GPM6B_HUMAN
ID GPM6B_HUMAN Reviewed; 265 AA.
AC Q13491; O76077; Q86X43; Q8N956;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2002, sequence version 2.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Neuronal membrane glycoprotein M6-b;
DE Short=M6b;
GN Name=GPM6B; Synonyms=M6B;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Spinal cord;
RX PubMed=8661015; DOI=10.1006/geno.1996.0231;
RA Olinsky S., Loop B.T., Dekosky A., Ripepi B., Weng W., Cummins J.,
RA Wenger S.L., Yan Y., Lagenaur C., Narayanan V.;
RT "Chromosomal mapping of the human M6 genes.";
RL Genomics 33:532-536(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1 AND 2).
RX PubMed=9674909;
RX DOI=10.1002/(sici)1096-8628(19980630)78:2<165::aid-ajmg13>3.0.co;2-l;
RA Narayanan V., Olinsky S.L., Dahle E., Naidu S., Zoghbi H.Y.;
RT "Mutation analysis of the M6b gene in patients with Rett syndrome.";
RL Am. J. Med. Genet. 78:165-168(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Xia J.-H., Liu C.-Y., Ruan Q.-G., Fu J.-J., Deng H.-X.;
RT "Cloning of human full-length m6b1 gene.";
RL Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
RA Liu C.-Y., Cui F., Fu J.-J., Xia J.-H.;
RT "Molecular cloning of a splicing form of M6b.";
RL Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC TISSUE=Brain;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP INTERACTION WITH SERT.
RX PubMed=18581270; DOI=10.1007/s12031-008-9092-4;
RA Fjorback A.W., Muller H.K., Wiborg O.;
RT "Membrane glycoprotein M6B interacts with the human serotonin
RT transporter.";
RL J. Mol. Neurosci. 37:191-200(2009).
RN [10]
RP FUNCTION.
RX PubMed=21638316; DOI=10.1002/jbmr.435;
RA Drabek K., van de Peppel J., Eijken M., van Leeuwen J.P.;
RT "GPM6B regulates osteoblast function and induction of mineralization by
RT controlling cytoskeleton and matrix vesicle release.";
RL J. Bone Miner. Res. 26:2045-2051(2011).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-318 (ISOFORM 4), AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
CC -!- FUNCTION: May be involved in neural development. Involved in regulation
CC of osteoblast function and bone formation. Involved in matrix vesicle
CC release by osteoblasts; this function seems to involve maintenance of
CC the actin cytoskeleton. May be involved in cellular trafficking of SERT
CC and thereby in regulation of serotonin uptake.
CC {ECO:0000269|PubMed:21638316}.
CC -!- SUBUNIT: Interacts with SERT. {ECO:0000269|PubMed:18581270}.
CC -!- INTERACTION:
CC Q13491-3; Q9Y282: ERGIC3; NbExp=3; IntAct=EBI-11992640, EBI-781551;
CC Q13491-3; Q16623: STX1A; NbExp=3; IntAct=EBI-11992640, EBI-712466;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}. Note=Colocalizes with SERT at the plasma
CC membrane. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=A;
CC IsoId=Q13491-1; Sequence=Displayed;
CC Name=2; Synonyms=B;
CC IsoId=Q13491-2; Sequence=VSP_003326;
CC Name=3;
CC IsoId=Q13491-3; Sequence=VSP_041121;
CC Name=4;
CC IsoId=Q13491-4; Sequence=VSP_041121, VSP_043247;
CC -!- TISSUE SPECIFICITY: Neurons and glia; cerebellar Bergmann glia, in glia
CC within white matter tracts of the cerebellum and cerebrum, and in
CC embryonic dorsal root ganglia.
CC -!- SIMILARITY: Belongs to the myelin proteolipid protein family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB16888.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAC19165.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; U45955; AAB16888.1; ALT_INIT; mRNA.
DR EMBL; AF037347; AAC19165.1; ALT_INIT; Genomic_DNA.
DR EMBL; AF037341; AAC19165.1; JOINED; Genomic_DNA.
DR EMBL; AF037342; AAC19165.1; JOINED; Genomic_DNA.
DR EMBL; AF037343; AAC19165.1; JOINED; Genomic_DNA.
DR EMBL; AF037344; AAC19165.1; JOINED; Genomic_DNA.
DR EMBL; AF037345; AAC19165.1; JOINED; Genomic_DNA.
DR EMBL; AF037346; AAC19165.1; JOINED; Genomic_DNA.
DR EMBL; AF037347; AAC19166.1; -; Genomic_DNA.
DR EMBL; AF037340; AAC19166.1; JOINED; Genomic_DNA.
DR EMBL; AF037342; AAC19166.1; JOINED; Genomic_DNA.
DR EMBL; AF037343; AAC19166.1; JOINED; Genomic_DNA.
DR EMBL; AF037344; AAC19166.1; JOINED; Genomic_DNA.
DR EMBL; AF037345; AAC19166.1; JOINED; Genomic_DNA.
DR EMBL; AF037346; AAC19166.1; JOINED; Genomic_DNA.
DR EMBL; AF016004; AAC28560.1; -; mRNA.
DR EMBL; AF047197; AAD13718.1; -; Genomic_DNA.
DR EMBL; AF047191; AAD13718.1; JOINED; Genomic_DNA.
DR EMBL; AF047192; AAD13718.1; JOINED; Genomic_DNA.
DR EMBL; AF047193; AAD13718.1; JOINED; Genomic_DNA.
DR EMBL; AF047194; AAD13718.1; JOINED; Genomic_DNA.
DR EMBL; AF047195; AAD13718.1; JOINED; Genomic_DNA.
DR EMBL; AF047196; AAD13718.1; JOINED; Genomic_DNA.
DR EMBL; AK095657; BAC04600.1; -; mRNA.
DR EMBL; AC003035; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC003037; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471074; EAW98845.1; -; Genomic_DNA.
DR EMBL; CH471074; EAW98846.1; -; Genomic_DNA.
DR EMBL; BC008151; AAH08151.1; -; mRNA.
DR EMBL; BC047295; AAH47295.1; -; mRNA.
DR CCDS; CCDS14158.1; -. [Q13491-1]
DR CCDS; CCDS35206.1; -. [Q13491-4]
DR CCDS; CCDS35207.1; -. [Q13491-3]
DR CCDS; CCDS48084.1; -. [Q13491-2]
DR RefSeq; NP_001001994.1; NM_001001994.2. [Q13491-2]
DR RefSeq; NP_001001995.1; NM_001001995.2. [Q13491-4]
DR RefSeq; NP_001001996.1; NM_001001996.2. [Q13491-3]
DR RefSeq; NP_005269.1; NM_005278.4. [Q13491-1]
DR AlphaFoldDB; Q13491; -.
DR SMR; Q13491; -.
DR BioGRID; 109085; 26.
DR IntAct; Q13491; 6.
DR GlyGen; Q13491; 2 sites.
DR iPTMnet; Q13491; -.
DR PhosphoSitePlus; Q13491; -.
DR BioMuta; GPM6B; -.
DR DMDM; 20141466; -.
DR EPD; Q13491; -.
DR jPOST; Q13491; -.
DR MassIVE; Q13491; -.
DR PeptideAtlas; Q13491; -.
DR PRIDE; Q13491; -.
DR ProteomicsDB; 59485; -. [Q13491-1]
DR ProteomicsDB; 59486; -. [Q13491-2]
DR ProteomicsDB; 59487; -. [Q13491-3]
DR ProteomicsDB; 59488; -. [Q13491-4]
DR Antibodypedia; 484; 148 antibodies from 24 providers.
DR DNASU; 2824; -.
DR Ensembl; ENST00000316715.9; ENSP00000316861.4; ENSG00000046653.15. [Q13491-4]
DR Ensembl; ENST00000355135.6; ENSP00000347258.2; ENSG00000046653.15. [Q13491-3]
DR Ensembl; ENST00000356942.9; ENSP00000349420.5; ENSG00000046653.15. [Q13491-1]
DR Ensembl; ENST00000454189.6; ENSP00000389915.2; ENSG00000046653.15. [Q13491-2]
DR GeneID; 2824; -.
DR KEGG; hsa:2824; -.
DR MANE-Select; ENST00000316715.9; ENSP00000316861.4; NM_001001995.3; NP_001001995.1. [Q13491-4]
DR UCSC; uc004cvw.4; human. [Q13491-1]
DR CTD; 2824; -.
DR DisGeNET; 2824; -.
DR GeneCards; GPM6B; -.
DR HGNC; HGNC:4461; GPM6B.
DR HPA; ENSG00000046653; Group enriched (brain, choroid plexus, retina).
DR MIM; 300051; gene.
DR neXtProt; NX_Q13491; -.
DR OpenTargets; ENSG00000046653; -.
DR PharmGKB; PA28844; -.
DR VEuPathDB; HostDB:ENSG00000046653; -.
DR GeneTree; ENSGT00390000006915; -.
DR InParanoid; Q13491; -.
DR OMA; CMARVPY; -.
DR OrthoDB; 914457at2759; -.
DR PhylomeDB; Q13491; -.
DR TreeFam; TF315162; -.
DR PathwayCommons; Q13491; -.
DR SignaLink; Q13491; -.
DR BioGRID-ORCS; 2824; 9 hits in 684 CRISPR screens.
DR ChiTaRS; GPM6B; human.
DR GeneWiki; GPM6B; -.
DR GenomeRNAi; 2824; -.
DR Pharos; Q13491; Tbio.
DR PRO; PR:Q13491; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; Q13491; protein.
DR Bgee; ENSG00000046653; Expressed in dorsal motor nucleus of vagus nerve and 200 other tissues.
DR ExpressionAtlas; Q13491; baseline and differential.
DR Genevisible; Q13491; HS.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0045121; C:membrane raft; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0085029; P:extracellular matrix assembly; IMP:UniProtKB.
DR GO; GO:2000009; P:negative regulation of protein localization to cell surface; ISS:UniProtKB.
DR GO; GO:0051612; P:negative regulation of serotonin uptake; ISS:UniProtKB.
DR GO; GO:0007399; P:nervous system development; NAS:UniProtKB.
DR GO; GO:0031175; P:neuron projection development; IBA:GO_Central.
DR GO; GO:0001503; P:ossification; IEA:UniProtKB-KW.
DR GO; GO:0030501; P:positive regulation of bone mineralization; IMP:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; IMP:UniProtKB.
DR GO; GO:0051893; P:regulation of focal adhesion assembly; IMP:UniProtKB.
DR InterPro; IPR001614; Myelin_PLP.
DR InterPro; IPR018237; Myelin_PLP_CS.
DR PANTHER; PTHR11683; PTHR11683; 1.
DR Pfam; PF01275; Myelin_PLP; 1.
DR PRINTS; PR00214; MYELINPLP.
DR SMART; SM00002; PLP; 1.
DR PROSITE; PS00575; MYELIN_PLP_1; 1.
DR PROSITE; PS01004; MYELIN_PLP_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Developmental protein;
KW Differentiation; Glycoprotein; Membrane; Neurogenesis; Osteogenesis;
KW Phosphoprotein; Protein transport; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..265
FT /note="Neuronal membrane glycoprotein M6-b"
FT /id="PRO_0000159021"
FT TRANSMEM 31..51
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 90..110
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 136..156
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 224..244
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOD_RES 257
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35803"
FT CARBOHYD 73
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 177
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..20
FT /note="MKPAMETAAEENTEQSQERK -> M (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:8661015"
FT /id="VSP_003326"
FT VAR_SEQ 20
FT /note="K -> KVNSRAEMEIGRYHWMYPGSKNHQYHPVPTLGDRASPLSSP (in
FT isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_041121"
FT VAR_SEQ 240..265
FT /note="LIYMMATTYNYAVLKFKSREDCCTKF -> IHFLMILSSNWAYLKDASKMQA
FT YQDIKAKEEQELQDIQSRSKEQLNSYT (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043247"
FT MOD_RES Q13491-4:318
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
SQ SEQUENCE 265 AA; 28989 MW; 560AB12DD2B5AE75 CRC64;
MKPAMETAAE ENTEQSQERK GCFECCIKCL GGVPYASLVA TILCFSGVAL FCGCGHVALA
GTVAILEQHF STNASDHALL SEVIQLMQYV IYGIASFFFL YGIILLAEGF YTTSAVKELH
GEFKTTACGR CISGMFVFLT YVLGVAWLGV FGFSAVPVFM FYNIWSTCEV IKSPQTNGTT
GVEQICVDIR QYGIIPWNAF PGKICGSALE NICNTNEFYM SYHLFIVACA GAGATVIALL
IYMMATTYNY AVLKFKSRED CCTKF
