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O00308 (WWP2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 135. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
NEDD4-like E3 ubiquitin-protein ligase WWP2

EC=6.3.2.-
Alternative name(s):
Atrophin-1-interacting protein 2
Short name=AIP2
WW domain-containing protein 2
Gene names
Name:WWP2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length870 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Polyubiquitinates POU5F1 by 'Lys-63'-linked conjugation and promotes it to proteasomal degradation; in embryonic stem cells (ESCs) the ubiquitination is proposed to regulate POU5F1 protein level. Ubiquitinates EGR2 and promotes it to proteasomal degradation; in T-cells the ubiquitination inhibits activation-induced cell death. Ubiquitinates SLC11A2; the ubiquitination is enhanced by presence of NDFIP1 and NDFIP2. Ubiquitinates RPB1 and promotes it to proteasomal degradation. Ref.13 Ref.15

Enzyme regulation

Activated by NDFIP1- and NDFIP2-binding.

Pathway

Protein modification; protein ubiquitination.

Subunit structure

Interacts with POU5F1, RBP1, EGR2 and SLC11A2 By similarity. Interacts with SCNN1A, SCNN1B, SCNN1G, WBP1, WBP2, ATN1 and adenovirus type 2 PIII. Interacts with ERBB4, NDFIP1 AND NDFIP2. Ref.1 Ref.7 Ref.8 Ref.9 Ref.10 Ref.13 Ref.15 Ref.16

Subcellular location

Nucleus Ref.13 Ref.16.

Tissue specificity

Detected in heart, throughout the brain, placenta, lung, liver, muscle, kidney and pancreas. Also detected in spleen and peripheral blood leukocytes. Ref.7 Ref.13

Developmental stage

Highly expressed in undifferentiated embryonic stem cells and expression is reduced after embryoid body (EB) formation. Not detectable at day 13 of EB formation; low levels are again detected at day 18 of EB formation. Ref.13

Domain

The C2 domain is involved in autoinhibition of the catalytic activity by interacting with the HECT domain By similarity. Ref.12

Post-translational modification

Autoubiquitinated. Ubiquitinated by the SCF(FBXL15) complex, leading to its degradation by the proteasome. Ref.14 Ref.18

Miscellaneous

A cysteine residue is required for ubiquitin-thioester formation.

Sequence similarities

Contains 1 C2 domain.

Contains 1 HECT (E6AP-type E3 ubiquitin-protein ligase) domain.

Contains 4 WW domains.

Sequence caution

The sequence BAC86528.1 differs from that shown. Reason: Frameshift at position 757.

Ontologies

Keywords
   Biological processHost-virus interaction
Ubl conjugation pathway
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
   DomainRepeat
   Molecular functionLigase
   PTMPhosphoprotein
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcellular protein modification process

Traceable author statement Ref.1. Source: ProtInc

negative regulation of gene expression

Inferred from mutant phenotype PubMed 18776082. Source: UniProtKB

negative regulation of protein transport

Inferred from mutant phenotype PubMed 18776082. Source: UniProtKB

negative regulation of sequence-specific DNA binding transcription factor activity

Inferred from sequence or structural similarity PubMed 15047715. Source: BHF-UCL

negative regulation of transcription from RNA polymerase II promoter

Inferred from mutant phenotype Ref.13. Source: BHF-UCL

negative regulation of transcription, DNA-templated

Inferred from sequence or structural similarity PubMed 15047715. Source: BHF-UCL

negative regulation of transporter activity

Inferred from direct assay PubMed 18776082. Source: UniProtKB

proteasome-mediated ubiquitin-dependent protein catabolic process

Inferred from mutant phenotype Ref.13. Source: UniProtKB

protein K63-linked ubiquitination

Inferred from sequence or structural similarity. Source: UniProtKB

protein ubiquitination

Inferred from direct assay PubMed 18776082. Source: UniProtKB

protein ubiquitination involved in ubiquitin-dependent protein catabolic process

Inferred from Biological aspect of Ancestor. Source: RefGenome

regulation of ion transmembrane transport

Inferred from direct assay PubMed 17289006. Source: BHF-UCL

regulation of membrane potential

Inferred from direct assay PubMed 17289006. Source: BHF-UCL

regulation of potassium ion transmembrane transporter activity

Inferred from direct assay PubMed 17289006. Source: BHF-UCL

viral entry into host cell

Traceable author statement Ref.9. Source: UniProtKB

   Cellular_componentcytoplasm

Inferred from sequence or structural similarity PubMed 15047715. Source: BHF-UCL

nucleus

Inferred from direct assay Ref.13. Source: UniProtKB

ubiquitin ligase complex

Traceable author statement Ref.7. Source: ProtInc

   Molecular_functionRNA polymerase II transcription factor binding

Inferred from physical interaction Ref.13. Source: BHF-UCL

transcription factor binding

Inferred from physical interaction Ref.15. Source: UniProtKB

ubiquitin-protein ligase activity

Inferred from direct assay Ref.13Ref.15. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O00308-1)

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: O00308-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-116: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: O00308-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-439: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 870870NEDD4-like E3 ubiquitin-protein ligase WWP2
PRO_0000120338

Regions

Domain20 – 10081C2
Domain300 – 33334WW 1
Domain330 – 36334WW 2
Domain405 – 43733WW 3
Domain444 – 47734WW 4
Domain536 – 870335HECT

Sites

Active site8381Glycyl thioester intermediate By similarity

Amino acid modifications

Modified residue2111Phosphoserine Ref.11 Ref.19

Natural variations

Alternative sequence1 – 439439Missing in isoform 3.
VSP_046461
Alternative sequence1 – 116116Missing in isoform 2.
VSP_044706

Experimental info

Mutagenesis4981K → R: Does not affect FBXL15-mediated ubiquitination. Ref.18
Mutagenesis5001H → K: Does not affect FBXL15-mediated ubiquitination. Ref.18
Mutagenesis8381C → A: Abolishes ubiquitination of POU5F1. Ref.13
Sequence conflict1361E → K in AAC51325. Ref.1
Sequence conflict3901F → L in BAG62027. Ref.3
Sequence conflict394 – 3952SS → FW in AAC51325. Ref.1
Sequence conflict5451Y → F in BAC86528. Ref.3

Sequences

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

Last modified June 20, 2003. Version 2.
Checksum: FCCD75CBA61F2204

FASTA87098,912
        10         20         30         40         50         60 
MASASSSRAG VALPFEKSQL TLKVVSAKPK VHNRQPRINS YVEVAVDGLP SETKKTGKRI 

        70         80         90        100        110        120 
GSSELLWNEI IILNVTAQSH LDLKVWSCHT LRNELLGTAS VNLSNVLKNN GGKMENMQLT 

       130        140        150        160        170        180 
LNLQTENKGS VVSGGELTIF LDGPTVDLGN VPNGSALTDG SQLPSRDSSG TAVAPENRHQ 

       190        200        210        220        230        240 
PPSTNCFGGR SRTHRHSGAS ARTTPATGEQ SPGARSRHRQ PVKNSGHSGL ANGTVNDEPT 

       250        260        270        280        290        300 
TATDPEEPSV VGVTSPPAAP LSVTPNPNTT SLPAPATPAE GEEPSTSGTQ QLPAAAQAPD 

       310        320        330        340        350        360 
ALPAGWEQRE LPNGRVYYVD HNTKTTTWER PLPPGWEKRT DPRGRFYYVD HNTRTTTWQR 

       370        380        390        400        410        420 
PTAEYVRNYE QWQSQRNQLQ GAMQHFSQRF LYQSSSASTD HDPLGPLPPG WEKRQDNGRV 

       430        440        450        460        470        480 
YYVNHNTRTT QWEDPRTQGM IQEPALPPGW EMKYTSEGVR YFVDHNTRTT TFKDPRPGFE 

       490        500        510        520        530        540 
SGTKQGSPGA YDRSFRWKYH QFRFLCHSNA LPSHVKISVS RQTLFEDSFQ QIMNMKPYDL 

       550        560        570        580        590        600 
RRRLYIIMRG EEGLDYGGIA REWFFLLSHE VLNPMYCLFE YAGKNNYCLQ INPASSINPD 

       610        620        630        640        650        660 
HLTYFRFIGR FIAMALYHGK FIDTGFTLPF YKRMLNKRPT LKDLESIDPE FYNSIVWIKE 

       670        680        690        700        710        720 
NNLEECGLEL YFIQDMEILG KVTTHELKEG GESIRVTEEN KEEYIMLLTD WRFTRGVEEQ 

       730        740        750        760        770        780 
TKAFLDGFNE VAPLEWLRYF DEKELELMLC GMQEIDMSDW QKSTIYRHYT KNSKQIQWFW 

       790        800        810        820        830        840 
QVVKEMDNEK RIRLLQFVTG TCRLPVGGFA ELIGSNGPQK FCIDKVGKET WLPRSHTCFN 

       850        860        870 
RLDLPPYKSY EQLREKLLYA IEETEGFGQE 

« Hide

Isoform 2 [UniParc].

Checksum: EB1D2F174EEE0676
Show »

FASTA75486,308
Isoform 3 [UniParc].

Checksum: 31464D3E9B6A8F77
Show »

FASTA43151,079

References

« Hide 'large scale' references
[1]"Identification of novel human WW domain-containing proteins by cloning of ligand targets."
Pirozzi G., McConnell S.J., Uveges A.J., Carter J.M., Sparks A.B., Kay B.K., Fowlkes D.M.
J. Biol. Chem. 272:14611-14616(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH WBP1; WBP2; SCNN1A; SCNN1B AND SCNN1G.
Tissue: Bone marrow and Brain.
[2]"Bioinformatic analysis of E3 ligase WWP2 in 14 different vertebrates."
Jiang G.Y., Yang J.H., Liu S.F.
Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[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. 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] (ISOFORMS 1; 2 AND 3).
Tissue: Placenta, Testis and Trachea.
[4]"The sequence and analysis of duplication-rich human chromosome 16."
Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J. expand/collapse author list , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]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 (JUL-2005) to the EMBL/GenBank/DDBJ databases
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] (ISOFORM 1).
Tissue: Brain, Ovary and Placenta.
[7]"Atrophin-1, the DRPLA gene product, interacts with two families of WW domain-containing proteins."
Wood J.D., Yuan J., Margolis R.L., Colomer V., Duan K., Kushi J., Kaminsky Z., Kleiderlein J.J. Jr., Sharp A.H., Ross C.A.
Mol. Cell. Neurosci. 11:149-160(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ATN1, TISSUE SPECIFICITY.
[8]"Ubiquitin-protein ligase WWP2 binds to and downregulates the epithelial Na(+) channel."
McDonald F.J., Western A.H., McNeil J.D., Thomas B.C., Olson D.R., Snyder P.M.
Am. J. Physiol. 283:F431-F436(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SCNN1A; SCNN1B AND SCNN1G.
[9]"Adenovirus protein involved in virus internalization recruits ubiquitin-protein ligases."
Galinier R., Gout E., Lortat-Jacob H., Wood J., Chroboczek J.
Biochemistry 41:14299-14305(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ADENOVIRUS TYPE 2 PIII.
[10]"N4WBP5, a potential target for ubiquitination by the Nedd4 family of proteins, is a novel Golgi-associated protein."
Harvey K.F., Shearwin-Whyatt L.M., Fotia A., Parton R.G., Kumar S.
J. Biol. Chem. 277:9307-9317(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NDFIP1.
[11]"A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-211, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"Autoinhibition of the HECT-type ubiquitin ligase Smurf2 through its C2 domain."
Wiesner S., Ogunjimi A.A., Wang H.R., Rotin D., Sicheri F., Wrana J.L., Forman-Kay J.D.
Cell 130:651-662(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: AUTOINHIBITION BY C2 DOMAIN.
[13]"WWP2 promotes degradation of transcription factor OCT4 in human embryonic stem cells."
Xu H., Wang W., Li C., Yu H., Yang A., Wang B., Jin Y.
Cell Res. 19:561-573(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN UBIQUITINATION OF POU5F1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, INTERACTION WITH POU5F1, MUTAGENESIS OF CYS-838.
[14]"Control of the activity of WW-HECT domain E3 ubiquitin ligases by NDFIP proteins."
Mund T., Pelham H.R.
EMBO Rep. 10:501-507(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACTIVATION BY NDFIP1 AND NDFIP2, AUTOUBIQUITINATION.
[15]"The HECT-type E3 ubiquitin ligase AIP2 inhibits activation-induced T-cell death by catalyzing EGR2 ubiquitination."
Chen A., Gao B., Zhang J., McEwen T., Ye S.Q., Zhang D., Fang D.
Mol. Cell. Biol. 29:5348-5356(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN UBIQUITINATION OF EGR2, INTERACTION WITH EGR2.
[16]"Interactions of ErbB4 and Kap1 connect the growth factor and DNA damage response pathways."
Gilmore-Hebert M., Ramabhadran R., Stern D.F.
Mol. Cancer Res. 8:1388-1398(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH ERBB4, SUBCELLULAR LOCATION.
[17]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]"SCF(FBXL15) regulates BMP signalling by directing the degradation of HECT-type ubiquitin ligase Smurf1."
Cui Y., He S., Xing C., Lu K., Wang J., Xing G., Meng A., Jia S., He F., Zhang L.
EMBO J. 30:2675-2689(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION, MUTAGENESIS OF LYS-498 AND HIS-500.
[19]"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-211, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U96114 mRNA. Translation: AAC51325.1.
JN712744 mRNA. Translation: AFK29253.1.
AK126332 mRNA. Translation: BAC86528.1. Frameshift.
AK300266 mRNA. Translation: BAG62027.1.
AK312792 mRNA. Translation: BAG35653.1.
AC026468 Genomic DNA. No translation available.
AC092115 Genomic DNA. No translation available.
CH471092 Genomic DNA. Translation: EAW83287.1.
BC000108 mRNA. Translation: AAH00108.1.
BC013645 mRNA. Translation: AAH13645.1.
BC064531 mRNA. Translation: AAH64531.1.
RefSeqNP_001257382.1. NM_001270453.1.
NP_001257383.1. NM_001270454.1.
NP_001257384.1. NM_001270455.1.
NP_008945.2. NM_007014.4.
NP_955456.1. NM_199424.2.
XP_005255835.1. XM_005255778.2.
UniGeneHs.408458.

3D structure databases

ProteinModelPortalO00308.
SMRO00308. Positions 17-143, 302-867.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116244. 52 interactions.
IntActO00308. 21 interactions.
MINTMINT-148449.
STRING9606.ENSP00000348283.

PTM databases

PhosphoSiteO00308.

Proteomic databases

PaxDbO00308.
PRIDEO00308.

Protocols and materials databases

DNASU11060.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000356003; ENSP00000348283; ENSG00000198373. [O00308-1]
ENST00000359154; ENSP00000352069; ENSG00000198373. [O00308-1]
ENST00000448661; ENSP00000396871; ENSG00000198373. [O00308-1]
ENST00000542271; ENSP00000445616; ENSG00000198373. [O00308-2]
ENST00000568684; ENSP00000456216; ENSG00000198373. [O00308-3]
ENST00000569174; ENSP00000455311; ENSG00000198373.
GeneID11060.
KEGGhsa:11060.
UCSCuc002exu.2. human. [O00308-1]

Organism-specific databases

CTD11060.
GeneCardsGC16P069796.
HGNCHGNC:16804. WWP2.
HPAHPA041682.
MIM602308. gene.
neXtProtNX_O00308.
PharmGKBPA134946925.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5021.
HOGENOMHOG000208453.
HOVERGENHBG004134.
InParanoidO00308.
KOK05630.
OMAINSYVEV.
OrthoDBEOG7RFTGT.
PhylomeDBO00308.
TreeFamTF323658.

Enzyme and pathway databases

SignaLinkO00308.
UniPathwayUPA00143.

Gene expression databases

ArrayExpressO00308.
BgeeO00308.
CleanExHS_WWP2.
GenevestigatorO00308.

Family and domain databases

Gene3D2.60.40.150. 1 hit.
InterProIPR000008. C2_dom.
IPR024928. E3_ub_ligase_SMURF1.
IPR000569. HECT.
IPR001202. WW_dom.
[Graphical view]
PfamPF00632. HECT. 1 hit.
PF00397. WW. 4 hits.
[Graphical view]
PIRSFPIRSF001569. E3_ub_ligase_SMURF1. 1 hit.
SMARTSM00239. C2. 1 hit.
SM00119. HECTc. 1 hit.
SM00456. WW. 4 hits.
[Graphical view]
SUPFAMSSF49562. SSF49562. 1 hit.
SSF51045. SSF51045. 4 hits.
SSF56204. SSF56204. 1 hit.
PROSITEPS50237. HECT. 1 hit.
PS01159. WW_DOMAIN_1. 4 hits.
PS50020. WW_DOMAIN_2. 4 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSWWP2. human.
GeneWikiWWP2.
GenomeRNAi11060.
NextBio13633274.
PROO00308.
SOURCESearch...

Entry information

Entry nameWWP2_HUMAN
AccessionPrimary (citable) accession number: O00308
Secondary accession number(s): A6NEP1 expand/collapse secondary AC list , B2R706, B4DTL5, F5H213, H3BRF3, I3RSG8, Q6ZTQ5, Q96CZ2, Q9BWN6
Entry history
Integrated into UniProtKB/Swiss-Prot: June 20, 2003
Last sequence update: June 20, 2003
Last modified: April 16, 2014
This is version 135 of the entry and version 2 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

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

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

Human chromosome 16

Human chromosome 16: entries, gene names and cross-references to MIM