform 3, isoform 4, isoform 5 and isoform 6).
PTM: Arg-241 was found to be 6% monomethylated and 60% symmetrically dimethylated.
DISEASE: The reduction in the surface charge of citrullinated and/or methylated MBP could result in a weakened attachment to the myelin membrane. This mechanism could be operative in demyelinating diseases such as chronical multiple sclerosis (MS), and fulminating MS (Marburg disease).
SIMILARITY: Belongs to the myelin basic protein family.
SEQUENCE CAUTION:
- Sequence=AAC41944.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. The C-terminus contains a Histidine tag
WEB RESOURCE: Name=Wikipedia; Note=Myelin basic protein entry; URL="http://en.wikipedia.org/wiki/Myelin_basic_protein";.

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

M30047; AAA59559.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M20009; AAA59561.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M13577; AAA59562.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M30516; AAA59563.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M30515; AAA59564.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X17286; CAA35179.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X17287; CAA35179.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X17290; CAA35179.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X17288; CAA35179.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X17369; CAA35179.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X17289; CAA35179.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
L18862; AAA72008.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
L18864; AAA72009.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
L18865; AAA72010.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
L18866; AAA72011.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
L41657; AAC41944.1; ALT_SEQ; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
CR536534; CAG38771.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
CR541919; CAG46717.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
CR627018; CAH10359.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AB208986; BAD92223.1; ALT_INIT; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AC093330; -; NOT_ANNOTATED_CDS; Genomic_DNA.	[EMBL / GenBank / DDBJ]
BC008749; AAH08749.3; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC065248; AAH65248.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC080654; AAH80654.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC101771; AAI01772.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC101773; AAI01774.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M63599; AAA59560.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A49635; A49635.
S10482; MBHUB.

RefSeq

NP_001020252.1; -.
NP_001020263.1; -.
NP_001020271.1; -.
NP_001020272.1; -.
NP_002376.1; -.

UniGene

Hs.551713

3D structure databases

PDB

1BX2; X-ray; 2.60 A; C/F=217-231.	[ExPASy / RCSB / EBI]
1FV1; X-ray; 1.90 A; C/F=218-237.	[ExPASy / RCSB / EBI]
1HQR; X-ray; 3.20 A; C=221-233.	[ExPASy / RCSB / EBI]
1QCL; Model; -; A=135-304.	[ExPASy / RCSB / EBI]
1YMM; X-ray; 3.50 A; C=217-238.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1BX2; -.
1FV1; -.
1HQR; -.
1QCL; -.
1YMM; -.

DisProt

DP00236; -.

ModBase

P02686.

Protein-protein interaction databases

IntAct

P02686; -.

PTM databases

PhosphoSite

P02686; -.

Organism-specific databases

HIX0014534; -.

HGNC:6925; MBP.

MBP.

CAB002300; -.

159430; gene. [NCBI / EBI]

PharmGKB

PA24759; -.

GeneCards

P02686.

Gene expression databases

ArrayExpress

P02686; -.

CleanEx

HS_MBP; -.

GermOnline

ENSG00000197971; Homo sapiens.

Ontologies

GO:0043209;	Cellular component: myelin sheath (inferred from electronic annotation from UniProtKB-SubCell).
GO:0019911;	Molecular function: structural constituent of myelin sheath (inferred from electronic annotation from InterPro).
GO:0008366;	Biological process: axon ensheathment (traceable author statement from ProtInc).
GO:0007417;	Biological process: central nervous system development (traceable author statement from ProtInc).
GO:0006955;	Biological process: immune response (traceable author statement from ProtInc).
GO:0007268;	Biological process: synaptic transmission (traceable author statement from ProtInc).
QuickGo view.

Family and domain databases

InterPro

IPR000548; Myelin_BP.
Graphical view of domain structure.

PANTHER

PTHR11429; Myelin_BP; 1.

Pfam

PF01669; Myelin_MBP; 1.
Pfam graphical view of domain structure.

PRINTS

PR00212; MYELINMBP.

ProDom

PD004542; Myelin_BP; 1.
[Domain structure / List of seq. sharing at least 1 domain]

PROSITE

PS00569; MYELIN_MBP; 1.

ProtoNet

P02686.

Genome annotation databases

Ensembl

ENSG00000197971; Homo sapiens. [Contig view]

GeneID

4155; -.

KEGG

hsa:4155; -.

Phylogenomic databases

HOVERGEN

P02686; -.

Other

P02686; -.

16362; -.

MBP; Homo sapiens.

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

Keywords

3D-structure; Acetylation; Alternative splicing; Autoimmune encephalomyelitis; Cell membrane; Citrullination; Direct protein sequencing; Membrane; Methylation; Phosphoprotein.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 304`	`304`	`Myelin basic protein.`	`PRO_0000158990`
`REGION`	`179 222`	`44`	`Induces experimental autoimmune encephalomyelitis (EAE) 1.`
`REGION`	`246 256`	`11`	`Induces experimental autoimmune encephalomyelitis (EAE) 2.`
`MOD_RES`	`96 96`		`Phosphoserine.`
`MOD_RES`	`141 141`		`Phosphoserine (By similarity).`
`MOD_RES`	`146 146`		`Phosphoserine (By similarity).`
`MOD_RES`	`159 159`		`Citrulline; in form C8.`
`MOD_RES`	`165 165`		`Citrulline; in form C8.`
`MOD_RES`	`169 169`		`Phosphothreonine (By similarity).`
`MOD_RES`	`174 174`		`Phosphoserine (By similarity).`
`MOD_RES`	`203 203`		`Phosphotyrosine (By similarity).`
`MOD_RES`	`205 205`		`Phosphoserine (By similarity).`
`MOD_RES`	`229 229`		`Phosphothreonine (By similarity).`
`MOD_RES`	`232 232`		`Phosphothreonine (By similarity).`
`MOD_RES`	`237 237`		`Deamidated glutamine (By similarity).`
`MOD_RES`	`241 241`		`Omega-N-methylarginine; alternate.`
`MOD_RES`	`241 241`		`Symmetric dimethylarginine; alternate.`
`MOD_RES`	`249 249`		`Phosphoserine (By similarity).`
`MOD_RES`	`256 256`		`Citrulline; in form C8.`
`MOD_RES`	`264 264`		`Citrulline; in form C8.`
`MOD_RES`	`281 281`		`Deamidated glutamine (By similarity).`
`MOD_RES`	`293 293`		`Citrulline; in form C8.`
`MOD_RES`	`295 295`		`Phosphoserine (By similarity).`
`MOD_RES`	`299 299`		`Phosphoserine (By similarity).`
`MOD_RES`	`304 304`		`Citrulline; in form C8.`
`VAR_SEQ`	`1 133`		`Missing (in isoform 3, isoform 4, isoform 5, isoform 6 and isoform 7).`	`VSP_003308`
`VAR_SEQ`	`161 203`		`Missing (in isoform 7).`	`VSP_019259`
`VAR_SEQ`	`192 192`		`K -> KVPWLKPGRSPLPSHARSQPGLCNMYK (in isoform 3 and isoform 4).`	`VSP_003309`
`VAR_SEQ`	`193 304`		`DSHHPARTAHYGSLPQKSHGRTQDENPVVHFFKNIVTPRT` `PPPSQGKGRGLSLSRFSWGAEGQRPGFGYGGRASDYKSAH` `KGFKGVDAQGTLSKIFKLGGRDSRSGSPMARR -> VSSEE (in isoform 2).`	`VSP_003311`
`VAR_SEQ`	`240 250`		`Missing (in isoform 4 and isoform 6).`	`VSP_003310`
`VAR_SEQ`	`251 304`		`Missing (in isoform 7).`	`VSP_019260`
`CONFLICT`	`300 300`		`P -> T (in Ref. 8; CAG38771).`
`STRAND`	`146 154`	`9`
`STRAND`	`160 162`	`3`
`STRAND`	`173 179`	`7`
`STRAND`	`241 248`	`8`
`STRAND`	`284 289`	`6`

Sequence information

Length: 304 AA [This is the length of the unprocessed precursor]

Molecular weight: 33117 Da [This is the MW of the unprocessed precursor]

CRC64: 4AD7305C1D5434C4 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MGNHAGKREL NAEKASTNSE TNRGESEKKR NLGELSRTTS EDNEVFGEAD ANQNNGTSSQ 

        70         80         90        100        110        120 
DTAVTDSKRT ADPKNAWQDA HPADPGSRPH LIRLFSRDAP GREDNTFKDR PSESDELQTI 

       130        140        150        160        170        180 
QEDSAATSES LDVMASQKRP SQRHGSKYLA TASTMDHARH GFLPRHRDTG ILDSIGRFFG 

       190        200        210        220        230        240 
GDRGAPKRGS GKDSHHPART AHYGSLPQKS HGRTQDENPV VHFFKNIVTP RTPPPSQGKG 

       250        260        270        280        290        300 
RGLSLSRFSW GAEGQRPGFG YGGRASDYKS AHKGFKGVDA QGTLSKIFKL GGRDSRSGSP 


MARR

P02686 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	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