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SH2B adapter protein 1 (Pro-rich, PH and SH2 domain-containing signaling mediator) (PSM) (SH2 domain-containing protein 1B) (SH2-B PH domain-containing signaling mediator 1)

 SH2B1_MOUSE             Reviewed;         756 AA.
Q91ZM2; O54867; Q05DJ7; Q792R7; Q91ZM3; Q91ZV5; Q9WVM5;
18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
18-MAR-2008, sequence version 2.
23-MAY-2018, entry version 125.
RecName: Full=SH2B adapter protein 1;
AltName: Full=Pro-rich, PH and SH2 domain-containing signaling mediator;
Short=PSM;
AltName: Full=SH2 domain-containing protein 1B;
AltName: Full=SH2-B PH domain-containing signaling mediator 1;
Name=Sh2b1; Synonyms=Sh2bpsm1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY, AND
INTERACTION WITH INSR.
PubMed=9498552; DOI=10.1093/oxfordjournals.jbchem.a021868;
Riedel H., Wang J., Hansen H., Yousaf N.;
"PSM, an insulin-dependent, pro-rich, PH, SH2 domain containing
partner of the insulin receptor.";
J. Biochem. 122:1105-1113(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 6), ALTERNATIVE SPLICING (ISOFORMS
1; 2 AND 3), TISSUE SPECIFICITY, AND INTERACTION WITH INSR AND ISR1.
PubMed=10594240; DOI=10.1007/s003359901183;
Nelms K., O'Neill T.J., Li S., Hubbard S.R., Gustafson T.A.,
Paul W.E.;
"Alternative splicing, gene localization, and binding of SH2-B to the
insulin receptor kinase domain.";
Mamm. Genome 10:1160-1167(1999).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4), FUNCTION, AND
PHOSPHORYLATION.
TISSUE=Brain;
PubMed=11502739; DOI=10.1074/jbc.M104191200;
Yousaf N., Deng Y., Kang Y., Riedel H.;
"Four PSM/SH2-B alternative splice variants and their differential
roles in mitogenesis.";
J. Biol. Chem. 276:40940-40948(2001).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
STRAIN=NOD;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4 AND 5).
STRAIN=C57BL/6J, and FVB/N; TISSUE=Mammary tumor;
PubMed=15489334; DOI=10.1101/gr.2596504;
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).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 518-631, AND INTERACTION WITH INSR AND
IGF1R.
PubMed=9452421; DOI=10.1074/jbc.273.6.3136;
Wang J., Riedel H.;
"Insulin-like growth factor-I receptor and insulin receptor
association with a Src homology-2 domain-containing putative
adapter.";
J. Biol. Chem. 273:3136-3139(1998).
[7]
FUNCTION IN GH SIGNALING, AND INTERACTION WITH JAK2.
TISSUE=Kidney;
PubMed=9343427; DOI=10.1128/MCB.17.11.6633;
Rui L., Mathews L.S., Hotta K., Gustafson T.A., Carter-Su C.;
"Identification of SH2-Bbeta as a substrate of the tyrosine kinase
JAK2 involved in growth hormone signaling.";
Mol. Cell. Biol. 17:6633-6644(1997).
[8]
FUNCTION IN LEPTIN SIGNALING, AND INTERACTION WITH JAK2; ISR1 AND
ISR2.
PubMed=15316008; DOI=10.1074/jbc.M408495200;
Duan C., Li M., Rui L.;
"SH2-B promotes insulin receptor substrate 1 (IRS1)- and IRS2-mediated
activation of the phosphatidylinositol 3-kinase pathway in response to
leptin.";
J. Biol. Chem. 279:43684-43691(2004).
[9]
FUNCTION IN LEPTIN SIGNALING.
PubMed=16098827; DOI=10.1016/j.cmet.2005.07.004;
Ren D., Li M., Duan C., Rui L.;
"Identification of SH2-B as a key regulator of leptin sensitivity,
energy balance, and body weight in mice.";
Cell Metab. 2:95-104(2005).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-88; SER-96; SER-417 AND
SER-420, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Kidney, Liver, Pancreas, Spleen,
and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[12]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-270, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, and Embryo;
PubMed=24129315; DOI=10.1074/mcp.O113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V.,
Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
Vemulapalli V., Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
[13]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 519-627 IN COMPLEX WITH JAK2.
PubMed=16824542; DOI=10.1016/j.jmb.2006.05.070;
Hu J., Hubbard S.R.;
"Structural basis for phosphotyrosine recognition by the Src homology-
2 domains of the adapter proteins SH2-B and APS.";
J. Mol. Biol. 361:69-79(2006).
-!- FUNCTION: Adapter protein for several members of the tyrosine
kinase receptor family. Involved in multiple signaling pathways
mediated by Janus kinase (JAK) and receptor tyrosine kinases,
including the receptors of insulin (INS), insulin-like growth
factor I (IGF1), nerve growth factor (NGF), brain-derived
neurotrophic factor (BDNF), glial cell line-derived neurotrophic
factor (GDNF), platelet-derived growth factor (PDGF) and
fibroblast growth factors (FGFs). In growth hormone (GH)
signaling, autophosphorylated ('Tyr-813') JAK2 recruits SH2B1,
which in turn is phosphorylated by JAK2 on tyrosine residues.
These phosphotyrosines form potential binding sites for other
signaling proteins. GH also promotes serine/threonine
phosphorylation of SH2B1 and these phosphorylated residues may
serve to recruit other proteins to the GHR-JAK2-SH2B1 complexes,
such as RAC1. In leptin (LEP) signaling, binds to and potentiates
the activation of JAK2 by globally enhancing downstream pathways.
In response to leptin, binds simultaneously to both, JAK2 and IRS1
or IRS2, thus mediating formation of a complex of JAK2, SH2B1 and
IRS1 or IRS2. Mediates tyrosine phosphorylation of IRS1 and IRS2,
resulting in activation of the PI 3-kinase pathway. Acts as
positive regulator of NGF-mediated activation of the Akt/Forkhead
pathway; prolongs NGF-induced phosphorylation of AKT1 on 'Ser-473'
and AKT1 enzymatic activity. Enhances the kinase activity of the
cytokine receptor-associated tyrosine kinase JAK2 and of other
receptor tyrosine kinases, such as FGFR3 and NTRK1. For JAK2, the
mechanism seems to involve dimerization of both, SH2B1 and JAK2.
Enhances RET phosphorylation and kinase activity (By similarity).
Isoforms seem to be differentially involved in IGF-I and PDGF-
induced mitogenesis, according the order: isoform 3 > isoform 4 >
isoform 1 > isoform 2. {ECO:0000250, ECO:0000269|PubMed:11502739,
ECO:0000269|PubMed:15316008, ECO:0000269|PubMed:16098827,
ECO:0000269|PubMed:9343427}.
-!- SUBUNIT: Self-associates. Homopentamer (By similarity). Forms a
heteromultimeric complex with SH2B2 (By similarity). Interacts
with SH2B2. Isoform 1 interacts via its SH2 domain with JAK2.
Isoform 2 interacts via its SH2 domain and its N-terminus with
JAK2; the SH2 domain is required for the major interaction with
JAK2 phosphorylated on tyrosine residues; the N-terminus provides
a low-affinity binding to JAK2 independent of JAK2
phosphorylation. Isoform 3 interacts via its SH2 domain with JAK2.
Isoform 1 interacts via its SH2 domain with INSR; the interaction
requires receptor activation. Isoform 3 interacts via its SH2
domain with INSR; the interaction requires receptor activation and
requires INSR phosphorylation at 'Tyr-1175'. Isoform 1 interacts
with IGF1R; the interaction requires receptor activation. Isoform
2 interacts via its SH2 domain with FGFR3; the interaction
requires FGFR3 'Tyr-719' and 'Tyr-755'. Isoform 2 interacts with
RET; the interaction requires RET kinase activity and RET 'Tyr-
982'. Isoform 2 interacts with RAC1. Isoform 2 interacts with
PDGFRA and/or PDGFRB; the interaction requires receptor
activation. Interacts with ISR1 and ISR2. Isoform 3 is probably
part of a complex consisting of INSR, ISR1 and SH2B1. Probably
part of a ternary complex consisting of SH2B1, JAK2 and ISR1 or
ISR2. May interact with FCER1G (By similarity). Interacts (via SH2
domain) with NTRK1 (phosphorylated) (By similarity).
{ECO:0000250}.
-!- INTERACTION:
Q62120:Jak2; NbExp=3; IntAct=EBI-7178606, EBI-646604;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Membrane
{ECO:0000305}. Nucleus {ECO:0000250}. Note=Shuttles between the
nucleus and the cytoplasm. {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=6;
Name=1; Synonyms=Alpha;
IsoId=Q91ZM2-1; Sequence=Displayed;
Name=2; Synonyms=Beta;
IsoId=Q91ZM2-2; Sequence=VSP_032032;
Name=3; Synonyms=Gamma;
IsoId=Q91ZM2-3; Sequence=VSP_032033;
Name=4; Synonyms=Delta;
IsoId=Q91ZM2-4; Sequence=VSP_032034;
Name=5;
IsoId=Q91ZM2-5; Sequence=VSP_032029, VSP_032031;
Name=6; Synonyms=Sh2bpsm1 gamma;
IsoId=Q91ZM2-6; Sequence=VSP_032030, VSP_032033;
-!- TISSUE SPECIFICITY: Widely expressed with highest levels in liver,
brain and heart. Isoform 3 is widely expressed.
{ECO:0000269|PubMed:10594240, ECO:0000269|PubMed:9498552}.
-!- PTM: Phosphorylated on tyrosine residues in response to IGF-I and
PDGF stimulation. {ECO:0000269|PubMed:11502739}.
-!- SIMILARITY: Belongs to the SH2B adapter family. {ECO:0000305}.
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EMBL; AF020526; AAC33414.1; -; mRNA.
EMBL; AF380422; AAL07566.1; -; mRNA.
EMBL; AF074329; AAD41655.1; -; mRNA.
EMBL; AF421138; AAL16069.1; -; mRNA.
EMBL; AF421139; AAL16070.1; -; mRNA.
EMBL; AK168439; BAE40344.1; -; mRNA.
EMBL; AK170444; BAE41802.1; -; mRNA.
EMBL; BC011422; AAH11422.1; -; mRNA.
EMBL; BC051978; AAH51978.1; -; mRNA.
EMBL; AF036355; AAC39955.2; -; mRNA.
CCDS; CCDS40126.1; -. [Q91ZM2-3]
CCDS; CCDS85410.1; -. [Q91ZM2-4]
CCDS; CCDS85411.1; -. [Q91ZM2-1]
CCDS; CCDS85412.1; -. [Q91ZM2-2]
PIR; JC5886; JC5886.
RefSeq; NP_001074928.1; NM_001081459.2. [Q91ZM2-2]
RefSeq; NP_001276467.1; NM_001289538.1. [Q91ZM2-1]
RefSeq; NP_001276468.1; NM_001289539.1. [Q91ZM2-2]
RefSeq; NP_001276469.1; NM_001289540.1. [Q91ZM2-2]
RefSeq; NP_001276470.1; NM_001289541.1. [Q91ZM2-4]
RefSeq; NP_001276471.1; NM_001289542.1. [Q91ZM2-4]
RefSeq; NP_035493.2; NM_011363.3. [Q91ZM2-3]
RefSeq; XP_006507541.1; XM_006507478.3. [Q91ZM2-1]
RefSeq; XP_006507543.1; XM_006507480.3. [Q91ZM2-1]
RefSeq; XP_006507544.1; XM_006507481.3. [Q91ZM2-1]
RefSeq; XP_006507545.1; XM_006507482.1. [Q91ZM2-1]
RefSeq; XP_006507548.1; XM_006507485.3. [Q91ZM2-3]
RefSeq; XP_006507550.1; XM_006507487.3. [Q91ZM2-2]
UniGene; Mm.8538; -.
PDB; 2HDV; X-ray; 2.00 A; A/B=519-627.
PDB; 2HDX; X-ray; 2.35 A; A/B/C/D/E/F=519-627.
PDBsum; 2HDV; -.
PDBsum; 2HDX; -.
ProteinModelPortal; Q91ZM2; -.
SMR; Q91ZM2; -.
BioGrid; 203201; 2.
IntAct; Q91ZM2; 4.
MINT; Q91ZM2; -.
STRING; 10090.ENSMUSP00000032978; -.
iPTMnet; Q91ZM2; -.
PhosphoSitePlus; Q91ZM2; -.
PaxDb; Q91ZM2; -.
PeptideAtlas; Q91ZM2; -.
PRIDE; Q91ZM2; -.
Ensembl; ENSMUST00000032978; ENSMUSP00000032978; ENSMUSG00000030733. [Q91ZM2-3]
Ensembl; ENSMUST00000205340; ENSMUSP00000145953; ENSMUSG00000030733. [Q91ZM2-2]
Ensembl; ENSMUST00000205440; ENSMUSP00000145554; ENSMUSG00000030733. [Q91ZM2-2]
Ensembl; ENSMUST00000205497; ENSMUSP00000145842; ENSMUSG00000030733. [Q91ZM2-4]
Ensembl; ENSMUST00000205733; ENSMUSP00000145754; ENSMUSG00000030733. [Q91ZM2-1]
Ensembl; ENSMUST00000205889; ENSMUSP00000146282; ENSMUSG00000030733. [Q91ZM2-4]
Ensembl; ENSMUST00000206664; ENSMUSP00000146121; ENSMUSG00000030733. [Q91ZM2-5]
GeneID; 20399; -.
KEGG; mmu:20399; -.
UCSC; uc009jrh.2; mouse. [Q91ZM2-2]
UCSC; uc009jrj.2; mouse. [Q91ZM2-4]
UCSC; uc009jrk.2; mouse. [Q91ZM2-3]
UCSC; uc009jrm.2; mouse. [Q91ZM2-1]
CTD; 25970; -.
MGI; MGI:1201407; Sh2b1.
eggNOG; ENOG410IMWK; Eukaryota.
eggNOG; ENOG41102PH; LUCA.
GeneTree; ENSGT00530000063355; -.
HOVERGEN; HBG006707; -.
InParanoid; Q91ZM2; -.
KO; K12459; -.
OMA; GDRWTHR; -.
OrthoDB; EOG091G04RI; -.
PhylomeDB; Q91ZM2; -.
TreeFam; TF323184; -.
Reactome; R-MMU-1170546; Prolactin receptor signaling.
Reactome; R-MMU-982772; Growth hormone receptor signaling.
Reactome; R-MMU-983231; Factors involved in megakaryocyte development and platelet production.
ChiTaRS; Sh2b1; mouse.
EvolutionaryTrace; Q91ZM2; -.
PRO; PR:Q91ZM2; -.
Proteomes; UP000000589; Chromosome 7.
Bgee; ENSMUSG00000030733; -.
CleanEx; MM_SH2B1; -.
ExpressionAtlas; Q91ZM2; baseline and differential.
Genevisible; Q91ZM2; MM.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0001726; C:ruffle; TAS:MGI.
GO; GO:0004871; F:signal transducer activity; IEA:InterPro.
GO; GO:0035591; F:signaling adaptor activity; IEA:InterPro.
GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
GO; GO:0030032; P:lamellipodium assembly; IDA:MGI.
GO; GO:0045840; P:positive regulation of mitotic nuclear division; IDA:UniProtKB.
GO; GO:2000278; P:regulation of DNA biosynthetic process; IMP:UniProtKB.
CDD; cd10346; SH2_SH2B_family; 1.
Gene3D; 2.30.29.30; -; 1.
Gene3D; 3.30.505.10; -; 1.
InterPro; IPR011993; PH-like_dom_sf.
InterPro; IPR001849; PH_domain.
InterPro; IPR015012; Phe_ZIP.
InterPro; IPR036290; Phe_ZIP_sf.
InterPro; IPR000980; SH2.
InterPro; IPR036860; SH2_dom_sf.
InterPro; IPR030523; SH2B.
InterPro; IPR030521; SH2B1.
InterPro; IPR035057; SH2B1_SH2.
PANTHER; PTHR10872; PTHR10872; 1.
PANTHER; PTHR10872:SF3; PTHR10872:SF3; 1.
Pfam; PF00169; PH; 1.
Pfam; PF08916; Phe_ZIP; 1.
Pfam; PF00017; SH2; 1.
PRINTS; PR00401; SH2DOMAIN.
SMART; SM00233; PH; 1.
SMART; SM00252; SH2; 1.
SUPFAM; SSF109805; SSF109805; 1.
SUPFAM; SSF55550; SSF55550; 1.
PROSITE; PS50001; SH2; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome; Cytoplasm;
Membrane; Methylation; Nucleus; Phosphoprotein; Reference proteome;
SH2 domain.
CHAIN 1 756 SH2B adapter protein 1.
/FTId=PRO_0000323594.
DOMAIN 267 376 PH.
DOMAIN 527 625 SH2. {ECO:0000255|PROSITE-
ProRule:PRU00191}.
REGION 1 555 Interaction with JAK2 (low-affinity
binding; independent of JAK2
phosphorylation). {ECO:0000250}.
REGION 24 85 Required for self-association.
{ECO:0000250}.
REGION 85 196 Interaction with RAC1. {ECO:0000250}.
REGION 100 243 Required for NGF signaling.
{ECO:0000250}.
REGION 224 233 Required for nuclear localization.
{ECO:0000250}.
MOD_RES 88 88 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 96 96 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 270 270 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 417 417 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 420 420 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 439 439 Phosphotyrosine; by JAK1, JAK2 and PDGFR.
{ECO:0000250|UniProtKB:Q62985}.
MOD_RES 494 494 Phosphotyrosine; by JAK1, JAK2.
{ECO:0000250|UniProtKB:Q62985}.
VAR_SEQ 437 443 GAYGGLS -> AVDSEKT (in isoform 5).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_032029.
VAR_SEQ 441 460 Missing (in isoform 6).
{ECO:0000303|PubMed:10594240}.
/FTId=VSP_032030.
VAR_SEQ 444 756 Missing (in isoform 5).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_032031.
VAR_SEQ 632 756 ERSTSRDPAQPSEPPPWTDPPHPGAEEASGAPEVAAATAAA
AKERQEKEKAGSGGVQEELVPVAELVPMVELEEAIAPGTEA
QGGAGSSGDLEVSLMVQLQQLPLGGNGEEGGHPRAINNQYS
FV -> GREQAGSHAGVCEGDRCYPDASSTLLPFGASDCVT
EHLP (in isoform 2).
{ECO:0000303|PubMed:11502739,
ECO:0000303|PubMed:16141072,
ECO:0000303|PubMed:9498552}.
/FTId=VSP_032032.
VAR_SEQ 632 756 ERSTSRDPAQPSEPPPWTDPPHPGAEEASGAPEVAAATAAA
AKERQEKEKAGSGGVQEELVPVAELVPMVELEEAIAPGTEA
QGGAGSSGDLEVSLMVQLQQLPLGGNGEEGGHPRAINNQYS
FV -> GEQSRSAGEEVPVHPRSEAGSRLGAMQGCARATDA
TPMPPPPSCPSERVTV (in isoform 3 and
isoform 6). {ECO:0000303|PubMed:10594240,
ECO:0000303|PubMed:11502739,
ECO:0000303|PubMed:16141072}.
/FTId=VSP_032033.
VAR_SEQ 632 756 ERSTSRDPAQPSEPPPWTDPPHPGAEEASGAPEVAAATAAA
AKERQEKEKAGSGGVQEELVPVAELVPMVELEEAIAPGTEA
QGGAGSSGDLEVSLMVQLQQLPLGGNGEEGGHPRAINNQYS
FV -> GEQSRSAGEEVPVHPRSENGAPPVTQPSPLNPLHG
QIPHILGQKRRRGRQKLRQPQPQQPKRGKRKRKRAVEGSRK
SWSPWLSWSPWLNWKRP (in isoform 4).
{ECO:0000303|PubMed:11502739,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_032034.
CONFLICT 172 172 W -> C (in Ref. 2; AAD41655).
{ECO:0000305}.
CONFLICT 399 399 F -> L (in Ref. 5; AAH11422).
{ECO:0000305}.
CONFLICT 564 564 Y -> C (in Ref. 2; AAD41655).
{ECO:0000305}.
HELIX 522 524 {ECO:0000244|PDB:2HDV}.
STRAND 528 531 {ECO:0000244|PDB:2HDV}.
HELIX 534 542 {ECO:0000244|PDB:2HDV}.
HELIX 545 548 {ECO:0000244|PDB:2HDV}.
STRAND 551 556 {ECO:0000244|PDB:2HDV}.
STRAND 558 560 {ECO:0000244|PDB:2HDX}.
STRAND 563 570 {ECO:0000244|PDB:2HDV}.
STRAND 573 581 {ECO:0000244|PDB:2HDV}.
STRAND 587 589 {ECO:0000244|PDB:2HDV}.
STRAND 592 596 {ECO:0000244|PDB:2HDV}.
HELIX 597 604 {ECO:0000244|PDB:2HDV}.
TURN 612 616 {ECO:0000244|PDB:2HDX}.
SEQUENCE 756 AA; 79625 MW; 388BDC44267E6DE8 CRC64;
MNGAPSPEDG VFPSPPALPP PPPPSWQEFC ESHARAAALD LARRFRLYLA SHPQYAEPGA
EAAFSGRFAE LFLQHFEAEV ARASGSLSPP VLAPLSPGVE IPPSHDLSLE SCRVGGPLAV
LGPSRSSEDL AGPLPSSVPS STTSSKPKLK KRFSLRSVGR SVRGSVRGIL QWRGAVDSPS
QAGPLETTSG PPVLGGNSNS NSSGGAGTVG RALANDGTSP GERWTHRFER LRLSRGGGTL
KDGAGMIQRE ELLSFMGAEE AAPDPAGVGR GGGAAGLTSG GGGQPQWQKC RLLLRSEGEG
GGGSRLEFFV PPKASRPRLS IPCSTITDVR TATALEMPDR ENTFVVKVEG PSEYILETSD
ALHVKAWVSD IQECLSPGPC PAISPRPMTL PLAPGTSFFT KDNTDSLELP CLNHSESLPS
QDLLLGPSES NDRLSQGAYG GLSDRPSASF SPSSASIAAS HFDSMELLPP ELPPRIPIEE
GPPAGTVHPL STPYPPLDTP EAATGSFLFQ GESEGGEGDQ PLSGYPWFHG MLSRLKAAQL
VLEGGTGSHG VFLVRQSETR RGEYVLTFNF QGKAKHLRLS LNEEGQCRVQ HLWFQSIFDM
LEHFRVHPIP LESGGSSDVV LVSYVPSQRQ QERSTSRDPA QPSEPPPWTD PPHPGAEEAS
GAPEVAAATA AAAKERQEKE KAGSGGVQEE LVPVAELVPM VELEEAIAPG TEAQGGAGSS
GDLEVSLMVQ LQQLPLGGNG EEGGHPRAIN NQYSFV


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