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Q9NRF2 (SH2B1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 105. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:SH2B1
Synonyms:KIAA1299, SH2B
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length756 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Isoforms seem to be differentially involved in IGF-I and PDGF-induced mitogenesis By similarity. Ref.1 Ref.8 Ref.9 Ref.12 Ref.13 Ref.14 Ref.15

Subunit structure

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. Ref.1 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.14 Ref.15

Subcellular location

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

Tissue specificity

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

Post-translational modification

Phosphorylated on tyrosine residues in response to receptor kinase stimulation. Phosphorylated by RET. Ref.1 Ref.8 Ref.11

Sequence similarities

Belongs to the SH2B adapter family.

Contains 1 PH domain.

Contains 1 SH2 domain.

Sequence caution

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.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

INSRP062136EBI-310491,EBI-475899

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9NRF2-1)

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.
Isoform 2 (identifier: Q9NRF2-2)

Also known as: Beta;

The sequence of this isoform differs from the canonical sequence as follows:
     633-756: EPTTSHDPPQ...RAINNQYSFV → GREQAGSHAG...ASDCVTDHLP
Isoform 3 (identifier: Q9NRF2-3)

Also known as: Gamma;

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 756756SH2B adapter protein 1
PRO_0000323593

Regions

Domain267 – 376110PH
Domain527 – 62599SH2
Region1 – 555555Interaction with JAK2 (low-affinity binding; independent of JAK2 phosphorylation) By similarity
Region24 – 8562Required for self-association
Region85 – 196112Interaction with RAC1 By similarity
Region100 – 243144Required for NGF signaling By similarity
Region224 – 23310Required for nuclear localization By similarity

Amino acid modifications

Modified residue881Phosphoserine
Modified residue961Phosphoserine Ref.16 Ref.17
Modified residue4391Phosphotyrosine; by JAK1, JAK2 and PDGFR By similarity
Modified residue4941Phosphotyrosine; by JAK1, JAK2 By similarity
Modified residue6241Phosphotyrosine

Natural variations

Alternative sequence633 – 756124EPTTS…QYSFV → GREQAGSHAGVCEGDGCHPD ASCTLMPFGASDCVTDHLP in isoform 2.
VSP_032027
Alternative sequence633 – 756124EPTTS…QYSFV → GEQSRSAGEEVPVHPRSEAG SRLGAMRGCAREMDATPMPP APSCPSERVTV in isoform 3.
VSP_032028
Natural variant4841T → A. Ref.1 Ref.4
Corresponds to variant rs7498665 [ dbSNP | Ensembl ].
VAR_039550
Natural variant5411V → A. Ref.2
Corresponds to variant rs17850682 [ dbSNP | Ensembl ].
VAR_039551

Experimental info

Mutagenesis291F → R: Abolishes self-association and interaction with INSR and IGF1R. Ref.1
Mutagenesis341A → D: Abolishes self-association and interaction with INSR and IGF1R. Ref.1
Mutagenesis381A → D: Abolishes self-association and interaction with INSR and IGF1R. Ref.1
Mutagenesis411F → A: Abolishes self-association and interaction with INSR and IGF1R. Ref.1
Mutagenesis421A → D: Abolishes self-association and interaction with INSR and IGF1R. Ref.1
Mutagenesis481Y → A: Abolishes self-association and interaction with INSR and IGF1R. Ref.1
Mutagenesis681F → A: Abolishes self-association and interaction with INSR and IGF1R. Ref.1
Mutagenesis721F → A: Abolishes self-association and interaction with INSR and IGF1R. Ref.1
Mutagenesis5551R → A: Abolishes self-association and interaction with INSR and IGF1R. Ref.1
Sequence conflict1971N → D in BAF83021. Ref.3
Sequence conflict5191D → G in BAF83021. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (Alpha) [UniParc].

Last modified November 30, 2010. Version 3.
Checksum: CF680B57114CB1D3

FASTA75679,366
        10         20         30         40         50         60 
MNGAPSPEDG ASPSSPPLPP PPPPSWREFC ESHARAAALD FARRFRLYLA SHPQYAGPGA 

        70         80         90        100        110        120 
EAAFSRRFAE LFLQHFEAEV ARASGSLSPP ILAPLSPGAE ISPHDLSLES CRVGGPLAVL 

       130        140        150        160        170        180 
GPSRSSEDLA GPLPSSVSSS STTSSKPKLK KRFSLRSVGR SVRGSVRGIL QWRGTVDPPS 

       190        200        210        220        230        240 
SAGPLETSSG PPVLGGNSNS NSSGGAGTVG RGLVSDGTSP GERWTHRFER LRLSRGGGAL 

       250        260        270        280        290        300 
KDGAGMVQRE ELLSFMGAEE AAPDPAGVGR GGGVAGPPSG GGGQPQWQKC RLLLRSEGEG 

       310        320        330        340        350        360 
GGGSRLEFFV PPKASRPRLS IPCSSITDVR TTTALEMPDR ENTFVVKVEG PSEYIMETVD 

       370        380        390        400        410        420 
AQHVKAWVSD IQECLSPGPC PATSPRPMTL PLAPGTSFLT RENTDSLELS CLNHSESLPS 

       430        440        450        460        470        480 
QDLLLGPSES NDRLSQGAYG GLSDRPSASI SPSSASIAAS HFDSMELLPP ELPPRIPIEE 

       490        500        510        520        530        540 
GPPTGTVHPL SAPYPPLDTP ETATGSFLFQ GEPEGGEGDQ PLSGYPWFHG MLSRLKAAQL 

       550        560        570        580        590        600 
VLTGGTGSHG VFLVRQSETR RGEYVLTFNF QGKAKHLRLS LNEEGQCRVQ HLWFQSIFDM 

       610        620        630        640        650        660 
LEHFRVHPIP LESGGSSDVV LVSYVPSSQR QQEPTTSHDP PQPPEPPSWT DPPQPGAEEA 

       670        680        690        700        710        720 
SRAPEVAAAA AAAAKERQEK EKAGGGGVPE ELVPVVELVP VVELEEAIAP GSEAQGAGSG 

       730        740        750 
GDAGVPPMVQ LQQSPLGGDG EEGGHPRAIN NQYSFV 

« Hide

Isoform 2 (Beta) [UniParc].

Checksum: 3EAD9A95F370FD94
Show »

FASTA67170,781
Isoform 3 (Gamma) [UniParc].

Checksum: 353155178527B5A7
Show »

FASTA68372,188

References

« Hide 'large scale' references
[1]"Kinase activation through dimerization by human SH2-B."
Nishi M., Werner E.D., Oh B.C., Frantz J.D., Dhe-Paganon S., Hansen L., Lee J., Shoelson S.E.
Mol. Cell. Biol. 25:2607-2621(2005) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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]"SH2B1beta adaptor is a key enhancer of RET tyrosine kinase signaling."
Donatello S., Fiorino A., Degl'Innocenti D., Alberti L., Miranda C., Gorla L., Bongarzone I., Rizzetti M.G., Pierotti M.A., Borrello M.G.
Oncogene 26:6546-6559(2007) [PubMed] [Europe PMC] [Abstract]
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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-96, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRT08662.
RefSeqNP_001139267.1. NM_001145795.1.
NP_001139268.1. NM_001145796.1.
NP_001139269.1. NM_001145797.1.
NP_001139284.1. NM_001145812.1.
NP_056318.2. NM_015503.2.
UniGeneHs.15744.

3D structure databases

ProteinModelPortalQ9NRF2.
SMRQ9NRF2. Positions 24-82, 247-379, 520-654.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid117455. 14 interactions.
IntActQ9NRF2. 5 interactions.
MINTMINT-1494470.
STRING9606.ENSP00000337163.

PTM databases

PhosphoSiteQ9NRF2.

Polymorphism databases

DMDM313104186.

Proteomic databases

PaxDbQ9NRF2.
PRIDEQ9NRF2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000322610; ENSP00000321221; ENSG00000178188. [Q9NRF2-1]
ENST00000337120; ENSP00000337163; ENSG00000178188. [Q9NRF2-2]
ENST00000359285; ENSP00000352232; ENSG00000178188. [Q9NRF2-3]
ENST00000395532; ENSP00000378903; ENSG00000178188. [Q9NRF2-2]
GeneID25970.
KEGGhsa:25970.
UCSCuc002dri.3. human. [Q9NRF2-1]
uc002drj.3. human. [Q9NRF2-3]
uc002drk.3. human. [Q9NRF2-2]

Organism-specific databases

CTD25970.
GeneCardsGC16P028875.
H-InvDBHIX0017272.
HGNCHGNC:30417. SH2B1.
MIM608937. gene.
neXtProtNX_Q9NRF2.
Orphanet261222. Distal 16p11.2 microdeletion syndrome.
261197. Proximal 16p11.2 microdeletion syndrome.
329249. Severe early-onset obesity-insulin resistance syndrome due to SH2B1 deficiency.
PharmGKBPA145148084.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG77816.
HOVERGENHBG006707.
InParanoidQ9NRF2.
KOK12459.
OMASPGVEIP.
OrthoDBEOG7034GG.
PhylomeDBQ9NRF2.
TreeFamTF323184.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_604. Hemostasis.
REACT_6900. Immune System.
SignaLinkQ9NRF2.

Gene expression databases

ArrayExpressQ9NRF2.
BgeeQ9NRF2.
CleanExHS_SH2B1.
GenevestigatorQ9NRF2.

Family and domain databases

Gene3D2.30.29.30. 1 hit.
3.30.505.10. 1 hit.
InterProIPR011993. PH_like_dom.
IPR015012. Phe_ZIP.
IPR001849. Pleckstrin_homology.
IPR000980. SH2.
[Graphical view]
PfamPF00169. PH. 1 hit.
PF08916. Phe_ZIP. 1 hit.
PF00017. SH2. 1 hit.
[Graphical view]
PRINTSPR00401. SH2DOMAIN.
SMARTSM00233. PH. 1 hit.
SM00252. SH2. 1 hit.
[Graphical view]
SUPFAMSSF109805. SSF109805. 1 hit.
SSF55550. SSF55550. 1 hit.
PROSITEPS50001. SH2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiSH2B1.
GenomeRNAi25970.
NextBio47602.
PROQ9NRF2.
SOURCESearch...

Entry information

Entry nameSH2B1_HUMAN
AccessionPrimary (citable) accession number: Q9NRF2
Secondary accession number(s): A8K2R7 expand/collapse secondary AC list , Q96FK3, Q96SX3, Q9NRF1, Q9NRF3, Q9P2P7, Q9Y3Y3
Entry history
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: November 30, 2010
Last modified: April 16, 2014
This is version 105 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

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SIMILARITY comments

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