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Protein

Connector enhancer of kinase suppressor of ras 2

Gene

CNKSR2

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

Functioni

May function as an adapter protein or regulator of Ras signaling pathways.1 Publication

GO - Biological processi

  1. regulation of signal transduction Source: InterPro
Complete GO annotation...

Enzyme and pathway databases

SignaLinkiQ8WXI2.

Names & Taxonomyi

Protein namesi
Recommended name:
Connector enhancer of kinase suppressor of ras 2
Short name:
Connector enhancer of KSR 2
Alternative name(s):
CNK homolog protein 2
Short name:
CNK2
Gene namesi
Name:CNKSR2
Synonyms:CNK2, KIAA0902, KSR2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome X

Organism-specific databases

HGNCiHGNC:19701. CNKSR2.

Subcellular locationi

GO - Cellular componenti

  1. extracellular vesicular exosome Source: UniProtKB
  2. Golgi apparatus Source: HPA
  3. neuronal cell body Source: Ensembl
  4. neuron projection Source: Ensembl
  5. plasma membrane Source: HPA
  6. postsynaptic membrane Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134867759.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10341034Connector enhancer of kinase suppressor of ras 2PRO_0000089970Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei908 – 9081Phosphoserine3 Publications

Post-translational modificationi

Phosphorylated on tyrosine.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ8WXI2.
PaxDbiQ8WXI2.
PRIDEiQ8WXI2.

PTM databases

PhosphoSiteiQ8WXI2.

Expressioni

Gene expression databases

BgeeiQ8WXI2.
CleanExiHS_CNKSR2.
HS_KSR2.
ExpressionAtlasiQ8WXI2. baseline and differential.
GenevestigatoriQ8WXI2.

Organism-specific databases

HPAiHPA001502.

Interactioni

Subunit structurei

Interacts with RAF1, RAB2L and RAL GTPase proteins.1 Publication

Protein-protein interaction databases

BioGridi116534. 7 interactions.
DIPiDIP-29736N.
IntActiQ8WXI2. 3 interactions.
MINTiMINT-1784713.
STRINGi9606.ENSP00000368824.

Structurei

Secondary structure

1
1034
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi8 – 103Combined sources
Helixi13 – 219Combined sources
Helixi25 – 306Combined sources
Helixi31 – 377Combined sources
Helixi41 – 455Combined sources
Helixi49 – 546Combined sources
Helixi60 – 7718Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2EANNMR-A8-77[»]
3BS5X-ray2.00B5-84[»]
ProteinModelPortaliQ8WXI2.
SMRiQ8WXI2. Positions 6-80, 575-661.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8WXI2.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini11 – 7666SAMPROSITE-ProRule annotationAdd
BLAST
Domaini84 – 17895CRICPROSITE-ProRule annotationAdd
BLAST
Domaini215 – 29783PDZPROSITE-ProRule annotationAdd
BLAST
Domaini332 – 515184DUF1170Add
BLAST
Domaini570 – 669100PHPROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili875 – 90430Sequence AnalysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi354 – 3574Poly-Pro
Compositional biasi703 – 7064Poly-Pro
Compositional biasi875 – 88814Poly-GluAdd
BLAST

Sequence similaritiesi

Belongs to the CNKSR family.Curated
Contains 1 CRIC domain.PROSITE-ProRule annotation
Contains 1 DUF1170 domain.Curated
Contains 1 PDZ (DHR) domain.PROSITE-ProRule annotation
Contains 1 PH domain.PROSITE-ProRule annotation
Contains 1 SAM (sterile alpha motif) domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG255577.
GeneTreeiENSGT00390000017199.
HOGENOMiHOG000231501.
HOVERGENiHBG051040.
InParanoidiQ8WXI2.
KOiK17536.
OMAiSTKLEYK.
OrthoDBiEOG71ZP0W.
PhylomeDBiQ8WXI2.
TreeFamiTF326495.

Family and domain databases

Gene3Di1.10.150.50. 1 hit.
2.30.29.30. 1 hit.
2.30.42.10. 1 hit.
InterProiIPR010599. CNKSR2.
IPR017874. CRIC_domain.
IPR019555. CRIC_domain_Chordata.
IPR001478. PDZ.
IPR001849. PH_domain.
IPR011993. PH_like_dom.
IPR001660. SAM.
IPR013761. SAM/pointed.
IPR021129. SAM_type1.
[Graphical view]
PfamiPF10534. CRIC_ras_sig. 1 hit.
PF06663. DUF1170. 1 hit.
PF00595. PDZ. 1 hit.
PF00169. PH. 1 hit.
PF00536. SAM_1. 1 hit.
[Graphical view]
SMARTiSM00228. PDZ. 1 hit.
SM00233. PH. 1 hit.
SM00454. SAM. 1 hit.
[Graphical view]
SUPFAMiSSF47769. SSF47769. 1 hit.
SSF50156. SSF50156. 1 hit.
PROSITEiPS51290. CRIC. 1 hit.
PS50106. PDZ. 1 hit.
PS50003. PH_DOMAIN. 1 hit.
PS50105. SAM_DOMAIN. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q8WXI2-1) [UniParc]FASTAAdd to basket

Also known as: CNK2A, KSR2A

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.

« Hide

        10         20         30         40         50
MALIMEPVSK WSPSQVVDWM KGLDDCLQQY IKNFEREKIS GDQLLRITHQ
60 70 80 90 100
ELEDLGVSRI GHQELILEAV DLLCALNYGL ETENLKTLSH KLNASAKNLQ
110 120 130 140 150
NFITGRRRSG HYDGRTSRKL PNDFLTSVVD LIGAAKSLLA WLDRSPFAAV
160 170 180 190 200
TDYSVTRNNV IQLCLELTTI VQQDCTVYET ENKILHVCKT LSGVCDHIIS
210 220 230 240 250
LSSDPLVSQS AHLEVIQLAN IKPSEGLGMY IKSTYDGLHV ITGTTENSPA
260 270 280 290 300
DRCKKIHAGD EVIQVNHQTV VGWQLKNLVN ALREDPSGVI LTLKKRPQSM
310 320 330 340 350
LTSAPALLKN MRWKPLALQP LIPRSPTSSV ATPSSTISTP TKRDSSALQD
360 370 380 390 400
LYIPPPPAEP YIPRDEKGNL PCEDLRGHMV GKPVHKGSES PNSFLDQEYR
410 420 430 440 450
KRFNIVEEDT VLYCYEYEKG RSSSQGRRES TPTYGKLRPI SMPVEYNWVG
460 470 480 490 500
DYEDPNKMKR DSRRENSLLR YMSNEKIAQE EYMFQRNSKK DTGKKSKKKG
510 520 530 540 550
DKSNSPTHYS LLPSLQMDAL RQDIMGTPVP ETTLYHTFQQ SSLQHKSKKK
560 570 580 590 600
NKGPIAGKSK RRISCKDLGR GDCEGWLWKK KDAKSYFSQK WKKYWFVLKD
610 620 630 640 650
ASLYWYINEE DEKAEGFISL PEFKIDRASE CRKKYAFKAC HPKIKSFYFA
660 670 680 690 700
AEHLDDMNRW LNRINMLTAG YAERERIKQE QDYWSESDKE EADTPSTPKQ
710 720 730 740 750
DSPPPPYDTY PRPPSMSCAS PYVEAKHSRL SSTETSQSQS SHEEFRQEVT
760 770 780 790 800
GSSAVSPIRK TASQRRSWQD LIETPLTSSG LHYLQTLPLE DSVFSDSAAI
810 820 830 840 850
SPEHRRQSTL PTQKCHLQDH YGPYPLAESE RMQVLNGNGG KPRSFTLPRD
860 870 880 890 900
SGFNHCCLNA PVSACDPQDD VQPPEVEEEE EEEEEEGEAA GENIGEKSES
910 920 930 940 950
REEKLGDSLQ DLYRALEQAS LSPLGEHRIS TKMEYKLSFI KRCNDPVMNE
960 970 980 990 1000
KLHRLRILKS TLKAREGEVA IIDKVLDNPD LTSKEFQQWK QMYLDLFLDI
1010 1020 1030
CQNTTSNDPL SISSEVDVIT SSLAHTHSYI ETHV
Length:1,034
Mass (Da):117,535
Last modified:March 1, 2002 - v1
Checksum:iE43DB0D8D72D954C
GO
Isoform 2 (identifier: Q8WXI2-2) [UniParc]FASTAAdd to basket

Also known as: CNK2B, KSR2B

The sequence of this isoform differs from the canonical sequence as follows:
     899-1034: Missing.

Show »
Length:898
Mass (Da):101,874
Checksum:i4DFEFE26960DF70C
GO
Isoform 3 (identifier: Q8WXI2-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     271-319: Missing.
     899-1034: Missing.

Note: No experimental confirmation available.

Show »
Length:849
Mass (Da):96,366
Checksum:iD95B2A7AC2639040
GO
Isoform 4 (identifier: Q8WXI2-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     435-464: Missing.

Note: No experimental confirmation available.

Show »
Length:1,004
Mass (Da):113,914
Checksum:iC635EA09FA4E6696
GO

Sequence cautioni

Isoform 2 : The sequence BAA74925.2 differs from that shown. Reason: Frameshift at positions 859, 929, 985 and 1019. Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti46 – 461R → H in a colorectal cancer sample; somatic mutation. 1 Publication
VAR_035681

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei271 – 31949Missing in isoform 3. 1 PublicationVSP_043168Add
BLAST
Alternative sequencei435 – 46430Missing in isoform 4. 1 PublicationVSP_043169Add
BLAST
Alternative sequencei899 – 1034136Missing in isoform 2 and isoform 3. 3 PublicationsVSP_010887Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF418269 mRNA. Translation: AAL60502.1.
AF418270 mRNA. Translation: AAL60503.1.
AB020709 mRNA. Translation: BAA74925.2. Frameshift.
AK294728 mRNA. Translation: BAG57875.1.
AL928874, AL772392, AL807781 Genomic DNA. Translation: CAH70863.1.
AL928874, AL772392, AL807781 Genomic DNA. Translation: CAH70864.1.
AL807781, AL772392, AL928874 Genomic DNA. Translation: CAI39866.1.
AL807781, AL772392, AL928874 Genomic DNA. Translation: CAI39867.1.
AL772392, AL807781, AL928874 Genomic DNA. Translation: CAI40765.1.
AL772392, AL807781, AL928874 Genomic DNA. Translation: CAI40766.1.
CH471074 Genomic DNA. Translation: EAW98977.1.
BC126121 mRNA. Translation: AAI26122.1.
BC136289 mRNA. Translation: AAI36290.1.
BC143839 mRNA. Translation: AAI43840.1.
CCDSiCCDS14198.1. [Q8WXI2-1]
CCDS55387.1. [Q8WXI2-2]
CCDS55388.1. [Q8WXI2-5]
CCDS55389.1. [Q8WXI2-4]
RefSeqiNP_001162118.1. NM_001168647.1. [Q8WXI2-5]
NP_001162119.1. NM_001168648.1. [Q8WXI2-2]
NP_001162120.1. NM_001168649.1. [Q8WXI2-4]
NP_055742.2. NM_014927.3. [Q8WXI2-1]
UniGeneiHs.555917.

Genome annotation databases

EnsembliENST00000279451; ENSP00000279451; ENSG00000149970. [Q8WXI2-2]
ENST00000379510; ENSP00000368824; ENSG00000149970. [Q8WXI2-1]
ENST00000425654; ENSP00000397906; ENSG00000149970. [Q8WXI2-5]
ENST00000543067; ENSP00000444633; ENSG00000149970. [Q8WXI2-4]
GeneIDi22866.
KEGGihsa:22866.
UCSCiuc004czw.3. human. [Q8WXI2-1]
uc011mjn.2. human. [Q8WXI2-4]
uc011mjo.2. human. [Q8WXI2-5]

Polymorphism databases

DMDMi50400586.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF418269 mRNA. Translation: AAL60502.1.
AF418270 mRNA. Translation: AAL60503.1.
AB020709 mRNA. Translation: BAA74925.2. Frameshift.
AK294728 mRNA. Translation: BAG57875.1.
AL928874, AL772392, AL807781 Genomic DNA. Translation: CAH70863.1.
AL928874, AL772392, AL807781 Genomic DNA. Translation: CAH70864.1.
AL807781, AL772392, AL928874 Genomic DNA. Translation: CAI39866.1.
AL807781, AL772392, AL928874 Genomic DNA. Translation: CAI39867.1.
AL772392, AL807781, AL928874 Genomic DNA. Translation: CAI40765.1.
AL772392, AL807781, AL928874 Genomic DNA. Translation: CAI40766.1.
CH471074 Genomic DNA. Translation: EAW98977.1.
BC126121 mRNA. Translation: AAI26122.1.
BC136289 mRNA. Translation: AAI36290.1.
BC143839 mRNA. Translation: AAI43840.1.
CCDSiCCDS14198.1. [Q8WXI2-1]
CCDS55387.1. [Q8WXI2-2]
CCDS55388.1. [Q8WXI2-5]
CCDS55389.1. [Q8WXI2-4]
RefSeqiNP_001162118.1. NM_001168647.1. [Q8WXI2-5]
NP_001162119.1. NM_001168648.1. [Q8WXI2-2]
NP_001162120.1. NM_001168649.1. [Q8WXI2-4]
NP_055742.2. NM_014927.3. [Q8WXI2-1]
UniGeneiHs.555917.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2EANNMR-A8-77[»]
3BS5X-ray2.00B5-84[»]
ProteinModelPortaliQ8WXI2.
SMRiQ8WXI2. Positions 6-80, 575-661.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116534. 7 interactions.
DIPiDIP-29736N.
IntActiQ8WXI2. 3 interactions.
MINTiMINT-1784713.
STRINGi9606.ENSP00000368824.

PTM databases

PhosphoSiteiQ8WXI2.

Polymorphism databases

DMDMi50400586.

Proteomic databases

MaxQBiQ8WXI2.
PaxDbiQ8WXI2.
PRIDEiQ8WXI2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000279451; ENSP00000279451; ENSG00000149970. [Q8WXI2-2]
ENST00000379510; ENSP00000368824; ENSG00000149970. [Q8WXI2-1]
ENST00000425654; ENSP00000397906; ENSG00000149970. [Q8WXI2-5]
ENST00000543067; ENSP00000444633; ENSG00000149970. [Q8WXI2-4]
GeneIDi22866.
KEGGihsa:22866.
UCSCiuc004czw.3. human. [Q8WXI2-1]
uc011mjn.2. human. [Q8WXI2-4]
uc011mjo.2. human. [Q8WXI2-5]

Organism-specific databases

CTDi22866.
GeneCardsiGC0XP021392.
HGNCiHGNC:19701. CNKSR2.
HPAiHPA001502.
MIMi300724. gene.
neXtProtiNX_Q8WXI2.
PharmGKBiPA134867759.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG255577.
GeneTreeiENSGT00390000017199.
HOGENOMiHOG000231501.
HOVERGENiHBG051040.
InParanoidiQ8WXI2.
KOiK17536.
OMAiSTKLEYK.
OrthoDBiEOG71ZP0W.
PhylomeDBiQ8WXI2.
TreeFamiTF326495.

Enzyme and pathway databases

SignaLinkiQ8WXI2.

Miscellaneous databases

ChiTaRSiCNKSR2. human.
EvolutionaryTraceiQ8WXI2.
GeneWikiiCNKSR2.
GenomeRNAii22866.
NextBioi43387.
PROiQ8WXI2.
SOURCEiSearch...

Gene expression databases

BgeeiQ8WXI2.
CleanExiHS_CNKSR2.
HS_KSR2.
ExpressionAtlasiQ8WXI2. baseline and differential.
GenevestigatoriQ8WXI2.

Family and domain databases

Gene3Di1.10.150.50. 1 hit.
2.30.29.30. 1 hit.
2.30.42.10. 1 hit.
InterProiIPR010599. CNKSR2.
IPR017874. CRIC_domain.
IPR019555. CRIC_domain_Chordata.
IPR001478. PDZ.
IPR001849. PH_domain.
IPR011993. PH_like_dom.
IPR001660. SAM.
IPR013761. SAM/pointed.
IPR021129. SAM_type1.
[Graphical view]
PfamiPF10534. CRIC_ras_sig. 1 hit.
PF06663. DUF1170. 1 hit.
PF00595. PDZ. 1 hit.
PF00169. PH. 1 hit.
PF00536. SAM_1. 1 hit.
[Graphical view]
SMARTiSM00228. PDZ. 1 hit.
SM00233. PH. 1 hit.
SM00454. SAM. 1 hit.
[Graphical view]
SUPFAMiSSF47769. SSF47769. 1 hit.
SSF50156. SSF50156. 1 hit.
PROSITEiPS51290. CRIC. 1 hit.
PS50106. PDZ. 1 hit.
PS50003. PH_DOMAIN. 1 hit.
PS50105. SAM_DOMAIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Human homologue of Drosophila CNK interacts with Ras effector proteins Raf and Rlf."
    Lanigan T.M., Liu A., Huang Y.Z., Mei L., Margolis B., Guan K.-L.
    FASEB J. 17:2048-2060(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, INTERACTION WITH RAF1; RAB2L AND RAL GTPASE PROTEINS, PHOSPHORYLATION.
    Tissue: Fetal brain.
  2. "Prediction of the coding sequences of unidentified human genes. XII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
    Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
    DNA Res. 5:355-364(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Brain.
  3. "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] (ISOFORM 3).
    Tissue: Brain.
  4. "The DNA sequence of the human X chromosome."
    Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
    , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
    Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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] (ISOFORMS 1 AND 4).
    Tissue: Brain and Testis.
  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-908, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  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-908, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-908, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  10. "Solution structure of the N-terminal SAM-domain of human KIAA0902 protein (connector enhancer of kinase suppressor of RAS 2)."
    RIKEN structural genomics initiative (RSGI)
    Submitted (JUL-2007) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 8-79.
  11. Cited for: VARIANT [LARGE SCALE ANALYSIS] HIS-46.

Entry informationi

Entry nameiCNKR2_HUMAN
AccessioniPrimary (citable) accession number: Q8WXI2
Secondary accession number(s): B4DGR4
, B7ZLJ1, B9EG83, E7ESA4, O94976, Q5JPK4, Q5JPN0, Q8WXI1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: March 1, 2002
Last modified: March 4, 2015
This is version 119 of the entry and version 1 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome X
    Human chromosome X: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.