Q8IX03 (KIBRA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1113 AA.
Sequence status	Complete.
Protein existence	Evidence 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.12 Ref.13 Ref.14 Ref.16
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.11 Ref.12 Ref.13 Ref.14 Ref.17
Subcellular location	Cytoplasm. Cytoplasm › perinuclear region. Nucleus. Cell projection › ruffle membrane. Note: Co-localizes with PRKCZ in the perinuclear region. Ref.1 Ref.9 Ref.12 Ref.13
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.12 Ref.13 Ref.14
Induction	Strongly up-regulated by progestin treatment. Ref.13
Domain	The C2-domain mediates homodimerization. Ref.14
Sequence similarities	Belongs to the WWC family. KIBRA subfamily. Contains 1 C2 domain. Contains 2 WW domains.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Cell membrane Cell projection Cytoplasm Membrane Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Coiled coil Repeat
Molecular function	Activator
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell migration Inferred from direct assay Ref.12. Source: UniProtKB hippo signaling cascade Traceable author statement. Source: Reactome positive regulation of MAPK cascade Inferred from direct assay Ref.13. Source: UniProtKB regulation of hippo signaling cascade Inferred from mutant phenotype Ref.16. Source: UniProtKB regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	Golgi apparatus Inferred from direct assay. Source: HPA cytosol Traceable author statement. Source: Reactome nucleus Inferred from direct assay Ref.9Ref.13. Source: UniProtKB perinuclear region of cytoplasm Inferred from direct assay Ref.12. Source: UniProtKB protein complex Inferred from electronic annotation. Source: Compara ruffle membrane Inferred from direct assay Ref.13. Source: UniProtKB
Molecular_function	transcription coactivator activity Inferred from direct assay Ref.9. Source: UniProtKB
Complete GO annotation...

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1113

1113

Protein KIBRA

PRO_0000242153

Regions

Domain

6 – 39

34

WW 1

Domain

53 – 86

34

WW 2

Domain

655 – 783

129

C2

Region

839 – 1113

275

Interaction with histone H3

Region

953 – 996

44

Interaction with PRKCZ

Coiled coil

107 – 193

87

Potential

Coiled coil

293 – 431

139

Potential

Coiled coil

1001 – 1032

32

Potential

Motif

1111 – 1113

3

ADDV motif

Compositional bias

261 – 265

5

Poly-Ser

Compositional bias

819 – 873

55

Glu-rich

Amino acid modifications

Modified residue

899

1

Phosphoserine By similarity

Modified residue

912

1

Phosphothreonine Ref.15

Modified residue

922

1

Phosphoserine Ref.10

Modified residue

923

1

Phosphothreonine Ref.10

Modified residue

927

1

Phosphoserine Ref.10

Modified residue

929

1

Phosphothreonine Ref.15

Modified residue

931

1

Phosphoserine Ref.15

Modified residue

975

1

Phosphoserine; by PKC/PRKCZ Ref.8

Modified residue

978

1

Phosphoserine; by PKC/PRKCZ Ref.8

Natural variations

Alternative sequence

974

1

S → SPPPQPS in isoform 2.

VSP_019448

Natural variant

250

1

R → C.
Corresponds to variant rs17551608 [ dbSNP | Ensembl ].

VAR_026844

Natural variant

734

1

M → I.
Corresponds to variant rs3822660 [ dbSNP | Ensembl ].

VAR_053449

Natural variant

735

1

S → A.
Corresponds to variant rs3822659 [ dbSNP | Ensembl ].

VAR_053450

Experimental info

Sequence conflict

561

1

F → L in CAE45903. Ref.4

Sequence conflict

759

1

C → R in CAE45903. Ref.4

Sequence conflict

811

1

T → TVSWDQ in AAO73817. Ref.6

Sequence conflict

834

1

S → N in CAE45903. Ref.4

Sequence conflict

865

1

Missing in AAO73817. Ref.6

Sequence conflict

1051

1

Missing in CAE45903. Ref.4

Sequence conflict

1051

1

Missing in BAA74892. Ref.5

Sequence conflict

1064 – 1065

2

DK → AR in AAO73817. Ref.6

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

1113

Helix Strand Turn

Details...

Beta strand

660 – 669

10

Turn

670 – 673

4

Beta strand

674 – 683

10

Helix

685 – 687

3

Beta strand

694 – 704

11

Helix

708 – 711

4

Beta strand

712 – 714

3

Beta strand

722 – 733

12

Helix

736 – 741

6

Beta strand

743 – 751

9

Beta strand

757 – 766

10

Beta strand

777 – 784

8

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified March 1, 2003. Version 1. Checksum: 9010B9C127129165	FASTA	1,113	125,301
	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
	Isoform 2 [UniParc]. Checksum: 0AB48E74AB261693	FASTA	1,119	125,905
	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 KRPSPPPQPS SVKSLRSERL IRTSLDLELD LQATRTWHSQ LTQEISVLKE 1030 1040 1050 1060 1070 1080 LKEQLEQAKS HGEKELPQWL REDERFRLLL RMLEKRQMDR AEHKGELQTD KMMRAAAKDV 1090 1100 1110 HRLRGQSCKE PPEVQSFREK MAFFTRPRMN IPALSADDV

References

	« Hide 'large scale' referencesShow '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. , 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. , 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]	"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra." Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D. J. Proteome Res. 6:4150-4162(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-922; THR-923 AND SER-927, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"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.
[12]	"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.
[13]	"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.
[14]	"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.
[15]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[16]	"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.
[17]	"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.
[18]	"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.

IPI

IPI00217340.
IPI00761080.

RefSeq

NP_001155133.1. NM_001161661.1.
NP_001155134.1. NM_001161662.1.
NP_056053.1. NM_015238.2.

UniGene

Hs.484047.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2Z0U	X-ray	2.20	A/B	638-785	[»]

ProteinModelPortal

Q8IX03.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-35287N.

IntAct

Q8IX03. 6 interactions.

MINT

MINT-1405937.

STRING

9606.ENSP00000265293.

PTM databases

PhosphoSite

Q8IX03.

Polymorphism databases

DMDM

74714457.

Proteomic databases

PaxDb

Q8IX03.

PRIDE

Q8IX03.

Protocols and materials databases

DNASU

23286.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000265293; ENSP00000265293; ENSG00000113645.
ENST00000521089; ENSP00000427772; ENSG00000113645.

GeneID

23286.

KEGG

hsa:23286.

UCSC

uc003lzu.3. human.
uc003lzv.3. human.

Organism-specific databases

CTD

23286.

GeneCards

GC05P167652.

HGNC

HGNC:29435. WWC1.

HPA

HPA038016.
HPA038017.

MIM

610533. gene.

neXtProt

NX_Q8IX03.

PharmGKB

PA143485670.

HUGE

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GenAtlas

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Phylogenomic databases

eggNOG

COG5021.

HOGENOM

HOG000013211.

HOVERGEN

HBG058082.

KO

K16685.

OMA

DPQVGDY.

OrthoDB

EOG4H4632.

PhylomeDB

Q8IX03.

Enzyme and pathway databases

Reactome

REACT_111102. Signal Transduction.

Gene expression databases

ArrayExpress

Q8IX03.

Bgee

Q8IX03.

CleanEx

HS_WWC1.

Genevestigator

Q8IX03.

Family and domain databases

InterPro

IPR008973. C2_Ca/lipid-bd_dom_CaLB.
IPR001202. WW_dom.
[Graphical view]

Pfam

PF00397. WW. 2 hits.
[Graphical view]

SMART

SM00456. WW. 2 hits.
[Graphical view]

SUPFAM

SSF49562. C2_CaLB. 1 hit.
SSF51045. WW_Rsp5_WWP. 2 hits.

PROSITE

PS50004. C2. False negative.
PS01159. WW_DOMAIN_1. 1 hit.
PS50020. WW_DOMAIN_2. 2 hits.
[Graphical view]

ProtoNet

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Other

EvolutionaryTrace

Q8IX03.

GenomeRNAi

23286.

NextBio

45094.

SOURCE

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Entry information

Entry name

KIBRA_HUMAN

Accession

Primary (citable) accession number: Q8IX03
Secondary accession number(s): B4DK05 , O94946, Q6MZX4, Q6Y2F8, Q7Z4G8, Q8WVM4, Q9BT29

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 27, 2006
Last sequence update:	March 1, 2003
Last modified:	May 1, 2013
This is version 79 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.