Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

SHC SH2 domain-binding protein 1

Gene

SHCBP1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

May play a role in signaling pathways governing cellular proliferation, cell growth and differentiation. May be a component of a novel signaling pathway downstream of Shc. Acts as a positive regulator of FGF signaling in neural progenitor cells (By similarity).By similarity

GO - Biological processi

Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
SHC SH2 domain-binding protein 1
Gene namesi
Name:SHCBP1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 16

Organism-specific databases

HGNCiHGNC:29547. SHCBP1.

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134931125.

Polymorphism and mutation databases

BioMutaiSHCBP1.
DMDMi296452958.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 672671SHC SH2 domain-binding protein 1PRO_0000076315Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineCombined sources
Modified residuei5 – 51PhosphoserineCombined sources
Modified residuei7 – 71PhosphothreonineCombined sources
Modified residuei31 – 311PhosphoserineCombined sources
Modified residuei42 – 421PhosphoserineCombined sources
Modified residuei44 – 441PhosphoserineCombined sources
Modified residuei47 – 471PhosphoserineCombined sources
Modified residuei273 – 2731PhosphoserineCombined sources
Modified residuei634 – 6341PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ8NEM2.
MaxQBiQ8NEM2.
PaxDbiQ8NEM2.
PRIDEiQ8NEM2.

PTM databases

iPTMnetiQ8NEM2.
PhosphoSiteiQ8NEM2.

Expressioni

Gene expression databases

BgeeiQ8NEM2.
CleanExiHS_SHCBP1.
ExpressionAtlasiQ8NEM2. baseline and differential.
GenevisibleiQ8NEM2. HS.

Organism-specific databases

HPAiHPA048876.

Interactioni

Subunit structurei

Interacts directly with isoform p52shc of SHC1 via its SH2 domain. Interacts with TRIM71; leading to enhance SHCBP1 protein stability (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
PRKCBP057712EBI-744700,EBI-706216

Protein-protein interaction databases

BioGridi122898. 31 interactions.
IntActiQ8NEM2. 12 interactions.
MINTiMINT-1450223.
STRINGi9606.ENSP00000306473.

Structurei

3D structure databases

ProteinModelPortaliQ8NEM2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati428 – 45124PbH1 1Add
BLAST
Repeati452 – 47322PbH1 2Add
BLAST
Repeati474 – 49623PbH1 3Add
BLAST
Repeati497 – 51822PbH1 4Add
BLAST
Repeati526 – 54823PbH1 5Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi211 – 2166Poly-Glu

Sequence similaritiesi

Contains 5 PbH1 repeats.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiENOG410IIV2. Eukaryota.
ENOG410XXTE. LUCA.
GeneTreeiENSGT00530000063807.
HOGENOMiHOG000154313.
HOVERGENiHBG060212.
InParanoidiQ8NEM2.
OMAiPERTGWA.
OrthoDBiEOG7VMP4V.
PhylomeDBiQ8NEM2.
TreeFamiTF329196.

Family and domain databases

Gene3Di2.160.20.10. 1 hit.
InterProiIPR006626. PbH1.
IPR012334. Pectin_lyas_fold.
IPR011050. Pectin_lyase_fold/virulence.
[Graphical view]
SMARTiSM00710. PbH1. 5 hits.
[Graphical view]
SUPFAMiSSF51126. SSF51126. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q8NEM2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MADGSLTGGG LEAAAMAPER MGWAVEQELA SLEKGLFQDE DSCSDCSYRD
60 70 80 90 100
KPGSSLQSFM PEGKTFFPEI FQTNQLLFYE RFRAYQDYIL ADCKASEVQE
110 120 130 140 150
FTAEFLEKVL EPSGWRAVWH TNVFKVLVEI TDVDFAALKA VVRLAEPYLC
160 170 180 190 200
DSQVSTFTME CMKELLDLKE HRLPLQELWV VFDDSGVFDQ TALAIEHVRF
210 220 230 240 250
FYQNIWRSWD EEEEDEYDYF VRCVEPRLRL HYDILEDRVP SGLIVDYHNL
260 270 280 290 300
LSQCEESYRK FLNLRSSLSN CNSDSEQENI SMVEGLKLYS EMEQLKQKLK
310 320 330 340 350
LIENPLLRYV FGYQKNSNIQ AKGVRSSGQK ITHVVSSTMM AGLLRSLLTD
360 370 380 390 400
RLCQEPGEEE REIQFHSDPL SAINACFEGD TVIVCPGHYV VHGTFSIADS
410 420 430 440 450
IELEGYGLPD DIVIEKRGKG DTFVDCTGAD IKISGIKFVQ HDAVEGILIV
460 470 480 490 500
HRGKTTLENC VLQCETTGVT VRTSAEFLMK NSDLYGAKGA GIEIYPGSQC
510 520 530 540 550
TLSDNGIHHC KEGILIKDFL DEHYDIPKIS MVNNIIHNNE GYGVVLVKPT
560 570 580 590 600
IFSDLQENAE DGTEENKALK IQTSGEPDVA ERVDLEELIE CATGKMELCA
610 620 630 640 650
RTDPSEQVEG NCEIVNELIA ASTQKGQIKK KRLSELGITQ ADDNLMSQEM
660 670
FVGIVGNQFK WNGKGSFGTF LF
Length:672
Mass (Da):75,690
Last modified:May 18, 2010 - v3
Checksum:iF3BF0210D5413376
GO

Sequence cautioni

The sequence BAB15208.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti118 – 1181V → A in BAB71049 (PubMed:14702039).Curated
Sequence conflicti329 – 3291Q → R in BAB71049 (PubMed:14702039).Curated
Sequence conflicti437 – 4371K → R in BAB15208 (PubMed:14702039).Curated
Sequence conflicti450 – 4501V → A in BAB15208 (PubMed:14702039).Curated
Sequence conflicti558 – 5581N → S in AAH30699 (PubMed:15489334).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti21 – 211M → T.Combined sources2 Publications
Corresponds to variant rs6598679 [ dbSNP | Ensembl ].
VAR_051354
Natural varianti60 – 601M → R.
Corresponds to variant rs11545690 [ dbSNP | Ensembl ].
VAR_051355

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK025662 mRNA. Translation: BAB15208.1. Different initiation.
AK055931 mRNA. Translation: BAB71049.1.
AC092368 Genomic DNA. No translation available.
BC000960 mRNA. Translation: AAH00960.1.
BC030699 mRNA. Translation: AAH30699.1.
CCDSiCCDS10720.1.
RefSeqiNP_079021.3. NM_024745.4.
UniGeneiHs.123253.

Genome annotation databases

EnsembliENST00000303383; ENSP00000306473; ENSG00000171241.
GeneIDi79801.
KEGGihsa:79801.
UCSCiuc002eec.5. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK025662 mRNA. Translation: BAB15208.1. Different initiation.
AK055931 mRNA. Translation: BAB71049.1.
AC092368 Genomic DNA. No translation available.
BC000960 mRNA. Translation: AAH00960.1.
BC030699 mRNA. Translation: AAH30699.1.
CCDSiCCDS10720.1.
RefSeqiNP_079021.3. NM_024745.4.
UniGeneiHs.123253.

3D structure databases

ProteinModelPortaliQ8NEM2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi122898. 31 interactions.
IntActiQ8NEM2. 12 interactions.
MINTiMINT-1450223.
STRINGi9606.ENSP00000306473.

PTM databases

iPTMnetiQ8NEM2.
PhosphoSiteiQ8NEM2.

Polymorphism and mutation databases

BioMutaiSHCBP1.
DMDMi296452958.

Proteomic databases

EPDiQ8NEM2.
MaxQBiQ8NEM2.
PaxDbiQ8NEM2.
PRIDEiQ8NEM2.

Protocols and materials databases

DNASUi79801.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000303383; ENSP00000306473; ENSG00000171241.
GeneIDi79801.
KEGGihsa:79801.
UCSCiuc002eec.5. human.

Organism-specific databases

CTDi79801.
GeneCardsiSHCBP1.
HGNCiHGNC:29547. SHCBP1.
HPAiHPA048876.
MIMi611027. gene.
neXtProtiNX_Q8NEM2.
PharmGKBiPA134931125.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IIV2. Eukaryota.
ENOG410XXTE. LUCA.
GeneTreeiENSGT00530000063807.
HOGENOMiHOG000154313.
HOVERGENiHBG060212.
InParanoidiQ8NEM2.
OMAiPERTGWA.
OrthoDBiEOG7VMP4V.
PhylomeDBiQ8NEM2.
TreeFamiTF329196.

Miscellaneous databases

ChiTaRSiSHCBP1. human.
GeneWikiiSHCBP1.
GenomeRNAii79801.
NextBioi69364.
PROiQ8NEM2.
SOURCEiSearch...

Gene expression databases

BgeeiQ8NEM2.
CleanExiHS_SHCBP1.
ExpressionAtlasiQ8NEM2. baseline and differential.
GenevisibleiQ8NEM2. HS.

Family and domain databases

Gene3Di2.160.20.10. 1 hit.
InterProiIPR006626. PbH1.
IPR012334. Pectin_lyas_fold.
IPR011050. Pectin_lyase_fold/virulence.
[Graphical view]
SMARTiSM00710. PbH1. 5 hits.
[Graphical view]
SUPFAMiSSF51126. SSF51126. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "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], VARIANT THR-21.
  2. "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.
    , 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].
  3. "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], VARIANT THR-21.
    Tissue: Placenta and Testis.
  4. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
    Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
    Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31, VARIANT [LARGE SCALE ANALYSIS] THR-21, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31; SER-42; SER-44; SER-47; SER-273 AND SER-634, VARIANT [LARGE SCALE ANALYSIS] THR-21, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  6. "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].
  7. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-634, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  8. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-5; THR-7; SER-31 AND SER-634, VARIANT [LARGE SCALE ANALYSIS] THR-21, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiSHCBP_HUMAN
AccessioniPrimary (citable) accession number: Q8NEM2
Secondary accession number(s): Q96N60, Q9BVS0, Q9H6P6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: May 18, 2010
Last modified: May 11, 2016
This is version 115 of the entry and version 3 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 16
    Human chromosome 16: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.