Q15464 (SHB_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
SH2 domain-containing adapter protein B

Gene names

Name:

SHB

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	509 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Adapter protein which regulates several signal transduction cascades by linking activated receptors to downstream signaling components. May play a role in angiogenesis by regulating FGFR1, VEGFR2 and PDGFR signaling. May also play a role in T-cell antigen receptor/TCR signaling, interleukin-2 signaling, apoptosis and neuronal cells differentiation by mediating basic-FGF and NGF-induced signaling cascades. May also regulate IRS1 and IRS2 signaling in insulin-producing cells. Ref.6 Ref.7 Ref.8 Ref.10 Ref.11 Ref.14 Ref.16 Ref.17 Ref.18 Ref.19
Subunit structure	Interacts with PTPN11 By similarity. Interacts with phosphorylated 'Tyr-720' of the ligand-activated receptor PDGFRA via its SH2 domain. Interacts with the ligand-activated receptors PDGFRB, FGFR1, KDR/VEGFR2, IL2RB and IL2RG. Interacts with EPS8 and V-SRC. Interacts with GRB2 and GRAP. Interacts with CD3Z. Interacts with tyrosine-phosphorylated LAT upon T-cell antigen receptor activation. Interacts with PLCG1. Interacts with ZAP70, LCP2/SLP-76, VAV1 and GRAP2. Interacts with JAK1 and JAK3. Interacts with PTK2/FAK1. Interacts with CRK/CrKII. Interacts with IRS2. Ref.1 Ref.5 Ref.8 Ref.9 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18
Subcellular location	Cytoplasm. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Note: Associates with membrane lipid rafts upon TCR stimulation. Ref.1 Ref.14
Tissue specificity	Widely expressed. Ref.8
Domain	The SH2 domain preferentially binds phosphopeptides with the consensus sequence Y-[TVI]-X-L and mediates interaction with PDGFRA, PDGFRB, FGRFR1, IL2RB, IL2RG, CD3Z and CRK/CrKII.
Post-translational modification	Phosphorylated upon PDGFRA, PDGFRB, TCR, IL2 receptor, FGFR1 or VEGFR2 activation. Ref.9 Ref.20 Ref.21 Ref.22 Ref.23 Ref.24 Ref.25
Sequence similarities	Contains 1 SH2 domain.
Sequence caution	The sequence AAH94765.1 differs from that shown. Reason: Erroneous initiation. The sequence CAA53091.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Angiogenesis Apoptosis Differentiation
Cellular component	Cell membrane Cytoplasm Membrane
Coding sequence diversity	Alternative splicing
Domain	SH2 domain
Molecular function	Developmental protein
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	angiogenesis Inferred from electronic annotation. Source: UniProtKB-KW apoptotic process Inferred from electronic annotation. Source: UniProtKB-KW cell differentiation Inferred from electronic annotation. Source: UniProtKB-KW signal transduction Traceable author statement. Source: ProtInc
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	SH3/SH2 adaptor activity Traceable author statement. Source: ProtInc
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q15464-1)

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: Q15464-2)

The sequence of this isoform differs from the canonical sequence as follows:
     280-297: EFQRQESVRSQHKGIQLY → GLQEAWRHSPSGCFPVGP
     298-509: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 509	509	SH2 domain-containing adapter protein B		PRO_0000246324
Regions
	Domain	410 – 504	95	SH2
	Region	1 – 410	410	Mediates interaction with LAT, PTK2/FAK1, JAK1 and JAK3
Amino acid modifications
	Modified residue	114	1	Phosphotyrosine Ref.21 Ref.25
	Modified residue	156	1	Phosphoserine By similarity
	Modified residue	246	1	Phosphotyrosine Ref.20 Ref.21 Ref.25
	Modified residue	268	1	Phosphotyrosine Ref.21 Ref.25
	Modified residue	310	1	Phosphoserine Ref.24
	Modified residue	314	1	Phosphoserine Ref.23
	Modified residue	317	1	Phosphoserine Ref.23
	Modified residue	336	1	Phosphotyrosine Ref.21
	Modified residue	388	1	Phosphoserine Ref.22 Ref.23
Natural variations
	Alternative sequence	280 – 297	18	EFQRQ…GIQLY → GLQEAWRHSPSGCFPVGP in isoform 2.		VSP_019846
	Alternative sequence	298 – 509	212	Missing in isoform 2.		VSP_019847
Experimental info
	Mutagenesis	435	1	R → K: Loss of interaction with CD3Z. Alters LAT, PLCG1, VAV1 and LCP2 phosphorylation, MAP kinase signaling, Rac1 and JNK activation, intracellular calcium increase, activation of the nuclear factor for activation of T-cells and subsequent interleukin-2 expression which normally occur upon T-cells stimulation. Ref.8
	Sequence conflict	91 – 93	3	DFE → HFQ in CAA53091. Ref.1
	Sequence conflict	347	1	I → S in CAA53091. Ref.1
	Sequence conflict	445	1	S → P in CAA53091. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified July 25, 2006. Version 2. Checksum: 15C392A6EEB761D6	FASTA	509	55,042
	10 20 30 40 50 60 MAKWLNKYFS LGNSKTKSPP QPPRPDYREQ RRRGERPSQP PQAVPQASSA ASASCGPATA 70 80 90 100 110 120 SCFSASSGSL PDDSGSTSDL IRAYRAQKER DFEDPYNGPG SSLRKLRAMC RLDYCGGSGE 130 140 150 160 170 180 PGGVQRAFSA SSASGAAGCC CASSGAGAAA SSSSSSGSPH LYRSSSERRP ATPAEVRYIS 190 200 210 220 230 240 PKHRLIKVES AAGGGAGDPL GGACAGGRTW SPTACGGKKL LNKCAASAAE ESGAGKKDKV 250 260 270 280 290 300 TIADDYSDPF DAKNDLKSKA GKGESAGYME PYEAQRIMTE FQRQESVRSQ HKGIQLYDTP 310 320 330 340 350 360 YEPEGQSVDS DSESTVSPRL RESKLPQDDD RPADEYDQPW EWNRVTIPAL AAQFNGNEKR 370 380 390 400 410 420 QSSPSPSRDR RRQLRAPGGG FKPIKHGSPE FCGILGERVD PAVPLEKQIW YHGAISRGDA 430 440 450 460 470 480 ENLLRLCKEC SYLVRNSQTS KHDYSLSLRS NQGFMHMKLA KTKEKYVLGQ NSPPFDSVPE 490 500 VIHYYTTRKL PIKGAEHLSL LYPVAVRTL
	Isoform 2 [UniParc]. Checksum: 81ECB44A67B0D8AD	FASTA	297	30,703
	10 20 30 40 50 60 MAKWLNKYFS LGNSKTKSPP QPPRPDYREQ RRRGERPSQP PQAVPQASSA ASASCGPATA 70 80 90 100 110 120 SCFSASSGSL PDDSGSTSDL IRAYRAQKER DFEDPYNGPG SSLRKLRAMC RLDYCGGSGE 130 140 150 160 170 180 PGGVQRAFSA SSASGAAGCC CASSGAGAAA SSSSSSGSPH LYRSSSERRP ATPAEVRYIS 190 200 210 220 230 240 PKHRLIKVES AAGGGAGDPL GGACAGGRTW SPTACGGKKL LNKCAASAAE ESGAGKKDKV 250 260 270 280 290 TIADDYSDPF DAKNDLKSKA GKGESAGYME PYEAQRIMTG LQEAWRHSPS GCFPVGP

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Shb is a ubiquitously expressed Src homology 2 protein." Welsh M., Mares J., Karlsson T., Lavergne C., Breant B., Claesson-Welsh L. Oncogene 9:19-27(1994) [PubMed: 8302579] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, INTERACTION WITH PDGFRB. Tissue: Fetal brain.
[2]	"DNA sequence and analysis of human chromosome 9." Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L. , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I. Nature 429:369-374(2004) [PubMed: 15164053] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	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].
[4]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). Tissue: Placenta and Testis.
[5]	"Molecular interactions of the Src homology 2 domain protein Shb with phosphotyrosine residues, tyrosine kinase receptors and Src homology 3 domain proteins." Karlsson T., Songyang Z., Landgren E., Lavergne C., Di Fiore P.P., Anafi M., Pawson T., Cantley L.C., Claesson-Welsh L., Welsh M. Oncogene 10:1475-1483(1995) [PubMed: 7537362] [Abstract] Cited for: INTERACTION WITH PDGFRB; FGFR1; EPS8 AND V-SRC.
[6]	"Apoptosis of NIH3T3 cells overexpressing the Src homology 2 domain protein Shb." Karlsson T., Welsh M. Oncogene 13:955-961(1996) [PubMed: 8806685] [Abstract] Cited for: FUNCTION.
[7]	"The Src homology 2 domain protein Shb transmits basic fibroblast growth factor- and nerve growth factor-dependent differentiation signals in PC12 cells." Karlsson T., Kullander K., Welsh M. Cell Growth Differ. 9:757-766(1998) [PubMed: 9751119] [Abstract] Cited for: FUNCTION.
[8]	"Stimulation through the T cell receptor leads to interactions between SHB and several signaling proteins." Welsh M., Songyang Z., Frantz J.D., Trueb T., Reedquist K.A., Karlsson T., Miyazaki M., Cantley L.C., Band H., Shoelson S.E. Oncogene 16:891-901(1998) [PubMed: 9484780] [Abstract] Cited for: FUNCTION, TISSUE SPECIFICITY, INTERACTION WITH GRB2; GRAP AND CD3Z, MUTAGENESIS OF ARG-435.
[9]	"Requirement of the Src homology 2 domain protein Shb for T cell receptor-dependent activation of the interleukin-2 gene nuclear factor for activation of T cells element in Jurkat T cells." Lindholm C.K., Gylfe E., Zhang W., Samelson L.E., Welsh M. J. Biol. Chem. 274:28050-28057(1999) [PubMed: 10488157] [Abstract] Cited for: PHOSPHORYLATION, INTERACTION WITH LAT AND PLCG1.
[10]	"Endostatin-induced tyrosine kinase signaling through the Shb adaptor protein regulates endothelial cell apoptosis." Dixelius J., Larsson H., Sasaki T., Holmqvist K., Lu L., Engstroem A., Timpl R., Welsh M., Claesson-Welsh L. Blood 95:3403-3411(2000) [PubMed: 10828022] [Abstract] Cited for: FUNCTION.
[11]	"Platelet-derived growth factor-mediated signaling through the Shb adaptor protein: effects on cytoskeletal organization." Hooshmand-Rad R., Lu L., Heldin C.-H., Claesson-Welsh L., Welsh M. Exp. Cell Res. 257:245-254(2000) [PubMed: 10837138] [Abstract] Cited for: FUNCTION, INTERACTION WITH PDGFRA.
[12]	"NGF-dependent neurite outgrowth in PC12 cells overexpressing the Src homology 2-domain protein shb requires activation of the Rap1 pathway." Lu L., Anneren C., Reedquist K.A., Bos J.L., Welsh M. Exp. Cell Res. 259:370-377(2000) [PubMed: 10964504] [Abstract] Cited for: INTERACTION WITH CRK.
[13]	"IL-2 receptor signaling through the Shb adapter protein in T and NK cells." Lindholm C.K. Biochem. Biophys. Res. Commun. 296:929-936(2002) [PubMed: 12200137] [Abstract] Cited for: INTERACTION WITH IL2RB; IL2RG; JAK1 AND JAK3.
[14]	"Shb links SLP-76 and Vav with the CD3 complex in Jurkat T cells." Lindholm C.K., Henriksson M.L., Hallberg B., Welsh M. Eur. J. Biochem. 269:3279-3288(2002) [PubMed: 12084069] [Abstract] Cited for: FUNCTION, INTERACTION WITH ZAP70; LCP2; VAV1 AND GRAP2, SUBCELLULAR LOCATION.
[15]	"The Shb adaptor protein binds to tyrosine 766 in the FGFR-1 and regulates the Ras/MEK/MAPK pathway via FRS2 phosphorylation in endothelial cells." Cross M.J., Lu L., Magnusson P., Nyqvist D., Holmqvist K., Welsh M., Claesson-Welsh L. Mol. Biol. Cell 13:2881-2893(2002) [PubMed: 12181353] [Abstract] Cited for: INTERACTION WITH FGFR1.
[16]	"Overexpression of the Shb SH2 domain-protein in insulin-producing cells leads to altered signaling through the IRS-1 and IRS-2 proteins." Welsh N., Makeeva N., Welsh M. Mol. Med. 8:695-704(2002) [PubMed: 12520086] [Abstract] Cited for: FUNCTION, INTERACTION WITH IRS2.
[17]	"The Shb adaptor protein causes Src-dependent cell spreading and activation of focal adhesion kinase in murine brain endothelial cells." Holmqvist K., Cross M.J., Riley D., Welsh M. Cell. Signal. 15:171-179(2003) [PubMed: 12464388] [Abstract] Cited for: FUNCTION, INTERACTION WITH PTK2/FAK1.
[18]	"The adaptor protein shb binds to tyrosine 1175 in vascular endothelial growth factor (VEGF) receptor-2 and regulates VEGF-dependent cellular migration." Holmqvist K., Cross M.J., Rolny C., Haegerkvist R., Rahimi N., Matsumoto T., Claesson-Welsh L., Welsh M. J. Biol. Chem. 279:22267-22275(2004) [PubMed: 15026417] [Abstract] Cited for: FUNCTION, INTERACTION WITH KDR.
[19]	"Shb promotes blood vessel formation in embryoid bodies by augmenting vascular endothelial growth factor receptor-2 and platelet-derived growth factor receptor-beta signaling." Rolny C., Lu L., Aagren N., Nilsson I., Roe C., Webb G.C., Welsh M. Exp. Cell Res. 308:381-393(2005) [PubMed: 15919073] [Abstract] Cited for: FUNCTION.
[20]	"Time-resolved mass spectrometry of tyrosine phosphorylation sites in the epidermal growth factor receptor signaling network reveals dynamic modules." Zhang Y., Wolf-Yadlin A., Ross P.L., Pappin D.J., Rush J., Lauffenburger D.A., White F.M. Mol. Cell. Proteomics 4:1240-1250(2005) [PubMed: 15951569] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-246, MASS SPECTROMETRY. Tissue: Mammary epithelium.
[21]	"Multiple reaction monitoring for robust quantitative proteomic analysis of cellular signaling networks." Wolf-Yadlin A., Hautaniemi S., Lauffenburger D.A., White F.M. Proc. Natl. Acad. Sci. U.S.A. 104:5860-5865(2007) [PubMed: 17389395] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-114; TYR-246; TYR-268 AND TYR-336, MASS SPECTROMETRY. Tissue: Mammary epithelium.
[22]	"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: 18220336] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-388, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[23]	"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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-314; SER-317 AND SER-388, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[24]	"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach." Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S. Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-310, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[25]	"An extensive survey of tyrosine phosphorylation revealing new sites in human mammary epithelial cells." Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A., Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D., Wiley H.S., Qian W.-J. J. Proteome Res. 8:3852-3861(2009) [PubMed: 19534553] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-114; TYR-246 AND TYR-268, MASS SPECTROMETRY. Tissue: Mammary epithelium.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X75342 mRNA. Translation: CAA53091.1. Different initiation. AL583849, AL138752, AL161448 Genomic DNA. Translation: CAH73120.1. AL161448, AL138752, AL583849 Genomic DNA. Translation: CAH73192.1. AL138752, AL161448, AL583849 Genomic DNA. Translation: CAI13876.1. CH471071 Genomic DNA. Translation: EAW58254.1. CH471071 Genomic DNA. Translation: EAW58255.1. BC094765 mRNA. Translation: AAH94765.1. Different initiation. BC136581 mRNA. Translation: AAI36582.1. BC136582 mRNA. Translation: AAI36583.1.
IPI	IPI00017578. IPI00604688.
PIR	I38228.
RefSeq	NP_003019.2. NM_003028.2.
UniGene	Hs.521482.
3D structure databases
ProteinModelPortal	Q15464.
SMR	Q15464. Positions 403-507.
ModBase	Search...
Protein-protein interaction databases
STRING	Q15464.
PTM databases
PhosphoSite	Q15464.
Polymorphism databases
DMDM	110816415.
Proteomic databases
PRIDE	Q15464.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000377707; ENSP00000366936; ENSG00000107338.
GeneID	6461.
KEGG	hsa:6461.
NMPDR	fig|9606.3.peg.31300.
UCSC	uc004aax.1. human.
Organism-specific databases
CTD	6461.
GeneCards	GC09M037909.
H-InvDB	HIX0008049. HIX0079163.
HGNC	HGNC:10838. SHB.
HPA	CAB010161.
MIM	600314. gene.
neXtProt	NX_Q15464.
PharmGKB	PA35744.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG19760.
GeneTree	ENSGT00390000015203.
HOGENOM	HBG716018.
HOVERGEN	HBG066172.
InParanoid	Q15464.
OMA	DPLGGAC.
OrthoDB	EOG45756M.
PhylomeDB	Q15464.
Enzyme and pathway databases
Pathway_Interaction_DB	pdgfrapathway. PDGFR-alpha signaling pathway. pdgfrbpathway. PDGFR-beta signaling pathway. vegfr1_2_pathway. Signaling events mediated by VEGFR1 and VEGFR2.
Gene expression databases
ArrayExpress	Q15464.
Bgee	Q15464.
CleanEx	HS_SHB.
Genevestigator	Q15464.
GermOnline	ENSG00000107338. Homo sapiens.
Family and domain databases
InterPro	IPR000980. SH2. [Graphical view]
Gene3D	G3DSA:3.30.505.10. SH2. 1 hit.
Pfam	PF00017. SH2. 1 hit. [Graphical view]
PRINTS	PR00401. SH2DOMAIN.
SMART	SM00252. SH2. 1 hit. [Graphical view]
PROSITE	PS50001. SH2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	25105.
SOURCE	Search...

Entry information

Entry name

SHB_HUMAN

Accession

Primary (citable) accession number: Q15464
Secondary accession number(s): B9EGM0 , D3DRQ5, Q504U5, Q5VUM8

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 25, 2006
Last sequence update:	July 25, 2006
Last modified:	January 25, 2012
This is version 81 of the entry and version 2 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.