Cytoplasmic protein NCK1 - Mus musculus (Mouse)

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Q99M51 (NCK1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 93. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Cytoplasmic protein NCK1

Alternative name(s):
NCK adaptor protein 1
Short name=Nck-1

Gene names

Name:

Nck1

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	377 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Adapter protein which associates with tyrosine-phosphorylated growth factor receptors, such as KDR and PDGFRB, or their cellular substrates. Maintains low levels of EIF2S1 phosphorylation by promoting its dephosphorylation by PP1. Plays a role in the DNA damage response, not in the detection of the damage by ATM/ATR, but for efficient activation of downstream effectors, such as that of CHEK2. Plays a role in ELK1-dependent transcriptional activation in response to activated Ras signaling.
Subunit structure	Associates with BLNK, PLCG1, VAV1 and NCK1 in a B-cell antigen receptor-dependent fashion. Interacts with SOCS7. This interaction is required for nuclear import. Part of a complex containing PPP1R15B, PP1 and NCK1. Interacts with RALGPS1. Interacts with CAV2 (tyrosine phosphorylated form). Interacts with ADAM15. Interacts with FASLG. Directly interacts with RASA1. Interacts with MINK1. Interacts with KDR (tyrosine phosphorylated). Interacts (via SH2 domain) with EPHB1; activates the JUN cascade to regulate cell adhesion. Interacts (via SH2 domain) with PDGFRB (tyrosine phosphorylated). Interacts (via SH2 domain and SH3 domain 2) with EGFR. Interacts with PAK1 and SOS1. Interacts (via SH3 domains) with PKN2 By similarity. Interacts with FLT1 (tyrosine phosphorylated). Ref.6
Subcellular location	Cytoplasm By similarity. Endoplasmic reticulum By similarity. Nucleus By similarity. Note: Mostly cytoplasmic, but shuttles between the cytoplasm and the nucleus. Import into the nucleus requires interaction with SOCS7. Predominantly nuclear following genotoxic stresses, such as UV irradiation, hydroxyurea or mitomycin C treatments By similarity.
Domain	Only the first and third SH3 domains seem to be involved in RASA1-binding; the second SH3 domain and the SH2 domains do not seem to be involved By similarity.
Post-translational modification	Phosphorylated on Ser and Tyr residues. Phosphorylated in response to activation of EGFR and FcERI. Phosphorylated by activated PDGFRB By similarity.
Sequence similarities	Contains 1 SH2 domain. Contains 3 SH3 domains.

Ontologies

Keywords
Biological process	Translation regulation
Cellular component	Cytoplasm Endoplasmic reticulum Nucleus
Domain	Repeat SH2 domain SH3 domain
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	T cell activation Inferred from electronic annotation. Source: Compara actin filament organization Inferred from mutant phenotype PubMed 12637565. Source: MGI cell migration Inferred from mutant phenotype PubMed 12637565. Source: MGI lamellipodium assembly Inferred from mutant phenotype PubMed 12808099. Source: MGI positive regulation of T cell proliferation Inferred from electronic annotation. Source: Compara positive regulation of actin filament polymerization Inferred from genetic interaction PubMed 17923684. Source: MGI positive regulation of transcription from RNA polymerase II promoter Inferred from sequence or structural similarity. Source: UniProtKB regulation of translation Inferred from electronic annotation. Source: UniProtKB-KW response to other organism Inferred from mutant phenotype PubMed 22966049. Source: MGI
Cellular_component	endoplasmic reticulum Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell vesicle membrane Inferred from direct assay PubMed 12147689. Source: MGI
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Abl1	P00520	2	EBI-642202,EBI-914519
Dok1	P97465	5	EBI-642202,EBI-914917

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 377

377

Cytoplasmic protein NCK1

PRO_0000413801

Regions

Domain

2 – 61

SH3 1

Domain

106 – 165

SH3 2

Domain

190 – 252

SH3 3

Domain

282 – 376

SH2

Amino acid modifications

Modified residue

Phosphoserine Ref.8

Modified residue

Phosphoserine By similarity

Modified residue

Phosphoserine By similarity

Modified residue

105

Phosphotyrosine Ref.7

Experimental info

Sequence conflict

E → G in AAD13752. Ref.1

Sequence conflict

E → G in AAC06352. Ref.2

Sequence conflict

W → C in AAC06352. Ref.2

Sequence conflict

T → N in AAC06352. Ref.2

Sequence conflict

P → T in AAC06352. Ref.2

Sequence conflict

A → E in AAC06352. Ref.2

Sequence conflict

155 – 157

FPS → LPC in AAC06352. Ref.2

Sequence conflict

202

S → G in AAC06352. Ref.2

Sequence conflict

206

D → N in AAC06352. Ref.2

Sequence conflict

307

I → V in AAC06352. Ref.2

Sequences

Sequence

Length

Mass (Da)

Tools

Q99M51 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 671BBFC870A88EB9
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FASTA

377

42,891

        10         20         30         40         50         60 
MAEEVVVVAK FDYVAQQEQE LDIKKNERLW LLDDSKSWWR VRNSMNKTGF VPSNYVERKN 

        70         80         90        100        110        120 
SARKASIVKN LKDTLGIGKV KRKPSVPDTA SPADDSFVDP GERLYDLNMP AFVKFNYMAE 

       130        140        150        160        170        180 
REDELSLIKG TKVIVMEKCS DGWWRGSYNG QIGWFPSNYV TEEGDSPLGD HVGSLSEKLA 

       190        200        210        220        230        240 
AVVNNLNTGQ VLHVVQALYP FSSSNDEELN FEKGDVMDVI EKPENDPEWW KCRKINGMVG 

       250        260        270        280        290        300 
LVPKNYVTIM QNNPLTSGLE PSPPQCDYIR PSLTGKFAGN PWYYGKVTRH QAEMALNERG 

       310        320        330        340        350        360 
HEGDFLIRDS ESSPNDFSVS LKAQGKNKHF KVQLKETVYC IGQRKFSTME ELVEHYKKAP 

       370 
IFTSEQGEKL YLVKHLS

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Mus musculus SH2/SH3 adaptor protein (Nck) mRNA, complete cds." Miyoshi-Akiyama T., Mayer B.J. Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	Chen M., She H.Y., Li W. Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"Lineage-specific biology revealed by a finished genome assembly of the mouse." Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. Ponting C.P. PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6J.
[4]	Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C. Submitted (JUL-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]. Strain: FVB/N. Tissue: Mammary tumor.
[6]	"Identification of vascular endothelial growth factor receptor-1 tyrosine phosphorylation sites and binding of SH2 domain-containing molecules." Ito N., Wernstedt C., Engstrom U., Claesson-Welsh L. J. Biol. Chem. 273:23410-23418(1998) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH FLT1.
[7]	"Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain." Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P. J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-105, MASS SPECTROMETRY. Tissue: Brain.
[8]	"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry." Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M. J. Proteome Res. 7:5314-5326(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-85, MASS SPECTROMETRY. Tissue: Melanoma.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF084183 mRNA. Translation: AAD13752.1. AF043259 mRNA. Translation: AAC06352.1. AC129223 Genomic DNA. No translation available. CH466560 Genomic DNA. Translation: EDL21028.1. CH466560 Genomic DNA. Translation: EDL21029.1. CH466560 Genomic DNA. Translation: EDL21031.1. BC002015 mRNA. Translation: AAH02015.1.
IPI	IPI00453999.
RefSeq	NP_035008.2. NM_010878.2.
UniGene	Mm.181485.
3D structure databases
HSSP	HSSP built from PDB template 2HSP based on UniProtKB P19174.
ProteinModelPortal	Q99M51.
SMR	Q99M51. Positions 1-61, 99-174, 193-250, 279-377.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q99M51. 14 interactions.
STRING	10090.ENSMUSP00000112221.
PTM databases
PhosphoSite	Q99M51.
2D gel databases
REPRODUCTION-2DPAGE	IPI00453999.
Proteomic databases
PRIDE	Q99M51.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000116522; ENSMUSP00000112221; ENSMUSG00000032475.
GeneID	17973.
KEGG	mmu:17973.
UCSC	uc009rex.1. mouse.
Organism-specific databases
CTD	4690.
MGI	MGI:109601. Nck1.
Phylogenomic databases
eggNOG	NOG261435.
GeneTree	ENSGT00550000074482.
HOGENOM	HOG000290684.
HOVERGEN	HBG000719.
InParanoid	Q9Z279.
KO	K07365.
OMA	AIVKYNY.
OrthoDB	EOG40ZQXR.
Gene expression databases
ArrayExpress	Q99M51.
Bgee	Q99M51.
Genevestigator	Q99M51.
Family and domain databases
Gene3D	3.30.505.10. 1 hit.
InterPro	IPR017304. Cytoplasmic_NCK. IPR000980. SH2. IPR001452. SH3_domain. [Graphical view]
Pfam	PF00017. SH2. 1 hit. PF00018. SH3_1. 3 hits. [Graphical view]
PIRSF	PIRSF037874. Cytoplasmic_NCK. 1 hit.
PRINTS	PR00401. SH2DOMAIN. PR00452. SH3DOMAIN.
SMART	SM00252. SH2. 1 hit. SM00326. SH3. 3 hits. [Graphical view]
SUPFAM	SSF50044. SH3. 3 hits.
PROSITE	PS50001. SH2. 1 hit. PS50002. SH3. 3 hits. [Graphical view]
ProtoNet	Search...
Other
NextBio	292925.
SOURCE	Search...

Entry information

Entry name

NCK1_MOUSE

Accession

Primary (citable) accession number: Q99M51
Secondary accession number(s): O55032, Q9Z279

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 16, 2011
Last sequence update:	June 1, 2001
Last modified:	May 1, 2013
This is version 93 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

2D gel databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents