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Q9BRG2 (SH23A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 100. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
SH2 domain-containing protein 3A
Alternative name(s):
Novel SH2-containing protein 1
Gene names
Name:SH2D3A
Synonyms:NSP1
ORF Names:UNQ175/PRO201
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length576 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May play a role in JNK activation.

Subunit structure

Interacts with BCAR1. Ref.1

Tissue specificity

Weakly expressed in placenta, fetal kidney, fetal lung, adult pancreas, adult kidney and adult lung. Ref.1

Post-translational modification

Phosphorylated on tyrosine. Ref.1

Sequence similarities

Contains 1 SH2 domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 576576SH2 domain-containing protein 3A
PRO_0000233132

Regions

Domain15 – 114100SH2
Compositional bias259 – 2679Poly-Glu

Amino acid modifications

Modified residue1231Phosphoserine Ref.6 Ref.7
Modified residue1251Phosphoserine Ref.6 Ref.8
Modified residue1471Phosphoserine Ref.8
Modified residue1801Phosphoserine Ref.6 Ref.8

Natural variations

Natural variant321N → D. Ref.1 Ref.2
Corresponds to variant rs7258236 [ dbSNP | Ensembl ].
VAR_026054
Natural variant2231D → G.
Corresponds to variant rs12608960 [ dbSNP | Ensembl ].
VAR_051349
Natural variant2651E → G in a breast cancer sample; somatic mutation. Ref.9
VAR_035989

Experimental info

Mutagenesis951Y → F: Loss of phosphorylation. Ref.1
Mutagenesis2311Y → F: Weak phosphorylation. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9BRG2 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 2909F7632B61F18D

FASTA57663,093
        10         20         30         40         50         60 
MQVPQDGEDL AGQPWYHGLL SRQKAEALLQ QNGDFLVRAS GSRGGNPVIS CRWRGSALHF 

        70         80         90        100        110        120 
EVFRVALRPR PGRPTALFQL EDEQFPSIPA LVHSYMTGRR PLSQATGAVV SRPVTWQGPL 

       130        140        150        160        170        180 
RRSFSEDTLM DGPARIEPLR ARKWSNSQPA DLAHMGRSRE DPAGMEASTM PISALPRTSS 

       190        200        210        220        230        240 
DPVLLKAPAP LGTVADSLRA SDGQLQAKAP TKPPRTPSFE LPDASERPPT YCELVPRVPS 

       250        260        270        280        290        300 
VQGTSPSQSC PEPEAPWWEA EEDEEEENRC FTRPQAEISF CPHDAPSCLL GPQNRPLEPQ 

       310        320        330        340        350        360 
VLHTLRGLFL EHHPGSTALH LLLVDCQATG LLGVTRDQRG NMGVSSGLEL LTLPHGHHLR 

       370        380        390        400        410        420 
LELLERHQTL ALAGALAVLG CSGPLEERAA ALRGLVELAL ALRPGAAGDL PGLAAVMGAL 

       430        440        450        460        470        480 
LMPQVSRLEH TWRQLRRSHT EAALAFEQEL KPLMRALDEG AGPCDPGEVA LPHVAPMVRL 

       490        500        510        520        530        540 
LEGEEVAGPL DESCERLLRT LHGARHMVRD APKFRKVAAQ RLRGFRPNPE LREALTTGFV 

       550        560        570 
RRLLWGSRGA GAPRAERFEK FQRVLGVLSQ RLEPDR 

« Hide

References

« Hide 'large scale' references
[1]"NSP1 defines a novel family of adaptor proteins linking integrin and tyrosine kinase receptors to the c-Jun N-terminal kinase/stress-activated protein kinase signaling pathway."
Lu Y., Brush J., Stewart T.A.
J. Biol. Chem. 274:10047-10052(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, PHOSPHORYLATION, INTERACTION WITH BCAR1, MUTAGENESIS OF TYR-95 AND TYR-231, VARIANT ASP-32.
Tissue: Fetal kidney.
[2]"The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment."
Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E. expand/collapse author list , Heldens S., Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.
Genome Res. 13:2265-2270(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ASP-32.
[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].
Tissue: Trachea.
[4]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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].
Tissue: Placenta.
[6]"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-123; SER-125 AND SER-180, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[7]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-123, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[8]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125; SER-147 AND SER-180, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[9]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] GLY-265.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF124249 mRNA. Translation: AAD28244.1.
AY358406 mRNA. Translation: AAQ88772.1.
AK292781 mRNA. Translation: BAF85470.1.
CH471139 Genomic DNA. Translation: EAW69059.1.
BC006281 mRNA. Translation: AAH06281.1.
RefSeqNP_005481.2. NM_005490.2.
UniGeneHs.439645.

3D structure databases

ProteinModelPortalQ9BRG2.
SMRQ9BRG2. Positions 15-97.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115356. 7 interactions.
IntActQ9BRG2. 3 interactions.
MINTMINT-1498531.
STRING9606.ENSP00000245908.

PTM databases

PhosphoSiteQ9BRG2.

Polymorphism databases

DMDM74732879.

Proteomic databases

PaxDbQ9BRG2.
PRIDEQ9BRG2.

Protocols and materials databases

DNASU10045.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000245908; ENSP00000245908; ENSG00000125731.
GeneID10045.
KEGGhsa:10045.
UCSCuc002mft.3. human.

Organism-specific databases

CTD10045.
GeneCardsGC19M006752.
HGNCHGNC:16885. SH2D3A.
HPAHPA035722.
MIM604721. gene.
neXtProtNX_Q9BRG2.
PharmGKBPA38192.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG148579.
HOGENOMHOG000231595.
HOVERGENHBG053174.
InParanoidQ9BRG2.
OMAGCSGPLE.
OrthoDBEOG7J9VPN.
PhylomeDBQ9BRG2.
TreeFamTF323756.

Enzyme and pathway databases

SignaLinkQ9BRG2.

Gene expression databases

ArrayExpressQ9BRG2.
BgeeQ9BRG2.
CleanExHS_SH2D3A.
GenevestigatorQ9BRG2.

Family and domain databases

Gene3D1.10.840.10. 1 hit.
3.30.505.10. 1 hit.
InterProIPR023578. Ras_GEF_dom.
IPR001895. RasGRF_CDC25.
IPR000980. SH2.
[Graphical view]
PfamPF00617. RasGEF. 1 hit.
PF00017. SH2. 1 hit.
[Graphical view]
PRINTSPR00401. SH2DOMAIN.
SMARTSM00252. SH2. 1 hit.
[Graphical view]
SUPFAMSSF48366. SSF48366. 1 hit.
SSF55550. SSF55550. 1 hit.
PROSITEPS50001. SH2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiSH2D3A.
GenomeRNAi10045.
NextBio37943.
PROQ9BRG2.
SOURCESearch...

Entry information

Entry nameSH23A_HUMAN
AccessionPrimary (citable) accession number: Q9BRG2
Secondary accession number(s): A8K9R6, Q9Y2X4
Entry history
Integrated into UniProtKB/Swiss-Prot: May 2, 2006
Last sequence update: June 1, 2001
Last modified: April 16, 2014
This is version 100 of the entry and version 1 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM