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Q9NRF2

- SH2B1_HUMAN

UniProt

Q9NRF2 - SH2B1_HUMAN

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Protein

SH2B adapter protein 1

Gene
SH2B1, KIAA1299, SH2B
Organism
Homo sapiens (Human)
Status
Reviewed - 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. Isoforms seem to be differentially involved in IGF-I and PDGF-induced mitogenesis By similarity.7 Publications

GO - Molecular functioni

  1. protein binding Source: IntAct
  2. signal transducer activity Source: InterPro

GO - Biological processi

  1. blood coagulation Source: Reactome
  2. cellular component movement Source: Ensembl
  3. intracellular signal transduction Source: InterPro
  4. lamellipodium assembly Source: Ensembl
  5. positive regulation of mitosis Source: Ensembl
  6. regulation of DNA biosynthetic process Source: Ensembl
Complete GO annotation...

Enzyme and pathway databases

ReactomeiREACT_111133. Growth hormone receptor signaling.
REACT_115697. Prolactin receptor signaling.
REACT_169118. Signaling by Leptin.
REACT_24970. Factors involved in megakaryocyte development and platelet production.
SignaLinkiQ9NRF2.

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
Gene namesi
Name:SH2B1
Synonyms:KIAA1299, SH2B
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 16

Organism-specific databases

HGNCiHGNC:30417. SH2B1.

Subcellular locationi

Cytoplasm By similarity. Membrane Inferred. Nucleus By similarity
Note: Shuttles between the nucleus and the cytoplasm By similarity.

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. membrane Source: UniProtKB-SubCell
  3. nucleus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi29 – 291F → R: Abolishes self-association and interaction with INSR and IGF1R. 1 Publication
Mutagenesisi34 – 341A → D: Abolishes self-association and interaction with INSR and IGF1R. 1 Publication
Mutagenesisi38 – 381A → D: Abolishes self-association and interaction with INSR and IGF1R. 1 Publication
Mutagenesisi41 – 411F → A: Abolishes self-association and interaction with INSR and IGF1R. 1 Publication
Mutagenesisi42 – 421A → D: Abolishes self-association and interaction with INSR and IGF1R. 1 Publication
Mutagenesisi48 – 481Y → A: Abolishes self-association and interaction with INSR and IGF1R. 1 Publication
Mutagenesisi68 – 681F → A: Abolishes self-association and interaction with INSR and IGF1R. 1 Publication
Mutagenesisi72 – 721F → A: Abolishes self-association and interaction with INSR and IGF1R. 1 Publication
Mutagenesisi555 – 5551R → A: Abolishes self-association and interaction with INSR and IGF1R. 1 Publication

Organism-specific databases

Orphaneti261222. Distal 16p11.2 microdeletion syndrome.
261197. Proximal 16p11.2 microdeletion syndrome.
329249. Severe early-onset obesity-insulin resistance syndrome due to SH2B1 deficiency.
PharmGKBiPA145148084.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 756756SH2B adapter protein 1PRO_0000323593Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei88 – 881Phosphoserine
Modified residuei96 – 961Phosphoserine2 Publications
Modified residuei439 – 4391Phosphotyrosine; by JAK1, JAK2 and PDGFR By similarity
Modified residuei494 – 4941Phosphotyrosine; by JAK1, JAK2 By similarity
Modified residuei624 – 6241Phosphotyrosine

Post-translational modificationi

Phosphorylated on tyrosine residues in response to receptor kinase stimulation. Phosphorylated by RET.3 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9NRF2.
PaxDbiQ9NRF2.
PRIDEiQ9NRF2.

PTM databases

PhosphoSiteiQ9NRF2.

Expressioni

Tissue specificityi

Widely expressed with highest levels in skeletal muscle and ovary.1 Publication

Gene expression databases

ArrayExpressiQ9NRF2.
BgeeiQ9NRF2.
CleanExiHS_SH2B1.
GenevestigatoriQ9NRF2.

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-1185'. Isoform 1 interacts with IGF1R; the interaction requires receptor activation. Isoform 2 interacts with PRKAR1A/RET (PTC2) fusion protein; the interaction requires RET 'Tyr-905' and Tyr-981'. Isoform 2 interacts via its SH2 domain with FGFR3; the interaction requires FGFR3 'Tyr-724' and 'Tyr-760'. Isoform 2 interacts with RET; the interaction requires RET kinase activity and RET 'Tyr-981'. 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.9 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
INSRP062136EBI-310491,EBI-475899

Protein-protein interaction databases

BioGridi117455. 14 interactions.
IntActiQ9NRF2. 6 interactions.
MINTiMINT-1494470.
STRINGi9606.ENSP00000337163.

Structurei

3D structure databases

ProteinModelPortaliQ9NRF2.
SMRiQ9NRF2. Positions 24-82, 247-379, 520-654.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini267 – 376110PHAdd
BLAST
Domaini527 – 62599SH2Add
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-associationAdd
BLAST
Regioni85 – 196112Interaction with RAC1 By similarityAdd
BLAST
Regioni100 – 243144Required for NGF signaling By similarityAdd
BLAST
Regioni224 – 23310Required for nuclear localization By similarity

Sequence similaritiesi

Belongs to the SH2B adapter family.
Contains 1 PH domain.
Contains 1 SH2 domain.

Keywords - Domaini

SH2 domain

Phylogenomic databases

eggNOGiNOG77816.
HOVERGENiHBG006707.
InParanoidiQ9NRF2.
KOiK12459.
OMAiQEPNTSH.
OrthoDBiEOG7034GG.
PhylomeDBiQ9NRF2.
TreeFamiTF323184.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
3.30.505.10. 1 hit.
InterProiIPR001849. PH_domain.
IPR011993. PH_like_dom.
IPR015012. Phe_ZIP.
IPR000980. SH2.
[Graphical view]
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.
SSF55550. SSF55550. 1 hit.
PROSITEiPS50001. SH2. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9NRF2-1) [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

MNGAPSPEDG ASPSSPPLPP PPPPSWREFC ESHARAAALD FARRFRLYLA    50
SHPQYAGPGA EAAFSRRFAE LFLQHFEAEV ARASGSLSPP ILAPLSPGAE 100
ISPHDLSLES CRVGGPLAVL GPSRSSEDLA GPLPSSVSSS STTSSKPKLK 150
KRFSLRSVGR SVRGSVRGIL QWRGTVDPPS SAGPLETSSG PPVLGGNSNS 200
NSSGGAGTVG RGLVSDGTSP GERWTHRFER LRLSRGGGAL KDGAGMVQRE 250
ELLSFMGAEE AAPDPAGVGR GGGVAGPPSG GGGQPQWQKC RLLLRSEGEG 300
GGGSRLEFFV PPKASRPRLS IPCSSITDVR TTTALEMPDR ENTFVVKVEG 350
PSEYIMETVD AQHVKAWVSD IQECLSPGPC PATSPRPMTL PLAPGTSFLT 400
RENTDSLELS CLNHSESLPS QDLLLGPSES NDRLSQGAYG GLSDRPSASI 450
SPSSASIAAS HFDSMELLPP ELPPRIPIEE GPPTGTVHPL SAPYPPLDTP 500
ETATGSFLFQ GEPEGGEGDQ PLSGYPWFHG MLSRLKAAQL VLTGGTGSHG 550
VFLVRQSETR RGEYVLTFNF QGKAKHLRLS LNEEGQCRVQ HLWFQSIFDM 600
LEHFRVHPIP LESGGSSDVV LVSYVPSSQR QQEPTTSHDP PQPPEPPSWT 650
DPPQPGAEEA SRAPEVAAAA AAAAKERQEK EKAGGGGVPE ELVPVVELVP 700
VVELEEAIAP GSEAQGAGSG GDAGVPPMVQ LQQSPLGGDG EEGGHPRAIN 750
NQYSFV 756
Length:756
Mass (Da):79,366
Last modified:November 30, 2010 - v3
Checksum:iCF680B57114CB1D3
GO
Isoform 2 (identifier: Q9NRF2-2) [UniParc]FASTAAdd to Basket

Also known as: Beta

The sequence of this isoform differs from the canonical sequence as follows:
     633-756: EPTTSHDPPQ...RAINNQYSFV → GREQAGSHAG...ASDCVTDHLP

Show »
Length:671
Mass (Da):70,781
Checksum:i3EAD9A95F370FD94
GO
Isoform 3 (identifier: Q9NRF2-3) [UniParc]FASTAAdd to Basket

Also known as: Gamma

The sequence of this isoform differs from the canonical sequence as follows:
     633-756: EPTTSHDPPQ...RAINNQYSFV → GEQSRSAGEE...PSCPSERVTV

Show »
Length:683
Mass (Da):72,188
Checksum:i353155178527B5A7
GO

Sequence cautioni

The sequence AAH10704.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
The sequence BAA92537.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
The sequence BAB55148.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti484 – 4841T → A.2 Publications
Corresponds to variant rs7498665 [ dbSNP | Ensembl ].
VAR_039550
Natural varianti541 – 5411V → A.1 Publication
Corresponds to variant rs17850682 [ dbSNP | Ensembl ].
VAR_039551

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei633 – 756124EPTTS…QYSFV → GREQAGSHAGVCEGDGCHPD ASCTLMPFGASDCVTDHLP in isoform 2. VSP_032027Add
BLAST
Alternative sequencei633 – 756124EPTTS…QYSFV → GEQSRSAGEEVPVHPRSEAG SRLGAMRGCAREMDATPMPP APSCPSERVTV in isoform 3. VSP_032028Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti197 – 1971N → D in BAF83021. 1 Publication
Sequence conflicti519 – 5191D → G in BAF83021. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF227967 mRNA. Translation: AAF73912.1.
AF227968 mRNA. Translation: AAF73913.1.
AF227969 mRNA. Translation: AAF73914.1.
AB037720 mRNA. Translation: BAA92537.1. Different initiation.
AK027488 mRNA. Translation: BAB55148.1. Different initiation.
AK290332 mRNA. Translation: BAF83021.1.
AL049924 mRNA. Translation: CAB43208.1.
AL713760 mRNA. Translation: CAD28530.1.
AC133550 Genomic DNA. No translation available.
BC010704 mRNA. Translation: AAH10704.1. Different initiation.
CCDSiCCDS32424.1. [Q9NRF2-2]
CCDS53996.1. [Q9NRF2-1]
CCDS53997.1. [Q9NRF2-3]
PIRiT08662.
RefSeqiNP_001139267.1. NM_001145795.1. [Q9NRF2-1]
NP_001139268.1. NM_001145796.1. [Q9NRF2-2]
NP_001139269.1. NM_001145797.1. [Q9NRF2-3]
NP_001139284.1. NM_001145812.1. [Q9NRF2-2]
NP_056318.2. NM_015503.2. [Q9NRF2-2]
UniGeneiHs.15744.

Genome annotation databases

EnsembliENST00000322610; ENSP00000321221; ENSG00000178188. [Q9NRF2-1]
ENST00000337120; ENSP00000337163; ENSG00000178188. [Q9NRF2-2]
ENST00000359285; ENSP00000352232; ENSG00000178188. [Q9NRF2-3]
ENST00000395532; ENSP00000378903; ENSG00000178188. [Q9NRF2-2]
GeneIDi25970.
KEGGihsa:25970.
UCSCiuc002dri.3. human. [Q9NRF2-1]
uc002drj.3. human. [Q9NRF2-3]
uc002drk.3. human. [Q9NRF2-2]

Polymorphism databases

DMDMi313104186.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF227967 mRNA. Translation: AAF73912.1 .
AF227968 mRNA. Translation: AAF73913.1 .
AF227969 mRNA. Translation: AAF73914.1 .
AB037720 mRNA. Translation: BAA92537.1 . Different initiation.
AK027488 mRNA. Translation: BAB55148.1 . Different initiation.
AK290332 mRNA. Translation: BAF83021.1 .
AL049924 mRNA. Translation: CAB43208.1 .
AL713760 mRNA. Translation: CAD28530.1 .
AC133550 Genomic DNA. No translation available.
BC010704 mRNA. Translation: AAH10704.1 . Different initiation.
CCDSi CCDS32424.1. [Q9NRF2-2 ]
CCDS53996.1. [Q9NRF2-1 ]
CCDS53997.1. [Q9NRF2-3 ]
PIRi T08662.
RefSeqi NP_001139267.1. NM_001145795.1. [Q9NRF2-1 ]
NP_001139268.1. NM_001145796.1. [Q9NRF2-2 ]
NP_001139269.1. NM_001145797.1. [Q9NRF2-3 ]
NP_001139284.1. NM_001145812.1. [Q9NRF2-2 ]
NP_056318.2. NM_015503.2. [Q9NRF2-2 ]
UniGenei Hs.15744.

3D structure databases

ProteinModelPortali Q9NRF2.
SMRi Q9NRF2. Positions 24-82, 247-379, 520-654.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 117455. 14 interactions.
IntActi Q9NRF2. 6 interactions.
MINTi MINT-1494470.
STRINGi 9606.ENSP00000337163.

PTM databases

PhosphoSitei Q9NRF2.

Polymorphism databases

DMDMi 313104186.

Proteomic databases

MaxQBi Q9NRF2.
PaxDbi Q9NRF2.
PRIDEi Q9NRF2.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000322610 ; ENSP00000321221 ; ENSG00000178188 . [Q9NRF2-1 ]
ENST00000337120 ; ENSP00000337163 ; ENSG00000178188 . [Q9NRF2-2 ]
ENST00000359285 ; ENSP00000352232 ; ENSG00000178188 . [Q9NRF2-3 ]
ENST00000395532 ; ENSP00000378903 ; ENSG00000178188 . [Q9NRF2-2 ]
GeneIDi 25970.
KEGGi hsa:25970.
UCSCi uc002dri.3. human. [Q9NRF2-1 ]
uc002drj.3. human. [Q9NRF2-3 ]
uc002drk.3. human. [Q9NRF2-2 ]

Organism-specific databases

CTDi 25970.
GeneCardsi GC16P028875.
H-InvDB HIX0017272.
HGNCi HGNC:30417. SH2B1.
MIMi 608937. gene.
neXtProti NX_Q9NRF2.
Orphaneti 261222. Distal 16p11.2 microdeletion syndrome.
261197. Proximal 16p11.2 microdeletion syndrome.
329249. Severe early-onset obesity-insulin resistance syndrome due to SH2B1 deficiency.
PharmGKBi PA145148084.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG77816.
HOVERGENi HBG006707.
InParanoidi Q9NRF2.
KOi K12459.
OMAi QEPNTSH.
OrthoDBi EOG7034GG.
PhylomeDBi Q9NRF2.
TreeFami TF323184.

Enzyme and pathway databases

Reactomei REACT_111133. Growth hormone receptor signaling.
REACT_115697. Prolactin receptor signaling.
REACT_169118. Signaling by Leptin.
REACT_24970. Factors involved in megakaryocyte development and platelet production.
SignaLinki Q9NRF2.

Miscellaneous databases

GeneWikii SH2B1.
GenomeRNAii 25970.
NextBioi 47602.
PROi Q9NRF2.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9NRF2.
Bgeei Q9NRF2.
CleanExi HS_SH2B1.
Genevestigatori Q9NRF2.

Family and domain databases

Gene3Di 2.30.29.30. 1 hit.
3.30.505.10. 1 hit.
InterProi IPR001849. PH_domain.
IPR011993. PH_like_dom.
IPR015012. Phe_ZIP.
IPR000980. SH2.
[Graphical view ]
Pfami PF00169. PH. 1 hit.
PF08916. Phe_ZIP. 1 hit.
PF00017. SH2. 1 hit.
[Graphical view ]
PRINTSi PR00401. SH2DOMAIN.
SMARTi SM00233. PH. 1 hit.
SM00252. SH2. 1 hit.
[Graphical view ]
SUPFAMi SSF109805. SSF109805. 1 hit.
SSF55550. SSF55550. 1 hit.
PROSITEi PS50001. SH2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), FUNCTION IN JAK2 ACTIVATION, SELF-ASSOCIATION, INTERACTION WITH JAK2; SH2B2; INSR AND IGF1R, PHOSPHORYLATION, TISSUE SPECIFICITY, MUTAGENESIS OF PHE-29; ALA-34; ALA-38; PHE-41; ALA-42; TYR-48; PHE-68; PHE-72 AND ARG-555, VARIANT ALA-484.
  2. "Prediction of the coding sequences of unidentified human genes. XVI. The complete sequences of 150 new cDNA clones from brain which code for large proteins in vitro."
    Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.
    DNA Res. 7:65-73(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), VARIANT ALA-541.
    Tissue: Brain.
  3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    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.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Teratocarcinoma and Tongue.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 144-756 (ISOFORM 3), VARIANT ALA-484.
    Tissue: Mammary cancer.
  5. "The sequence and analysis of duplication-rich human chromosome 16."
    Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.
    , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
    Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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] OF 60-756 (ISOFORM 2).
    Tissue: Eye.
  7. "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: INTERACTION WITH INSR.
  8. "SH2-Balpha is an insulin-receptor adapter protein and substrate that interacts with the activation loop of the insulin-receptor kinase."
    Kotani K., Wilden P., Pillay T.S.
    Biochem. J. 335:103-109(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH INSR, PHOSPHORYLATION.
  9. "Platelet-derived growth factor (PDGF) stimulates the association of SH2-Bbeta with PDGF receptor and phosphorylation of SH2-Bbeta."
    Rui L., Carter-Su C.
    J. Biol. Chem. 273:21239-21245(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PDGF SIGNALING, INTERACTION WITH PDGFRA/B.
  10. "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: INTERACTION WITH INSR AND ISR1.
  11. "SH2-B family members differentially regulate JAK family tyrosine kinases."
    O'Brien K.B., O'Shea J.J., Carter-Su C.
    J. Biol. Chem. 277:8673-8681(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH JAK1; JAK2 AND JAK3, PHOSPHORYLATION.
  12. "Interaction of fibroblast growth factor receptor 3 and the adapter protein SH2-B. A role in STAT5 activation."
    Kong M., Wang C.S., Donoghue D.J.
    J. Biol. Chem. 277:15962-15970(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN FGF SIGNALING, INTERACTION WITH FGFR3.
  13. "SH2-B is a positive regulator of nerve growth factor-mediated activation of the Akt/Forkhead pathway in PC12 cells."
    Wang X., Chen L., Maures T.J., Herrington J., Carter-Su C.
    J. Biol. Chem. 279:133-141(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN NGF SIGNALING.
  14. "Interaction of SH2-Bbeta with RET is involved in signaling of GDNF-induced neurite outgrowth."
    Zhang Y., Zhu W., Wang Y.G., Liu X.J., Jiao L., Liu X., Zhang Z.H., Lu C.L., He C.
    J. Cell Sci. 119:1666-1676(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN GDNF SIGNALING, INTERACTION WITH RET.
  15. Cited for: FUNCTION IN RET SIGNALING, INTERACTION WITH PRKAR1A/RET.
  16. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
    Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
    J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-96, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  17. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-96, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.

Entry informationi

Entry nameiSH2B1_HUMAN
AccessioniPrimary (citable) accession number: Q9NRF2
Secondary accession number(s): A8K2R7
, Q96FK3, Q96SX3, Q9NRF1, Q9NRF3, Q9P2P7, Q9Y3Y3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: November 30, 2010
Last modified: September 3, 2014
This is version 109 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 16
    Human chromosome 16: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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