Q9BRG2 (SH23A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
SH2 domain-containing protein 3A

Alternative name(s):
Novel SH2-containing protein 1

Gene names

Name:	SH2D3A
Synonyms:	NSP1
ORF Names:	UNQ175/PRO201

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	576 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

Ontologies

Keywords
Coding sequence diversity	Polymorphism
Domain	SH2 domain
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	JNK cascade Traceable author statement Ref.1. Source: ProtInc small GTPase mediated signal transduction Inferred from electronic annotation. Source: InterPro
Cellular_component	intracellular Inferred from electronic annotation. Source: InterPro
Molecular_function	SH3/SH2 adaptor activity Traceable author statement Ref.1. Source: ProtInc guanyl-nucleotide exchange factor activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 576	576	SH2 domain-containing protein 3A		PRO_0000233132
Regions
	Domain	15 – 114	100	SH2
	Compositional bias	259 – 267	9	Poly-Glu
Amino acid modifications
	Modified residue	123	1	Phosphoserine Ref.6 Ref.7
	Modified residue	125	1	Phosphoserine Ref.6 Ref.8
	Modified residue	147	1	Phosphoserine Ref.8
	Modified residue	180	1	Phosphoserine Ref.6 Ref.8
Natural variations
	Natural variant	32	1	N → D. Ref.1 Ref.2 Corresponds to variant rs7258236 [ dbSNP | Ensembl ].		VAR_026054
	Natural variant	223	1	D → G. Corresponds to variant rs12608960 [ dbSNP | Ensembl ].		VAR_051349
	Natural variant	265	1	E → G in a breast cancer sample; somatic mutation. Ref.9		VAR_035989
Experimental info
	Mutagenesis	95	1	Y → F: Loss of phosphorylation. Ref.1
	Mutagenesis	231	1	Y → F: Weak phosphorylation. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q9BRG2 [UniParc]. Last modified June 1, 2001. Version 1. Checksum: 2909F7632B61F18D	FASTA	576	63,093
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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. , 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY.
[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. , 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.
IPI	IPI00305020.
RefSeq	NP_005481.2. NM_005490.2.
UniGene	Hs.439645.
3D structure databases
ProteinModelPortal	Q9BRG2.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9BRG2. 1 interaction.
MINT	MINT-1498531.
STRING	9606.ENSP00000245908.
PTM databases
PhosphoSite	Q9BRG2.
Polymorphism databases
DMDM	74732879.
Proteomic databases
PaxDb	Q9BRG2.
PRIDE	Q9BRG2.
Protocols and materials databases
DNASU	10045.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000245908; ENSP00000245908; ENSG00000125731.
GeneID	10045.
KEGG	hsa:10045.
UCSC	uc002mft.3. human.
Organism-specific databases
CTD	10045.
GeneCards	GC19M006752.
HGNC	HGNC:16885. SH2D3A.
HPA	HPA035722.
MIM	604721. gene.
neXtProt	NX_Q9BRG2.
PharmGKB	PA38192.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG148579.
HOGENOM	HOG000231595.
HOVERGEN	HBG053174.
InParanoid	Q9BRG2.
OMA	GCSGPLE.
OrthoDB	EOG418BNC.
PhylomeDB	Q9BRG2.
Gene expression databases
ArrayExpress	Q9BRG2.
Bgee	Q9BRG2.
CleanEx	HS_SH2D3A.
Genevestigator	Q9BRG2.
GermOnline	ENSG00000125731. Homo sapiens.
Family and domain databases
Gene3D	1.10.840.10. 1 hit. 3.30.505.10. 1 hit.
InterPro	IPR023578. Ras_GEF_dom. IPR001895. RasGRF_CDC25. IPR000980. SH2. [Graphical view]
Pfam	PF00617. RasGEF. 1 hit. PF00017. SH2. 1 hit. [Graphical view]
PRINTS	PR00401. SH2DOMAIN.
SMART	SM00252. SH2. 1 hit. [Graphical view]
SUPFAM	SSF48366. Ras_GEF. 1 hit.
PROSITE	PS50001. SH2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	10045.
NextBio	37943.
SOURCE	Search...

Entry information

Entry name

SH23A_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 92 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.