[1]	NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH VAV1 AND CDK4. DOI=10.1038/sj.onc.1208043; PubMed=15558030 [NCBI, ExPASy, EBI, Israel, Japan] Houlard M., Romero-Portillo F., Germani A., Depaux A., Regnier-Ricard F., Gisselbrecht S., Varin-Blank N.; "Characterization of VIK-1: a new Vav-interacting Kruppel-like protein."; Oncogene 24:28-38(2005).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ASP-52. TISSUE=Brain, Cervix, and Skin; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).

Comments

FUNCTION: May be involved in transcriptional regulation.
SUBUNIT: Interacts with VAV1 and CDK4.
INTERACTION:
P11802:CDK4; NbExp=2; IntAct=EBI-625509, EBI-295644;
P15498:VAV1; NbExp=4; IntAct=EBI-625509, EBI-625518;
SUBCELLULAR LOCATION: Nucleus (Probable).
SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein family.
SIMILARITY: Contains 6 C2H2-type zinc fingers.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AY099353; AAM33786.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC011816; AAH11816.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC024770; AAH24770.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC037407; AAH37407.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_001009960.1; -.
NP_612503.1; -.

UniGene

Hs.696221

3D structure databases

HSSP

P08045; 1ZNF. [HSSP ENTRY / PDB]

ModBase

Q8N720.

Protein-protein interaction databases

IntAct

Q8N720; -.

Organism-specific databases

HGNC:30899; ZNF655.

PA134883537; -.

Gene expression databases

ArrayExpress

Q8N720; -.

CleanEx

HS_ZNF655; -.

GermOnline

ENSG00000197343; Homo sapiens.

Ontologies

GO:0005634;	Cellular component: nucleus (inferred from electronic annotation from UniProtKB-KW).
GO:0003677;	Molecular function: DNA binding (inferred from electronic annotation from UniProtKB-KW).
GO:0005515;	Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0008270;	Molecular function: zinc ion binding (inferred from electronic annotation from InterPro).
GO:0006355;	Biological process: regulation of transcription, DNA-dependent (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR007087; Znf_C2H2.
IPR015880; Znf_C2H2-like.
IPR013087; Znf_C2H2/integrase_DNA-bd.
Graphical view of domain structure.

Gene3D

G3DSA:3.30.160.60; Znf_C2H2/integrase_DNA-bd; 4.

Pfam

PF00096; zf-C2H2; 6.
Pfam graphical view of domain structure.

ProDom

PD000003; Znf_C2H2; 5.
[Domain structure / List of seq. sharing at least 1 domain]

SMART

SM00355; ZnF_C2H2; 7.
SMART graphical view of domain structure.

PROSITE

PS00028; ZINC_FINGER_C2H2_1; 6.
PS50157; ZINC_FINGER_C2H2_2; 6.
PROSITE graphical view of domain structure (profiles).

ProtoNet

Q8N720.

Proteomic databases

PeptideAtlas

Q8N720; -.

Genome annotation databases

Ensembl

ENSG00000197343; Homo sapiens. [Contig view]

GeneID

79027; -.

Phylogenomic databases

HOGENOM

Q8N720; -.

HOVERGEN

Q8N720; -.

Other

LinkHub

Q8N720; -.

NextBio

67721; -.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

DNA-binding; Metal-binding; Nucleus; Polymorphism; Repeat; Transcription; Transcription regulation; Zinc; Zinc-finger.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 491`	`491`	`Zinc finger protein 655.`	`PRO_0000047700`
`ZN_FING`	`212 234`	`23`	`C2H2-type 1.`
`ZN_FING`	`240 262`	`23`	`C2H2-type 2.`
`ZN_FING`	`303 325`	`23`	`C2H2-type 3.`
`ZN_FING`	`330 353`	`24`	`C2H2-type 4.`
`ZN_FING`	`380 402`	`23`	`C2H2-type 5.`
`ZN_FING`	`408 430`	`23`	`C2H2-type 6.`
`VARIANT`	`52 52`	`1`	`E -> D.`	`VAR_028165`

Sequence information

Length: 491 AA [This is the length of the unprocessed precursor]

Molecular weight: 57407 Da [This is the MW of the unprocessed precursor]

CRC64: 04FD791D769C3A80 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MEEIPAQEAA GSPRVQFQSL ETQSECLSPE PQFVQDTDME QGLTGDGETR EENKLLIPKQ 

        70         80         90        100        110        120 
KISEEVHSYK VRVGRLKHDI TQVPETREVY KSEDRLERLQ EILRKFLYLE REFRQITISK 

       130        140        150        160        170        180 
ETFTSEKNNE CHEPEKSFSL DSTIDADQRV LRIQNTDDND KYDMSFNQNS ASGKHEHLNL 

       190        200        210        220        230        240 
TEDFQSSECK ESLMDLSHLN KWESIPNTEK SYKCDVCGKI FHQSSALTRH QRIHTREKPY 

       250        260        270        280        290        300 
KCKECEKSFS QSSSLSRHKR IHTREKPYKC EASDKSCEAS DKSCSPSSGI IQHKKIHTRA 

       310        320        330        340        350        360 
KSYKCSSCER VFSRSVHLTQ HQKIHKEMPC KCTVCGSDFC HTSYLLEHQR VHHEEKAYEY 

       370        380        390        400        410        420 
DEYGLAYIKQ QGIHFREKPY TCSECGKDFR LNSHLIQHQR IHTGEKAHEC NECGKAFSQT 

       430        440        450        460        470        480 
SCLIQHHKMH RKEKSYECNE YEGSFSHSSD LILQQEVLTR QKAFDCDVWE KNSSQRAHLV 

       490 
QHQSIHTKEN S

Q8N720 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools