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O70142 (SHC2_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 68. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
SHC-transforming protein 2
Alternative name(s):
Protein Sck
SH2 domain protein C2
Src homology 2 domain-containing-transforming protein C2
Gene names
Name:Shc2
Synonyms:Sck
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length573 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Signaling adapter that couples activated growth factor receptors to signaling pathway in neurons. Involved in the signal transduction pathways of neurotrophin-activated Trk receptors in cortical neurons By similarity.

Subunit structure

Interacts with the Trk receptors in a phosphotyrosine-dependent manner and MEGF12. Once activated, binds to GRB2 By similarity.

Domain

The PID domain mediates binding to the TrkA receptor By similarity.

Post-translational modification

Phosphorylated on tyrosine by the Trk receptors By similarity.

Sequence similarities

Contains 1 PID domain.

Contains 1 SH2 domain.

Ontologies

Keywords
   DomainSH2 domain
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processintracellular signal transduction

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 573573SHC-transforming protein 2
PRO_0000342264

Regions

Domain125 – 307183PID
Domain478 – 56992SH2

Sequences

Sequence LengthMass (Da)Tools
O70142 [UniParc].

Last modified July 1, 2008. Version 2.
Checksum: F81449473CB4F7AB

FASTA57361,770
        10         20         30         40         50         60 
MTQGPGGRAA PEPEAPTTFC ALLPRMPQWK FAAPGSFLGR GPAAARVAGA AEAQPEPGVP 

        70         80         90        100        110        120 
ALAAVLGACE PRCAAPCPLP ALGRCRGSGS RGARGTPDVA DEWVRKGGFI HKPAHGWLHP 

       130        140        150        160        170        180 
DARVLGPGVS YIVRYMGCIE VLRSMRSLDF NTRTQVTREA INRLHEAVPG VRGSWKKKAP 

       190        200        210        220        230        240 
NKALASILGK SNLRFAGMSI SVNISVDGLN LSVPATRQII ANHHMQSISF ASGGDTDMTD 

       250        260        270        280        290        300 
YVAYVAKDPI NQRACHILEC CEGLAQSVIS TVGQAFELRF KQYLHSPPKA VVPPERLTGL 

       310        320        330        340        350        360 
EESAWGDGEV TADHDYYNSI PGKEPPLGGL VDSRLAVTQP CALTTLGGLG QGLSPAWRDV 

       370        380        390        400        410        420 
RGLPWDMGPS GAVPPGDGYV QADARGPHDY EEHLYVNTQG LDALELEDTS ETPLQPEDSP 

       430        440        450        460        470        480 
KKDLFDMRPF EDALKLHECS VAAGITAASL PLEDQWPSPP TRRAPIAPTE EQLRQEPWYH 

       490        500        510        520        530        540 
GRMSRRAAEK LLRADGDFLV RDSITNPGQY VLTGMHAGQP KHLLLVDPEG VVRTKDVLFE 

       550        560        570 
SISHLIDYHL KNGLPIVAAE SELHLRGVVS REP

« Hide

References

« Hide 'large scale' references
[1]"Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M. expand/collapse author list , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Brown Norway.
[2]"N-Shc and Sck, two neuronally expressed Shc adapter homologs. Their differential regional expression in the brain and roles in neurotrophin and Src signaling."
Nakamura T., Muraoka S., Sanokawa R., Mori N.
J. Biol. Chem. 273:6960-6967(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 97-573.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AABR03055985 Genomic DNA. No translation available.
AABR03059160 Genomic DNA. No translation available.
AB001452 mRNA. Translation: BAA28173.1.
IPIIPI00369445.
RefSeqNP_001101535.1. NM_001108065.1.
UniGeneRn.120041.

3D structure databases

HSSPHSSP built from PDB template 1N3H based on UniProtKB P29353.
ProteinModelPortalO70142.
SMRO70142. Positions 82-284, 471-572.
ModBaseSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000010714.

PTM databases

PhosphoSiteO70142.

Proteomic databases

PaxDbO70142.
PRIDEO70142.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000010714; ENSRNOP00000010714; ENSRNOG00000008030.
GeneID314612.
KEGGrno:314612.
UCSCRGD:1307137. rat.

Organism-specific databases

CTD25759.
RGD1307137. Shc2.

Phylogenomic databases

eggNOGNOG315087.
GeneTreeENSGT00390000018860.
HOGENOMHOG000231974.
HOVERGENHBG050121.
KOK06279.
OrthoDBEOG42NJ0D.

Gene expression databases

GenevestigatorO70142.

Family and domain databases

Gene3D2.30.29.30. 1 hit.
3.30.505.10. 1 hit.
InterProIPR011993. PH_like_dom.
IPR006019. PID_domain.
IPR006020. PTyr_interaction_dom.
IPR000980. SH2.
[Graphical view]
PfamPF00640. PID. 1 hit.
PF00017. SH2. 1 hit.
[Graphical view]
PRINTSPR00401. SH2DOMAIN.
PR00629. SHCPIDOMAIN.
SMARTSM00462. PTB. 1 hit.
SM00252. SH2. 1 hit.
[Graphical view]
PROSITEPS01179. PID. 1 hit.
PS50001. SH2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio667898.

Entry information

Entry nameSHC2_RAT
AccessionPrimary (citable) accession number: O70142
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 2008
Last sequence update: July 1, 2008
Last modified: April 3, 2013
This is version 68 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents