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Q15464

- SHB_HUMAN

UniProt

Q15464 - SHB_HUMAN

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Protein
SH2 domain-containing adapter protein B
Gene
SHB
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.10 Publications

GO - Molecular functioni

  1. SH3/SH2 adaptor activity Source: ProtInc
  2. protein binding Source: IntAct

GO - Biological processi

  1. B cell proliferation Source: Ensembl
  2. angiogenesis Source: UniProtKB-KW
  3. apoptotic process Source: UniProtKB-KW
  4. cell differentiation Source: UniProtKB-KW
  5. hemopoiesis Source: Ensembl
  6. negative regulation of oocyte maturation Source: Ensembl
  7. positive regulation of signal transduction Source: GOC
  8. signal transduction Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Angiogenesis, Apoptosis, Differentiation

Enzyme and pathway databases

SignaLinkiQ15464.

Names & Taxonomyi

Protein namesi
Recommended name:
SH2 domain-containing adapter protein B
Gene namesi
Name:SHB
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 9

Organism-specific databases

HGNCiHGNC:10838. SHB.

Subcellular locationi

Cytoplasm. Cell membrane; Peripheral membrane protein; Cytoplasmic side
Note: Associates with membrane lipid rafts upon TCR stimulation.2 Publications

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
  2. plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi435 – 4351R → 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. 1 Publication

Organism-specific databases

PharmGKBiPA35744.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 509509SH2 domain-containing adapter protein B
PRO_0000246324Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei317 – 3171Phosphoserine1 Publication
Modified residuei388 – 3881Phosphoserine1 Publication

Post-translational modificationi

Phosphorylated upon PDGFRA, PDGFRB, TCR, IL2 receptor, FGFR1 or VEGFR2 activation.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ15464.
PaxDbiQ15464.
PRIDEiQ15464.

PTM databases

PhosphoSiteiQ15464.

Expressioni

Tissue specificityi

Widely expressed.1 Publication

Gene expression databases

BgeeiQ15464.
CleanExiHS_SHB.
GenevestigatoriQ15464.

Organism-specific databases

HPAiCAB010161.
HPA049911.

Interactioni

Subunit structurei

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 IRS2.12 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ABL1P005195EBI-4402156,EBI-375543
KITP107212EBI-4402156,EBI-1379503
METP085814EBI-4402156,EBI-1039152

Protein-protein interaction databases

BioGridi112358. 16 interactions.
IntActiQ15464. 8 interactions.
MINTiMINT-7046528.
STRINGi9606.ENSP00000366936.

Structurei

3D structure databases

ProteinModelPortaliQ15464.
SMRiQ15464. Positions 405-487.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini410 – 50495SH2
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 410410Mediates interaction with LAT, PTK2/FAK1, JAK1 and JAK3
Add
BLAST

Domaini

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.

Sequence similaritiesi

Contains 1 SH2 domain.

Keywords - Domaini

SH2 domain

Phylogenomic databases

eggNOGiNOG80632.
HOGENOMiHOG000038038.
HOVERGENiHBG066172.
InParanoidiQ15464.
OMAiRPDYREQ.
OrthoDBiEOG793B9C.
PhylomeDBiQ15464.
TreeFamiTF325799.

Family and domain databases

Gene3Di3.30.505.10. 1 hit.
InterProiIPR000980. SH2.
[Graphical view]
PfamiPF00017. SH2. 1 hit.
[Graphical view]
PRINTSiPR00401. SH2DOMAIN.
SMARTiSM00252. SH2. 1 hit.
[Graphical view]
SUPFAMiSSF55550. SSF55550. 1 hit.
PROSITEiPS50001. SH2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q15464-1) [UniParc]FASTAAdd to Basket

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

MAKWLNKYFS LGNSKTKSPP QPPRPDYREQ RRRGERPSQP PQAVPQASSA    50
ASASCGPATA SCFSASSGSL PDDSGSTSDL IRAYRAQKER DFEDPYNGPG 100
SSLRKLRAMC RLDYCGGSGE PGGVQRAFSA SSASGAAGCC CASSGAGAAA 150
SSSSSSGSPH LYRSSSERRP ATPAEVRYIS PKHRLIKVES AAGGGAGDPL 200
GGACAGGRTW SPTACGGKKL LNKCAASAAE ESGAGKKDKV TIADDYSDPF 250
DAKNDLKSKA GKGESAGYME PYEAQRIMTE FQRQESVRSQ HKGIQLYDTP 300
YEPEGQSVDS DSESTVSPRL RESKLPQDDD RPADEYDQPW EWNRVTIPAL 350
AAQFNGNEKR QSSPSPSRDR RRQLRAPGGG FKPIKHGSPE FCGILGERVD 400
PAVPLEKQIW YHGAISRGDA ENLLRLCKEC SYLVRNSQTS KHDYSLSLRS 450
NQGFMHMKLA KTKEKYVLGQ NSPPFDSVPE VIHYYTTRKL PIKGAEHLSL 500
LYPVAVRTL 509
Length:509
Mass (Da):55,042
Last modified:July 25, 2006 - v2
Checksum:i15C392A6EEB761D6
GO
Isoform 2 (identifier: Q15464-2) [UniParc]FASTAAdd to Basket

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

Note: No experimental confirmation available.

Show »
Length:297
Mass (Da):30,703
Checksum:i81ECB44A67B0D8AD
GO

Sequence cautioni

The sequence AAH94765.1 differs from that shown. Reason: Erroneous initiation.
The sequence CAA53091.1 differs from that shown. Reason: Erroneous initiation.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei280 – 29718EFQRQ…GIQLY → GLQEAWRHSPSGCFPVGP in isoform 2.
VSP_019846Add
BLAST
Alternative sequencei298 – 509212Missing in isoform 2.
VSP_019847Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti91 – 933DFE → HFQ in CAA53091. 1 Publication
Sequence conflicti347 – 3471I → S in CAA53091. 1 Publication
Sequence conflicti445 – 4451S → P in CAA53091. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS43806.1. [Q15464-1]
PIRiI38228.
RefSeqiNP_003019.2. NM_003028.2. [Q15464-1]
UniGeneiHs.521482.

Genome annotation databases

EnsembliENST00000377700; ENSP00000366929; ENSG00000107338. [Q15464-2]
ENST00000377707; ENSP00000366936; ENSG00000107338. [Q15464-1]
GeneIDi6461.
KEGGihsa:6461.
UCSCiuc004aax.3. human. [Q15464-1]

Polymorphism databases

DMDMi110816415.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS43806.1. [Q15464-1 ]
PIRi I38228.
RefSeqi NP_003019.2. NM_003028.2. [Q15464-1 ]
UniGenei Hs.521482.

3D structure databases

ProteinModelPortali Q15464.
SMRi Q15464. Positions 405-487.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 112358. 16 interactions.
IntActi Q15464. 8 interactions.
MINTi MINT-7046528.
STRINGi 9606.ENSP00000366936.

PTM databases

PhosphoSitei Q15464.

Polymorphism databases

DMDMi 110816415.

Proteomic databases

MaxQBi Q15464.
PaxDbi Q15464.
PRIDEi Q15464.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000377700 ; ENSP00000366929 ; ENSG00000107338 . [Q15464-2 ]
ENST00000377707 ; ENSP00000366936 ; ENSG00000107338 . [Q15464-1 ]
GeneIDi 6461.
KEGGi hsa:6461.
UCSCi uc004aax.3. human. [Q15464-1 ]

Organism-specific databases

CTDi 6461.
GeneCardsi GC09M037953.
H-InvDB HIX0008049.
HIX0079163.
HIX0189186.
HGNCi HGNC:10838. SHB.
HPAi CAB010161.
HPA049911.
MIMi 600314. gene.
neXtProti NX_Q15464.
PharmGKBi PA35744.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG80632.
HOGENOMi HOG000038038.
HOVERGENi HBG066172.
InParanoidi Q15464.
OMAi RPDYREQ.
OrthoDBi EOG793B9C.
PhylomeDBi Q15464.
TreeFami TF325799.

Enzyme and pathway databases

SignaLinki Q15464.

Miscellaneous databases

ChiTaRSi SHB. human.
GeneWikii SHB_(gene).
GenomeRNAii 6461.
NextBioi 25105.
PROi Q15464.
SOURCEi Search...

Gene expression databases

Bgeei Q15464.
CleanExi HS_SHB.
Genevestigatori Q15464.

Family and domain databases

Gene3Di 3.30.505.10. 1 hit.
InterProi IPR000980. SH2.
[Graphical view ]
Pfami PF00017. SH2. 1 hit.
[Graphical view ]
PRINTSi PR00401. SH2DOMAIN.
SMARTi SM00252. SH2. 1 hit.
[Graphical view ]
SUPFAMi SSF55550. SSF55550. 1 hit.
PROSITEi PS50001. SH2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  20. "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-388, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  21. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-317, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  22. "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] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  23. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.

Entry informationi

Entry nameiSHB_HUMAN
AccessioniPrimary (citable) accession number: Q15464
Secondary accession number(s): B9EGM0
, D3DRQ5, Q504U5, Q5VUM8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 25, 2006
Last sequence update: July 25, 2006
Last modified: July 9, 2014
This is version 106 of the entry and version 2 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 9
    Human chromosome 9: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi