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Q8IX03 (KIBRA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 89. 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:
Protein KIBRA
Alternative name(s):
HBeAg-binding protein 3
Kidney and brain protein
Short name=KIBRA
WW domain-containing protein 1
Gene names
Name:WWC1
Synonyms:KIAA0869
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1113 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Probable regulator of the Hippo/SWH (Sav/Wts/Hpo) signaling pathway, a signaling pathway that plays a pivotal role in tumor suppression by restricting proliferation and promoting apoptosis. Along with NF2 can synergistically induce the phosphorylation of LATS1 and LATS2 and can probably function in the regulation of the Hippo/SWH (Sav/Wts/Hpo) signaling pathway. Acts as a transcriptional coactivator of ESR1 which plays an essential role in DYNLL1-mediated ESR1 transactivation. Regulates collagen-stimulated activation of the ERK/MAPK cascade. Modulates directional migration of podocytes. Acts as a substrate for PRKCZ and may be associated with memory performance. Ref.8 Ref.9 Ref.11 Ref.12 Ref.13 Ref.15

Subunit structure

Homodimer. Interacts with DDN. Interacts with DYNLL1 and histone H3. The interaction with DYNLL1 is mandatory for the recruitment and transactivation functions of ESR1 or DYNLL1 to the target chromatin and the interaction with histone H3 ensures proper regulatory interaction of WWC1-DYNLL1-ESR1 complexes with target chromatin. Interacts (via WW domains) with DDR1 (via PPxY motif) in a collagen-regulated manner. Interacts with PRKCZ (via the protein kinase domain). Forms a tripartite complex with DDR1 and PRKCZ, but predominantly in the absence of collagen. Interacts (via the ADDV motif) with INADL (via PDZ domain 8). Interacts (via WW domains) with SYNPO (via PPxY motifs). Interacts with NF2 and SNX4. Ref.1 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.16

Subcellular location

Cytoplasm. Cytoplasmperinuclear region. Nucleus. Cell projectionruffle membrane. Note: Colocalizes with PRKCZ in the perinuclear region. Ref.1 Ref.9 Ref.11 Ref.12

Tissue specificity

Expressed in mammary epithelial cells and breast cancer cell lines. Found in the luminal epithelium surrounding the ducts in the normal breast. In the brain, expressed in somatodendritic compartment of neurons in the cortex and hippocampus and in the cerebellum it is found in the Purkinje cells and some granule cells (at protein level). Detected in brain, heart, colon and kidney. In the kidney, expressed in glomerular podocytes, in some tubules and in the collecting duct. Ref.1 Ref.11 Ref.12 Ref.13

Induction

Strongly up-regulated by progestin treatment. Ref.12

Domain

The C2-domain mediates homodimerization. Ref.13

Post-translational modification

Phosphorylation at Ser-542 and Ser-931 by CDK1 in response to spindle damage stress regulates mitotic exit, these two sites are dephosphorylated by CDC14B. Ref.8 Ref.9 Ref.12 Ref.18

Sequence similarities

Belongs to the WWC family. KIBRA subfamily.

Contains 1 C2 domain.

Contains 2 WW domains.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8IX03-1)

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: Q8IX03-2)

The sequence of this isoform differs from the canonical sequence as follows:
     974-974: S → SPPPQPS

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 11131113Protein KIBRA
PRO_0000242153

Regions

Domain6 – 3934WW 1
Domain53 – 8634WW 2
Domain655 – 783129C2
Region839 – 1113275Interaction with histone H3
Region953 – 99644Interaction with PRKCZ
Coiled coil107 – 19387 Potential
Coiled coil293 – 431139 Potential
Coiled coil1001 – 103232 Potential
Motif1111 – 11133ADDV motif
Compositional bias261 – 2655Poly-Ser
Compositional bias819 – 87355Glu-rich

Amino acid modifications

Modified residue5421Phosphoserine; by CDK1 Ref.18
Modified residue8991Phosphoserine By similarity
Modified residue9121Phosphothreonine Ref.14
Modified residue9291Phosphothreonine Ref.14
Modified residue9311Phosphoserine; by CDK1 Ref.14 Ref.18
Modified residue9471Phosphoserine Ref.17
Modified residue9751Phosphoserine; by PKC/PRKCZ Ref.8
Modified residue9781Phosphoserine; by PKC/PRKCZ Ref.8

Natural variations

Alternative sequence9741S → SPPPQPS in isoform 2.
VSP_019448
Natural variant2501R → C.
Corresponds to variant rs17551608 [ dbSNP | Ensembl ].
VAR_026844
Natural variant7341M → I.
Corresponds to variant rs3822660 [ dbSNP | Ensembl ].
VAR_053449
Natural variant7351S → A.
Corresponds to variant rs3822659 [ dbSNP | Ensembl ].
VAR_053450

Experimental info

Sequence conflict5611F → L in CAE45903. Ref.4
Sequence conflict7591C → R in CAE45903. Ref.4
Sequence conflict8111T → TVSWDQ in AAO73817. Ref.6
Sequence conflict8341S → N in CAE45903. Ref.4
Sequence conflict8651Missing in AAO73817. Ref.6
Sequence conflict10511Missing in CAE45903. Ref.4
Sequence conflict10511Missing in BAA74892. Ref.5
Sequence conflict1064 – 10652DK → AR in AAO73817. Ref.6

Secondary structure

...................... 1113
Helix Strand Turn

Details...

Sequences

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

Last modified March 1, 2003. Version 1.
Checksum: 9010B9C127129165

FASTA1,113125,301
        10         20         30         40         50         60 
MPRPELPLPE GWEEARDFDG KVYYIDHTNR TTSWIDPRDR YTKPLTFADC ISDELPLGWE 

        70         80         90        100        110        120 
EAYDPQVGDY FIDHNTKTTQ IEDPRVQWRR EQEHMLKDYL VVAQEALSAQ KEIYQVKQQR 

       130        140        150        160        170        180 
LELAQQEYQQ LHAVWEHKLG SQVSLVSGSS SSSKYDPEIL KAEIATAKSR VNKLKREMVH 

       190        200        210        220        230        240 
LQHELQFKER GFQTLKKIDK KMSDAQGSYK LDEAQAVLRE TKAIKKAITC GEKEKQDLIK 

       250        260        270        280        290        300 
SLAMLKDGFR TDRGSHSDLW SSSSSLESSS FPLPKQYLDV SSQTDISGSF GINSNNQLAE 

       310        320        330        340        350        360 
KVRLRLRYEE AKRRIANLKI QLAKLDSEAW PGVLDSERDR LILINEKEEL LKEMRFISPR 

       370        380        390        400        410        420 
KWTQGEVEQL EMARKRLEKD LQAARDTQSK ALTERLKLNS KRNQLVRELE EATRQVATLH 

       430        440        450        460        470        480 
SQLKSLSSSM QSLSSGSSPG SLTSSRGSLV ASSLDSSTSA SFTDLYYDPF EQLDSELQSK 

       490        500        510        520        530        540 
VEFLLLEGAT GFRPSGCITT IHEDEVAKTQ KAEGGGRLQA LRSLSGTPKS MTSLSPRSSL 

       550        560        570        580        590        600 
SSPSPPCSPL MADPLLAGDA FLNSLEFEDP ELSATLCELS LGNSAQERYR LEEPGTEGKQ 

       610        620        630        640        650        660 
LGQAVNTAQG CGLKVACVSA AVSDESVAGD SGVYEASVQR LGASEAAAFD SDESEAVGAT 

       670        680        690        700        710        720 
RIQIALKYDE KNKQFAILII QLSNLSALLQ QQDQKVNIRV AVLPCSESTT CLFRTRPLDA 

       730        740        750        760        770        780 
SDTLVFNEVF WVSMSYPALH QKTLRVDVCT TDRSHLEECL GGAQISLAEV CRSGERSTRW 

       790        800        810        820        830        840 
YNLLSYKYLK KQSRELKPVG VMAPASGPAS TDAVSALLEQ TAVELEKRQE GRSSTQTLED 

       850        860        870        880        890        900 
SWRYEETSEN EAVAEEEEEE VEEEEGEEDV FTEKASPDMD GYPALKVDKE TNTETPAPSP 

       910        920        930        940        950        960 
TVVRPKDRRV GTPSQGPFLR GSTIIRSKTF SPGPQSQYVC RLNRSDSDSS TLSKKPPFVR 

       970        980        990       1000       1010       1020 
NSLERRSVRM KRPSSVKSLR SERLIRTSLD LELDLQATRT WHSQLTQEIS VLKELKEQLE 

      1030       1040       1050       1060       1070       1080 
QAKSHGEKEL PQWLREDERF RLLLRMLEKR QMDRAEHKGE LQTDKMMRAA AKDVHRLRGQ 

      1090       1100       1110 
SCKEPPEVQS FREKMAFFTR PRMNIPALSA DDV 

« Hide

Isoform 2 [UniParc].

Checksum: 0AB48E74AB261693
Show »

FASTA1,119125,905

References

« Hide 'large scale' references
[1]"Characterization of KIBRA, a novel WW domain-containing protein."
Kremerskothen J., Plaas C., Buether K., Finger I., Veltel S., Matanis T., Liedtke T., Barnekow A.
Biochem. Biophys. Res. Commun. 300:862-867(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH DDN, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
Tissue: Brain.
[2]"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. expand/collapse author list , 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 2).
Tissue: Thalamus.
[3]"The DNA sequence and comparative analysis of human chromosome 5."
Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S. expand/collapse author list , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 36-1113 (ISOFORM 2).
Tissue: Fetal brain.
[5]"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] OF 225-1113 (ISOFORM 2).
Tissue: Brain.
[6]"Screening and cloning of interaction protein 3 of HBeAg."
Lu Y., Liu Y., Cheng J.
Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 202-1113 (ISOFORM 1).
Tissue: Liver.
[7]"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] OF 782-1113 (ISOFORM 1).
Tissue: Liver and Placenta.
[8]"KIBRA is a novel substrate for protein kinase Czeta."
Buether K., Plaas C., Barnekow A., Kremerskothen J.
Biochem. Biophys. Res. Commun. 317:703-707(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBUNIT, INTERACTION WITH PRKCZ, PHOSPHORYLATION AT SER-975 AND SER-978.
[9]"Essential role of KIBRA in co-activator function of dynein light chain 1 in mammalian cells."
Rayala S.K., den Hollander P., Manavathi B., Talukder A.H., Song C., Peng S., Barnekow A., Kremerskothen J., Kumar R.
J. Biol. Chem. 281:19092-19099(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION, INTERACTION WITH DYNLL1 AND HISTONE H3.
[10]"SNX4 coordinates endosomal sorting of TfnR with dynein-mediated transport into the endocytic recycling compartment."
Traer C.J., Rutherford A.C., Palmer K.J., Wassmer T., Oakley J., Attar N., Carlton J.G., Kremerskothen J., Stephens D.J., Cullen P.J.
Nat. Cell Biol. 9:1370-1380(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SNX4.
[11]"KIBRA modulates directional migration of podocytes."
Duning K., Schurek E.M., Schlueter M., Bayer M., Reinhardt H.C., Schwab A., Schaefer L., Benzing T., Schermer B., Saleem M.A., Huber T.B., Bachmann S., Kremerskothen J., Weide T., Pavenstaedt H.
J. Am. Soc. Nephrol. 19:1891-1903(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH SYNPO AND INADL, TISSUE SPECIFICITY.
[12]"KIBRA interacts with discoidin domain receptor 1 to modulate collagen-induced signalling."
Hilton H.N., Stanford P.M., Harris J., Oakes S.R., Kaplan W., Daly R.J., Ormandy C.J.
Biochim. Biophys. Acta 1783:383-393(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION, INDUCTION, INTERACTION WITH DDR1 AND PRKCZ, TISSUE SPECIFICITY.
[13]"Temporal-spatial expression and novel biochemical properties of the memory-related protein KIBRA."
Johannsen S., Duning K., Pavenstaedt H., Kremerskothen J., Boeckers T.M.
Neuroscience 155:1165-1173(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBUNIT, TISSUE SPECIFICITY, DOMAIN C2.
[14]"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 THR-912; THR-929 AND SER-931, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[15]"Kibra functions as a tumor suppressor protein that regulates Hippo signaling in conjunction with Merlin and Expanded."
Yu J., Zheng Y., Dong J., Klusza S., Deng W.-M., Pan D.
Dev. Cell 18:288-299(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[16]"Kibra Is a regulator of the Salvador/Warts/Hippo signaling network."
Genevet A., Wehr M.C., Brain R., Thompson B.J., Tapon N.
Dev. Cell 18:300-308(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NF2.
[17]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-947, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[18]"Phospho-regulation of KIBRA by CDK1 and CDC14 phosphatase controls cell-cycle progression."
Ji M., Yang S., Chen Y., Xiao L., Zhang L., Dong J.
Biochem. J. 447:93-102(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-542 AND SER-931 BY CDK1, DEPHOSPHORYLATION BY CDC14B.
[19]"Crystal structure of C2 domain of KIBRA protein."
RIKEN structural genomics initiative (RSGI)
Submitted (FEB-2009) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 638-785.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF506799 mRNA. Translation: AAO15881.1.
AK296323 mRNA. Translation: BAG59017.1.
AC020894 Genomic DNA. No translation available.
AC026689 Genomic DNA. No translation available.
BX640827 mRNA. Translation: CAE45903.1.
AB020676 mRNA. Translation: BAA74892.1.
AF530058 mRNA. Translation: AAQ09942.1.
AY189820 mRNA. Translation: AAO73817.1.
BC004394 mRNA. Translation: AAH04394.1.
BC017746 mRNA. Translation: AAH17746.1.
RefSeqNP_001155133.1. NM_001161661.1.
NP_001155134.1. NM_001161662.1.
NP_056053.1. NM_015238.2.
UniGeneHs.484047.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2Z0UX-ray2.20A/B638-785[»]
ProteinModelPortalQ8IX03.
SMRQ8IX03. Positions 7-87, 623-786.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116884. 15 interactions.
DIPDIP-35287N.
IntActQ8IX03. 23 interactions.
MINTMINT-1405937.
STRING9606.ENSP00000265293.

PTM databases

PhosphoSiteQ8IX03.

Polymorphism databases

DMDM74714457.

Proteomic databases

PaxDbQ8IX03.
PRIDEQ8IX03.

Protocols and materials databases

DNASU23286.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000265293; ENSP00000265293; ENSG00000113645. [Q8IX03-1]
ENST00000521089; ENSP00000427772; ENSG00000113645. [Q8IX03-2]
GeneID23286.
KEGGhsa:23286.
UCSCuc003lzu.3. human. [Q8IX03-1]
uc011den.2. human. [Q8IX03-2]

Organism-specific databases

CTD23286.
GeneCardsGC05P167652.
HGNCHGNC:29435. WWC1.
HPAHPA038016.
HPA038017.
MIM610533. gene.
neXtProtNX_Q8IX03.
PharmGKBPA143485670.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5021.
HOGENOMHOG000013211.
HOVERGENHBG058082.
KOK16685.
OMADPQVGDY.
OrthoDBEOG7DJSNR.
PhylomeDBQ8IX03.
TreeFamTF324040.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
SignaLinkQ8IX03.

Gene expression databases

ArrayExpressQ8IX03.
BgeeQ8IX03.
CleanExHS_WWC1.
GenevestigatorQ8IX03.

Family and domain databases

Gene3D2.60.40.150. 1 hit.
InterProIPR000008. C2_dom.
IPR001202. WW_dom.
[Graphical view]
PfamPF00397. WW. 2 hits.
[Graphical view]
SMARTSM00456. WW. 2 hits.
[Graphical view]
SUPFAMSSF49562. SSF49562. 1 hit.
SSF51045. SSF51045. 2 hits.
PROSITEPS01159. WW_DOMAIN_1. 1 hit.
PS50020. WW_DOMAIN_2. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ8IX03.
GeneWikiWWC1.
GenomeRNAi23286.
NextBio45094.
PROQ8IX03.
SOURCESearch...

Entry information

Entry nameKIBRA_HUMAN
AccessionPrimary (citable) accession number: Q8IX03
Secondary accession number(s): B4DK05 expand/collapse secondary AC list , O94946, Q6MZX4, Q6Y2F8, Q7Z4G8, Q8WVM4, Q9BT29
Entry history
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: March 1, 2003
Last modified: April 16, 2014
This is version 89 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 5

Human chromosome 5: entries, gene names and cross-references to MIM