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Q969H4 (CNKR1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 117. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Connector enhancer of kinase suppressor of ras 1

Short name=Connector enhancer of KSR 1
Alternative name(s):
CNK homolog protein 1
Short name=CNK1
Short name=hCNK1
Connector enhancer of KSR-like
Gene names
Name:CNKSR1
Synonyms:CNK1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length720 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May function as an adapter protein or regulator of Ras signaling pathways.

Subunit structure

Interacts with RHO and RALGDS. Ref.6

Subcellular location

Cytoplasm By similarity. Membrane; Peripheral membrane protein By similarity.

Post-translational modification

Phosphorylated on tyrosine.

Sequence similarities

Belongs to the CNKSR family.

Contains 1 CRIC domain.

Contains 1 PDZ (DHR) domain.

Contains 1 PH domain.

Contains 1 SAM (sterile alpha motif) domain.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q969H4-1)

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.
Isoform 2 (identifier: Q969H4-2)

The sequence of this isoform differs from the canonical sequence as follows:
     253-259: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 720720Connector enhancer of kinase suppressor of ras 1
PRO_0000089969

Regions

Domain7 – 7064SAM
Domain78 – 16487CRIC
Domain196 – 28590PDZ
Domain403 – 502100PH
Coiled coil615 – 64632 Potential
Compositional bias285 – 37894Pro-rich

Amino acid modifications

Modified residue3141Phosphoserine Ref.7 Ref.8

Natural variations

Alternative sequence253 – 2597Missing in isoform 2.
VSP_010886
Natural variant6621R → W.
Corresponds to variant rs17163640 [ dbSNP | Ensembl ].
VAR_057790

Experimental info

Mutagenesis4931W → A: No interaction with Rho. Ref.6
Sequence conflict6941H → N in AAC80558. Ref.1

Secondary structure

................... 720
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: E090785D1486D84B

FASTA72079,706
        10         20         30         40         50         60 
MEPVETWTPG KVATWLRGLD DSLQDYPFED WQLPGKNLLQ LCPQSLEALA VRSLGHQELI 

        70         80         90        100        110        120 
LGGVEQLQAL SSRLQTENLQ SLTEGLLGAT HDFQSIVQGC LGDCAKTPID VLCAAVELLH 

       130        140        150        160        170        180 
EADALLFWLS RYLFSHLNDF SACQEIRDLL EELSQVLHED GPAAEKEGTV LRICSHVAGI 

       190        200        210        220        230        240 
CHNILVCCPK ELLEQKAVLE QVQLDSPLGL EIHTTSNCQH FVSQVDTQVP TDSRLQIQPG 

       250        260        270        280        290        300 
DEVVQINEQV VVREERDMVG WPRKNMVREL LREPAGLSLV LKKIPIPETP PQTPPQVLDS 

       310        320        330        340        350        360 
PHQRSPSLSL APLSPRAPSE DVFAFDLSSN PSPGPSPAWT DSASLGPEPL PIPPEPPAIL 

       370        380        390        400        410        420 
PAGVAGTPGL PESPDKSPVG RKKSKGLATR LSRRRVSCRE LGRPDCDGWL LLRKAPGGFM 

       430        440        450        460        470        480 
GPRWRRRWFV LKGHTLYWYR QPQDEKAEGL INVSNYSLES GHDQKKKYVF QLTHDVYKPF 

       490        500        510        520        530        540 
IFAADTLTDL SMWVRHLITC ISKYQSPGRA PPPREEDCYS ETEAEDPDDE AGSHSASPSP 

       550        560        570        580        590        600 
AQAGSPLHGD TSPAATPTQR SPRTSFGSLT DSSEEALEGM VRGLRQGGVS LLGQPQPLTQ 

       610        620        630        640        650        660 
EQWRSSFMRR NRDPQLNERV HRVRALQSTL KAKLQELQVL EEVLGDPELT GEKFRQWKEQ 

       670        680        690        700        710        720 
NRELYSEGLG AWGVAQAEGS SHILTSDSTE QSPHSLPSDP EEHSHLCPLT SESSLRPPDL 

« Hide

Isoform 2 [UniParc].

Checksum: BF7383CCDA911E7E
Show »

FASTA71378,790

References

« Hide 'large scale' references
[1]"CNK, a RAF-binding multidomain protein required for RAS signaling."
Therrien M., Wong A.M., Rubin G.M.
Cell 95:343-353(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Tissue: Neuroepithelium.
[2]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[3]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-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] (ISOFORM 1).
Tissue: Placenta.
[6]"Human CNK1 acts as a scaffold protein, linking Rho and Ras signal transduction pathways."
Jaffe A.B., Aspenstroem P., Hall A.
Mol. Cell. Biol. 24:1736-1746(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RHO AND RALGDS, MUTAGENESIS OF TRP-493.
[7]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-314, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[8]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-314, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[9]"Solution structure of the SAM domain of human connector enhancer of KSR-like protein CNK1."
RIKEN structural genomics initiative (RSGI)
Submitted (JUL-2005) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 1-78.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF100153 mRNA. Translation: AAC80558.1.
BT006900 mRNA. Translation: AAP35546.1.
AL355877, AL391650 Genomic DNA. Translation: CAH71543.1.
AL391650, AL355877 Genomic DNA. Translation: CAI17138.1.
CH471059 Genomic DNA. Translation: EAX07842.1.
BC011604 mRNA. Translation: AAH11604.1.
BC012797 mRNA. Translation: AAH12797.1.
RefSeqNP_006305.2. NM_006314.2.
UniGeneHs.16232.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1WWVNMR-A1-78[»]
ProteinModelPortalQ969H4.
SMRQ969H4. Positions 1-78, 198-287, 404-497.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115550. 9 interactions.
IntActQ969H4. 2 interactions.
MINTMINT-1198255.
STRING9606.ENSP00000354609.

PTM databases

PhosphoSiteQ969H4.

Polymorphism databases

DMDM50400606.

Proteomic databases

PaxDbQ969H4.
PRIDEQ969H4.

Protocols and materials databases

DNASU10256.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000361530; ENSP00000354609; ENSG00000142675. [Q969H4-2]
ENST00000374253; ENSP00000363371; ENSG00000142675. [Q969H4-1]
GeneID10256.
KEGGhsa:10256.
UCSCuc001bln.4. human. [Q969H4-1]

Organism-specific databases

CTD10256.
GeneCardsGC01P026503.
H-InvDBHIX0000288.
HGNCHGNC:19700. CNKSR1.
HPAHPA030847.
HPA054309.
MIM603272. gene.
neXtProtNX_Q969H4.
PharmGKBPA134901167.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG251550.
HOGENOMHOG000231154.
HOVERGENHBG051039.
InParanoidQ969H4.
OMATHDVYKP.
OrthoDBEOG71ZP0W.
PhylomeDBQ969H4.
TreeFamTF326495.

Enzyme and pathway databases

SignaLinkQ969H4.

Gene expression databases

ArrayExpressQ969H4.
BgeeQ969H4.
CleanExHS_CNKSR1.
GenevestigatorQ969H4.

Family and domain databases

Gene3D1.10.150.50. 1 hit.
2.30.29.30. 1 hit.
2.30.42.10. 1 hit.
InterProIPR017874. CRIC_domain.
IPR019555. CRIC_domain_Chordata.
IPR001478. PDZ.
IPR011993. PH_like_dom.
IPR001849. Pleckstrin_homology.
IPR001660. SAM.
IPR013761. SAM/pointed.
IPR021129. SAM_type1.
[Graphical view]
PfamPF10534. CRIC_ras_sig. 1 hit.
PF00169. PH. 1 hit.
PF00536. SAM_1. 1 hit.
[Graphical view]
SMARTSM00233. PH. 1 hit.
SM00454. SAM. 1 hit.
[Graphical view]
SUPFAMSSF47769. SSF47769. 1 hit.
PROSITEPS51290. CRIC. 1 hit.
PS50106. PDZ. 1 hit.
PS50003. PH_DOMAIN. 1 hit.
PS50105. SAM_DOMAIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ969H4.
GeneWikiCNKSR1.
GenomeRNAi10256.
NextBio38864.
PROQ969H4.
SOURCESearch...

Entry information

Entry nameCNKR1_HUMAN
AccessionPrimary (citable) accession number: Q969H4
Secondary accession number(s): B1AMW9, O95381
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: December 1, 2001
Last modified: April 16, 2014
This is version 117 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM