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Protein

SH2B adapter protein 1

Gene

Sh2b1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.By similarity4 Publications

GO - Molecular functioni

GO - Biological processi

  • intracellular signal transduction Source: InterPro
  • lamellipodium assembly Source: MGI
  • positive regulation of mitotic nuclear division Source: UniProtKB
  • regulation of DNA biosynthetic process Source: UniProtKB
Complete GO annotation...

Enzyme and pathway databases

ReactomeiR-MMU-1170546. Prolactin receptor signaling.
R-MMU-2586551. Signaling by Leptin.
R-MMU-2586552. Signaling by Leptin.
R-MMU-982772. Growth hormone receptor signaling.
R-MMU-983231. Factors involved in megakaryocyte development and platelet production.

Names & Taxonomyi

Protein namesi
Recommended name:
SH2B adapter protein 1
Alternative name(s):
Pro-rich, PH and SH2 domain-containing signaling mediator
Short name:
PSM
SH2 domain-containing protein 1B
SH2-B PH domain-containing signaling mediator 1
Gene namesi
Name:Sh2b1
Synonyms:Sh2bpsm1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 7

Organism-specific databases

MGIiMGI:1201407. Sh2b1.

Subcellular locationi

  • Cytoplasm By similarity
  • Membrane Curated
  • Nucleus By similarity

  • Note: Shuttles between the nucleus and the cytoplasm.By similarity

GO - Cellular componenti

  • cytosol Source: Reactome
  • membrane Source: UniProtKB-SubCell
  • nucleus Source: UniProtKB-SubCell
  • ruffle Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 756756SH2B adapter protein 1PRO_0000323594Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei88 – 881PhosphoserineCombined sources
Modified residuei96 – 961PhosphoserineCombined sources
Modified residuei417 – 4171PhosphoserineCombined sources
Modified residuei420 – 4201PhosphoserineCombined sources
Modified residuei439 – 4391Phosphotyrosine; by JAK1, JAK2 and PDGFRBy similarity
Modified residuei494 – 4941Phosphotyrosine; by JAK1, JAK2By similarity

Post-translational modificationi

Phosphorylated on tyrosine residues in response to IGF-I and PDGF stimulation.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ91ZM2.
MaxQBiQ91ZM2.
PaxDbiQ91ZM2.
PRIDEiQ91ZM2.

PTM databases

iPTMnetiQ91ZM2.
PhosphoSiteiQ91ZM2.

Expressioni

Tissue specificityi

Widely expressed with highest levels in liver, brain and heart. Isoform 3 is widely expressed.2 Publications

Gene expression databases

BgeeiQ91ZM2.
CleanExiMM_SH2B1.
GenevisibleiQ91ZM2. MM.

Interactioni

Subunit structurei

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).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
Jak2Q621203EBI-7178606,EBI-646604

Protein-protein interaction databases

BioGridi203201. 2 interactions.
IntActiQ91ZM2. 4 interactions.
MINTiMINT-8025517.
STRINGi10090.ENSMUSP00000032978.

Structurei

Secondary structure

1
756
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi522 – 5243Combined sources
Beta strandi528 – 5314Combined sources
Helixi534 – 5429Combined sources
Helixi545 – 5484Combined sources
Beta strandi551 – 5566Combined sources
Beta strandi558 – 5603Combined sources
Beta strandi563 – 5708Combined sources
Beta strandi573 – 5819Combined sources
Beta strandi587 – 5893Combined sources
Beta strandi592 – 5965Combined sources
Helixi597 – 6048Combined sources
Turni612 – 6165Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2HDVX-ray2.00A/B519-627[»]
2HDXX-ray2.35A/B/C/D/E/F519-627[»]
ProteinModelPortaliQ91ZM2.
SMRiQ91ZM2. Positions 24-82, 247-379, 520-627.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ91ZM2.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini267 – 376110PHAdd
BLAST
Domaini527 – 62599SH2PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 555555Interaction with JAK2 (low-affinity binding; independent of JAK2 phosphorylation)By similarityAdd
BLAST
Regioni24 – 8562Required for self-associationBy similarityAdd
BLAST
Regioni85 – 196112Interaction with RAC1By similarityAdd
BLAST
Regioni100 – 243144Required for NGF signalingBy similarityAdd
BLAST
Regioni224 – 23310Required for nuclear localizationBy similarity

Sequence similaritiesi

Belongs to the SH2B adapter family.Curated
Contains 1 PH domain.Curated
Contains 1 SH2 domain.PROSITE-ProRule annotation

Keywords - Domaini

SH2 domain

Phylogenomic databases

eggNOGiENOG410IMWK. Eukaryota.
ENOG41102PH. LUCA.
GeneTreeiENSGT00530000063355.
HOVERGENiHBG006707.
InParanoidiQ91ZM2.
KOiK12459.
OMAiQEPNTSH.
OrthoDBiEOG7034GG.
PhylomeDBiQ91ZM2.
TreeFamiTF323184.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
3.30.505.10. 1 hit.
InterProiIPR011993. PH_dom-like.
IPR001849. PH_domain.
IPR015012. Phe_ZIP.
IPR000980. SH2.
IPR030523. SH2B.
IPR030521. SH2B1.
[Graphical view]
PANTHERiPTHR10872. PTHR10872. 3 hits.
PTHR10872:SF3. PTHR10872:SF3. 3 hits.
PfamiPF00169. PH. 1 hit.
PF08916. Phe_ZIP. 1 hit.
PF00017. SH2. 1 hit.
[Graphical view]
PRINTSiPR00401. SH2DOMAIN.
SMARTiSM00233. PH. 1 hit.
SM00252. SH2. 1 hit.
[Graphical view]
SUPFAMiSSF109805. SSF109805. 1 hit.
SSF50729. SSF50729. 1 hit.
SSF55550. SSF55550. 1 hit.
PROSITEiPS50001. SH2. 1 hit.
[Graphical view]

Sequences (6)i

Sequence statusi: Complete.

This entry describes 6 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q91ZM2-1) [UniParc]FASTAAdd to basket

Also known as: Alpha

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MNGAPSPEDG VFPSPPALPP PPPPSWQEFC ESHARAAALD LARRFRLYLA
60 70 80 90 100
SHPQYAEPGA EAAFSGRFAE LFLQHFEAEV ARASGSLSPP VLAPLSPGVE
110 120 130 140 150
IPPSHDLSLE SCRVGGPLAV LGPSRSSEDL AGPLPSSVPS STTSSKPKLK
160 170 180 190 200
KRFSLRSVGR SVRGSVRGIL QWRGAVDSPS QAGPLETTSG PPVLGGNSNS
210 220 230 240 250
NSSGGAGTVG RALANDGTSP GERWTHRFER LRLSRGGGTL KDGAGMIQRE
260 270 280 290 300
ELLSFMGAEE AAPDPAGVGR GGGAAGLTSG GGGQPQWQKC RLLLRSEGEG
310 320 330 340 350
GGGSRLEFFV PPKASRPRLS IPCSTITDVR TATALEMPDR ENTFVVKVEG
360 370 380 390 400
PSEYILETSD ALHVKAWVSD IQECLSPGPC PAISPRPMTL PLAPGTSFFT
410 420 430 440 450
KDNTDSLELP CLNHSESLPS QDLLLGPSES NDRLSQGAYG GLSDRPSASF
460 470 480 490 500
SPSSASIAAS HFDSMELLPP ELPPRIPIEE GPPAGTVHPL STPYPPLDTP
510 520 530 540 550
EAATGSFLFQ GESEGGEGDQ PLSGYPWFHG MLSRLKAAQL VLEGGTGSHG
560 570 580 590 600
VFLVRQSETR RGEYVLTFNF QGKAKHLRLS LNEEGQCRVQ HLWFQSIFDM
610 620 630 640 650
LEHFRVHPIP LESGGSSDVV LVSYVPSQRQ QERSTSRDPA QPSEPPPWTD
660 670 680 690 700
PPHPGAEEAS GAPEVAAATA AAAKERQEKE KAGSGGVQEE LVPVAELVPM
710 720 730 740 750
VELEEAIAPG TEAQGGAGSS GDLEVSLMVQ LQQLPLGGNG EEGGHPRAIN

NQYSFV
Length:756
Mass (Da):79,625
Last modified:March 18, 2008 - v2
Checksum:i388BDC44267E6DE8
GO
Isoform 2 (identifier: Q91ZM2-2) [UniParc]FASTAAdd to basket

Also known as: Beta

The sequence of this isoform differs from the canonical sequence as follows:
     632-756: ERSTSRDPAQ...RAINNQYSFV → GREQAGSHAG...ASDCVTEHLP

Show »
Length:670
Mass (Da):70,855
Checksum:iBFBFA44F8E97B710
GO
Isoform 3 (identifier: Q91ZM2-3) [UniParc]FASTAAdd to basket

Also known as: Gamma

The sequence of this isoform differs from the canonical sequence as follows:
     632-756: ERSTSRDPAQ...RAINNQYSFV → GEQSRSAGEE...PSCPSERVTV

Show »
Length:682
Mass (Da):72,067
Checksum:iBC7F894A42959027
GO
Isoform 4 (identifier: Q91ZM2-4) [UniParc]FASTAAdd to basket

Also known as: Delta

The sequence of this isoform differs from the canonical sequence as follows:
     632-756: ERSTSRDPAQ...RAINNQYSFV → GEQSRSAGEE...WSPWLNWKRP

Show »
Length:724
Mass (Da):77,594
Checksum:iD23C6FC816B3B0C9
GO
Isoform 5 (identifier: Q91ZM2-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     437-443: GAYGGLS → AVDSEKT
     444-756: Missing.

Show »
Length:443
Mass (Da):46,389
Checksum:i24C3C4516A9DE22C
GO
Isoform 6 (identifier: Q91ZM2-6) [UniParc]FASTAAdd to basket

Also known as: Sh2bpsm1 gamma

The sequence of this isoform differs from the canonical sequence as follows:
     441-460: Missing.
     632-756: ERSTSRDPAQ...RAINNQYSFV → GEQSRSAGEE...PSCPSERVTV

Show »
Length:662
Mass (Da):70,190
Checksum:i17417293AF539C7C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti172 – 1721W → C in AAD41655 (PubMed:10594240).Curated
Sequence conflicti399 – 3991F → L in AAH11422 (PubMed:15489334).Curated
Sequence conflicti564 – 5641Y → C in AAD41655 (PubMed:10594240).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei437 – 4437GAYGGLS → AVDSEKT in isoform 5. 1 PublicationVSP_032029
Alternative sequencei441 – 46020Missing in isoform 6. 1 PublicationVSP_032030Add
BLAST
Alternative sequencei444 – 756313Missing in isoform 5. 1 PublicationVSP_032031Add
BLAST
Alternative sequencei632 – 756125ERSTS…QYSFV → GREQAGSHAGVCEGDRCYPD ASSTLLPFGASDCVTEHLP in isoform 2. 3 PublicationsVSP_032032Add
BLAST
Alternative sequencei632 – 756125ERSTS…QYSFV → GEQSRSAGEEVPVHPRSEAG SRLGAMQGCARATDATPMPP PPSCPSERVTV in isoform 3 and isoform 6. 3 PublicationsVSP_032033Add
BLAST
Alternative sequencei632 – 756125ERSTS…QYSFV → GEQSRSAGEEVPVHPRSENG APPVTQPSPLNPLHGQIPHI LGQKRRRGRQKLRQPQPQQP KRGKRKRKRAVEGSRKSWSP WLSWSPWLNWKRP in isoform 4. 2 PublicationsVSP_032034Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF020526 mRNA. Translation: AAC33414.1.
AF380422 mRNA. Translation: AAL07566.1.
AF074329 mRNA. Translation: AAD41655.1.
AF421138 mRNA. Translation: AAL16069.1.
AF421139 mRNA. Translation: AAL16070.1.
AK168439 mRNA. Translation: BAE40344.1.
AK170444 mRNA. Translation: BAE41802.1.
BC011422 mRNA. Translation: AAH11422.1.
BC051978 mRNA. Translation: AAH51978.1.
AF036355 mRNA. Translation: AAC39955.2.
CCDSiCCDS40126.1. [Q91ZM2-3]
PIRiJC5886.
RefSeqiNP_001074928.1. NM_001081459.2. [Q91ZM2-2]
NP_001276467.1. NM_001289538.1. [Q91ZM2-1]
NP_001276468.1. NM_001289539.1. [Q91ZM2-2]
NP_001276469.1. NM_001289540.1. [Q91ZM2-2]
NP_001276470.1. NM_001289541.1. [Q91ZM2-4]
NP_001276471.1. NM_001289542.1. [Q91ZM2-4]
NP_035493.2. NM_011363.3. [Q91ZM2-3]
XP_006507541.1. XM_006507478.2. [Q91ZM2-1]
XP_006507543.1. XM_006507480.2. [Q91ZM2-1]
XP_006507544.1. XM_006507481.2. [Q91ZM2-1]
XP_006507545.1. XM_006507482.1. [Q91ZM2-1]
XP_006507548.1. XM_006507485.2. [Q91ZM2-3]
XP_006507550.1. XM_006507487.2. [Q91ZM2-2]
UniGeneiMm.8538.

Genome annotation databases

EnsembliENSMUST00000032978; ENSMUSP00000032978; ENSMUSG00000030733. [Q91ZM2-3]
ENSMUST00000205340; ENSMUSP00000145953; ENSMUSG00000030733. [Q91ZM2-2]
ENSMUST00000205440; ENSMUSP00000145554; ENSMUSG00000030733. [Q91ZM2-2]
ENSMUST00000205497; ENSMUSP00000145842; ENSMUSG00000030733. [Q91ZM2-4]
ENSMUST00000205733; ENSMUSP00000145754; ENSMUSG00000030733. [Q91ZM2-1]
ENSMUST00000205889; ENSMUSP00000146282; ENSMUSG00000030733. [Q91ZM2-4]
ENSMUST00000206664; ENSMUSP00000146121; ENSMUSG00000030733. [Q91ZM2-5]
GeneIDi20399.
KEGGimmu:20399.
UCSCiuc009jrh.2. mouse. [Q91ZM2-2]
uc009jrj.2. mouse. [Q91ZM2-4]
uc009jrk.2. mouse. [Q91ZM2-3]
uc009jrm.2. mouse. [Q91ZM2-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF020526 mRNA. Translation: AAC33414.1.
AF380422 mRNA. Translation: AAL07566.1.
AF074329 mRNA. Translation: AAD41655.1.
AF421138 mRNA. Translation: AAL16069.1.
AF421139 mRNA. Translation: AAL16070.1.
AK168439 mRNA. Translation: BAE40344.1.
AK170444 mRNA. Translation: BAE41802.1.
BC011422 mRNA. Translation: AAH11422.1.
BC051978 mRNA. Translation: AAH51978.1.
AF036355 mRNA. Translation: AAC39955.2.
CCDSiCCDS40126.1. [Q91ZM2-3]
PIRiJC5886.
RefSeqiNP_001074928.1. NM_001081459.2. [Q91ZM2-2]
NP_001276467.1. NM_001289538.1. [Q91ZM2-1]
NP_001276468.1. NM_001289539.1. [Q91ZM2-2]
NP_001276469.1. NM_001289540.1. [Q91ZM2-2]
NP_001276470.1. NM_001289541.1. [Q91ZM2-4]
NP_001276471.1. NM_001289542.1. [Q91ZM2-4]
NP_035493.2. NM_011363.3. [Q91ZM2-3]
XP_006507541.1. XM_006507478.2. [Q91ZM2-1]
XP_006507543.1. XM_006507480.2. [Q91ZM2-1]
XP_006507544.1. XM_006507481.2. [Q91ZM2-1]
XP_006507545.1. XM_006507482.1. [Q91ZM2-1]
XP_006507548.1. XM_006507485.2. [Q91ZM2-3]
XP_006507550.1. XM_006507487.2. [Q91ZM2-2]
UniGeneiMm.8538.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2HDVX-ray2.00A/B519-627[»]
2HDXX-ray2.35A/B/C/D/E/F519-627[»]
ProteinModelPortaliQ91ZM2.
SMRiQ91ZM2. Positions 24-82, 247-379, 520-627.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi203201. 2 interactions.
IntActiQ91ZM2. 4 interactions.
MINTiMINT-8025517.
STRINGi10090.ENSMUSP00000032978.

PTM databases

iPTMnetiQ91ZM2.
PhosphoSiteiQ91ZM2.

Proteomic databases

EPDiQ91ZM2.
MaxQBiQ91ZM2.
PaxDbiQ91ZM2.
PRIDEiQ91ZM2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000032978; ENSMUSP00000032978; ENSMUSG00000030733. [Q91ZM2-3]
ENSMUST00000205340; ENSMUSP00000145953; ENSMUSG00000030733. [Q91ZM2-2]
ENSMUST00000205440; ENSMUSP00000145554; ENSMUSG00000030733. [Q91ZM2-2]
ENSMUST00000205497; ENSMUSP00000145842; ENSMUSG00000030733. [Q91ZM2-4]
ENSMUST00000205733; ENSMUSP00000145754; ENSMUSG00000030733. [Q91ZM2-1]
ENSMUST00000205889; ENSMUSP00000146282; ENSMUSG00000030733. [Q91ZM2-4]
ENSMUST00000206664; ENSMUSP00000146121; ENSMUSG00000030733. [Q91ZM2-5]
GeneIDi20399.
KEGGimmu:20399.
UCSCiuc009jrh.2. mouse. [Q91ZM2-2]
uc009jrj.2. mouse. [Q91ZM2-4]
uc009jrk.2. mouse. [Q91ZM2-3]
uc009jrm.2. mouse. [Q91ZM2-1]

Organism-specific databases

CTDi25970.
MGIiMGI:1201407. Sh2b1.

Phylogenomic databases

eggNOGiENOG410IMWK. Eukaryota.
ENOG41102PH. LUCA.
GeneTreeiENSGT00530000063355.
HOVERGENiHBG006707.
InParanoidiQ91ZM2.
KOiK12459.
OMAiQEPNTSH.
OrthoDBiEOG7034GG.
PhylomeDBiQ91ZM2.
TreeFamiTF323184.

Enzyme and pathway databases

ReactomeiR-MMU-1170546. Prolactin receptor signaling.
R-MMU-2586551. Signaling by Leptin.
R-MMU-2586552. Signaling by Leptin.
R-MMU-982772. Growth hormone receptor signaling.
R-MMU-983231. Factors involved in megakaryocyte development and platelet production.

Miscellaneous databases

ChiTaRSiSh2b1. mouse.
EvolutionaryTraceiQ91ZM2.
NextBioi298350.
PROiQ91ZM2.
SOURCEiSearch...

Gene expression databases

BgeeiQ91ZM2.
CleanExiMM_SH2B1.
GenevisibleiQ91ZM2. MM.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
3.30.505.10. 1 hit.
InterProiIPR011993. PH_dom-like.
IPR001849. PH_domain.
IPR015012. Phe_ZIP.
IPR000980. SH2.
IPR030523. SH2B.
IPR030521. SH2B1.
[Graphical view]
PANTHERiPTHR10872. PTHR10872. 3 hits.
PTHR10872:SF3. PTHR10872:SF3. 3 hits.
PfamiPF00169. PH. 1 hit.
PF08916. Phe_ZIP. 1 hit.
PF00017. SH2. 1 hit.
[Graphical view]
PRINTSiPR00401. SH2DOMAIN.
SMARTiSM00233. PH. 1 hit.
SM00252. SH2. 1 hit.
[Graphical view]
SUPFAMiSSF109805. SSF109805. 1 hit.
SSF50729. SSF50729. 1 hit.
SSF55550. SSF55550. 1 hit.
PROSITEiPS50001. SH2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "PSM, an insulin-dependent, pro-rich, PH, SH2 domain containing partner of the insulin receptor."
    Riedel H., Wang J., Hansen H., Yousaf N.
    J. Biochem. 122:1105-1113(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY, INTERACTION WITH INSR.
  2. "Alternative splicing, gene localization, and binding of SH2-B to the insulin receptor kinase domain."
    Nelms K., O'Neill T.J., Li S., Hubbard S.R., Gustafson T.A., Paul W.E.
    Mamm. Genome 10:1160-1167(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 6), ALTERNATIVE SPLICING (ISOFORMS 1; 2 AND 3), TISSUE SPECIFICITY, INTERACTION WITH INSR AND ISR1.
  3. "Four PSM/SH2-B alternative splice variants and their differential roles in mitogenesis."
    Yousaf N., Deng Y., Kang Y., Riedel H.
    J. Biol. Chem. 276:40940-40948(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4), FUNCTION, PHOSPHORYLATION.
    Tissue: Brain.
  4. "The transcriptional landscape of the mammalian genome."
    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.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
    Strain: NOD.
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4 AND 5).
    Strain: C57BL/6J and FVB/N.
    Tissue: Mammary tumor.
  6. "Insulin-like growth factor-I receptor and insulin receptor association with a Src homology-2 domain-containing putative adapter."
    Wang J., Riedel H.
    J. Biol. Chem. 273:3136-3139(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 518-631, INTERACTION WITH INSR AND IGF1R.
  7. "Identification of SH2-Bbeta as a substrate of the tyrosine kinase JAK2 involved in growth hormone signaling."
    Rui L., Mathews L.S., Hotta K., Gustafson T.A., Carter-Su C.
    Mol. Cell. Biol. 17:6633-6644(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN GH SIGNALING, INTERACTION WITH JAK2.
    Tissue: Kidney.
  8. "SH2-B promotes insulin receptor substrate 1 (IRS1)- and IRS2-mediated activation of the phosphatidylinositol 3-kinase pathway in response to leptin."
    Duan C., Li M., Rui L.
    J. Biol. Chem. 279:43684-43691(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN LEPTIN SIGNALING, INTERACTION WITH JAK2; ISR1 AND ISR2.
  9. "Identification of SH2-B as a key regulator of leptin sensitivity, energy balance, and body weight in mice."
    Ren D., Li M., Duan C., Rui L.
    Cell Metab. 2:95-104(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN LEPTIN SIGNALING.
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-88; SER-96; SER-417 AND SER-420, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Kidney, Liver, Pancreas, Spleen and Testis.
  12. "Structural basis for phosphotyrosine recognition by the Src homology-2 domains of the adapter proteins SH2-B and APS."
    Hu J., Hubbard S.R.
    J. Mol. Biol. 361:69-79(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 519-627 IN COMPLEX WITH JAK2.

Entry informationi

Entry nameiSH2B1_MOUSE
AccessioniPrimary (citable) accession number: Q91ZM2
Secondary accession number(s): O54867
, Q05DJ7, Q792R7, Q91ZM3, Q91ZV5, Q9WVM5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: March 18, 2008
Last modified: March 16, 2016
This is version 109 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.