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Reviewed, UniProtKB/Swiss-Prot O00308 (WWP2_HUMAN)

Last modified July 13, 2010. Version 96. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents
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Names and originHide

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

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

Sequence length870 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level.
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General annotation (Comments)Hide

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 By similarity.

Pathway

Protein modification; protein ubiquitination.

Subunit structure

Binds SCNN1A, SCNN1B, SCNN1G, WBP1, WBP2, DRPLA and adenovirus type 2 PIII. Interacts with NDFIP1 in vitro. Ref.1 Ref.6 Ref.7 Ref.8 Ref.9

Tissue specificity

Detected in heart, throughout the brain, placenta, lung, liver, muscle, kidney and pancreas. Ref.6

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.

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Binary interactionsHide

With

Entry

#Exp.

IntAct

Notes

RPS27AP629881EBI-743923,EBI-413034
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Sequence annotation (Features)Hide

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.10 Ref.11 Ref.13

Experimental info

Sequence conflict1361E → K in AAC51325. Ref.1
Sequence conflict394 – 3952SS → FW in AAC51325. Ref.1
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SequencesHide

Sequence LengthMass (Da)Tools
O00308-1 [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

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ReferencesHide

« 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: 9169421] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH WBP1; WBP2; SCNN1A; SCNN1B AND SCNN1G.
Tissue: Bone marrow and 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: 14702039] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Testis.
[3]"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: 15616553] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain, Ovary and Placenta.
[6]"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: 9647693] [Abstract]
Cited for: INTERACTION WITH DRPLA, TISSUE SPECIFICITY.
[7]"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: 12167593] [Abstract]
Cited for: INTERACTION WITH SCNN1A; SCNN1B AND SCNN1G.
[8]"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: 12450395] [Abstract]
Cited for: INTERACTION WITH ADENOVIRUS TYPE 2 PIII.
[9]"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: 11748237] [Abstract]
Cited for: INTERACTION WITH NDFIP1.
[10]"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: 16964243] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-211, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[11]"Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis."
Wang B., Malik R., Nigg E.A., Korner R.
Anal. Chem. 80:9526-9533(2008) [PubMed: 19007248] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-211, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[12]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-211, MASS SPECTROMETRY.
Tissue: Embryonic kidney.
+Additional computationally mapped references.
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Cross-referencesHide

Sequence databases

EMBL
GenBank
DDBJ
U96114 mRNA. Translation: AAC51325.1.
AK312792 mRNA. Translation: BAG35653.1.
AC026468 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.
IPIIPI00013010.
RefSeqNP_008945.2.
NP_955455.1.
NP_955456.1.
UniGeneHs.408458

3D structure databases

SMRO00308. Positions 16-147, 302-331, 326-437, 402-477, 495-865.
ModBaseSearch...

Protein-protein interaction databases

IntActO00308. 9 interactions.
MINTMINT-148449.
STRINGO00308.

PTM databases

PhosphoSiteO00308.

Proteomic databases

PRIDEO00308.

Genome annotation databases

EnsemblENST00000356003; ENSP00000348283; ENSG00000198373; Homo sapiens. [Genome view]
ENST00000359154; ENSP00000352069; ENSG00000198373; Homo sapiens. [Genome view]
ENST00000448661; ENSP00000396871; ENSG00000198373; Homo sapiens. [Genome view]
GeneID11060.
KEGGhsa:11060.
UCSCuc002exu.1. human.

Organism-specific databases

CTD11060.
GeneCardsGC16P068353.
HGNCHGNC:16804. WWP2.
MIM602308. gene.
PharmGKBPA128394764.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG14571.
HOGENOMHBG607874.
HOVERGENHBG004134.
InParanoidO00308.
OMADMSDWQK.
OrthoDBEOG9RBT45.
PhylomeDBO00308.

Gene expression databases

ArrayExpressO00308.
BgeeO00308.
CleanExHS_WWP2.
GenevestigatorO00308.
GermOnlineENSG00000198373. Homo sapiens.

Family and domain databases

InterProIPR000008. C2_Ca-dep.
IPR008973. C2_Ca/lipid-bd_dom_CaLB.
IPR000569. HECT.
IPR001202. WW_Rsp5_WWP.
[Graphical view]
PfamPF00632. HECT. 1 hit.
PF00397. WW. 4 hits.
[Graphical view]
SMARTSM00239. C2. 1 hit.
SM00119. HECTc. 1 hit.
SM00456. WW. 4 hits.
[Graphical view]
SUPFAMSSF49562. C2_CaLB. 1 hit.
SSF56204. HECT. 1 hit.
SSF51045. WW_Rsp5_WWP. 4 hits.
PROSITEPS50004. C2. False negative.
PS50237. HECT. 1 hit.
PS01159. WW_DOMAIN_1. 4 hits.
PS50020. WW_DOMAIN_2. 4 hits.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio42023.
SOURCESearch...
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Entry informationHide

Entry nameWWP2_HUMAN
AccessionPrimary (citable) accession number: O00308
Secondary accession number(s): A6NEP1 expand/collapse secondary AC list , B2R706, Q96CZ2, Q9BWN6
Entry history
Integrated into UniProtKB/Swiss-Prot: June 20, 2003
Last sequence update: June 20, 2003
Last modified: July 13, 2010
This is version 96 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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.
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Relevant documentsHide

Human chromosome 16

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

MIM cross-references

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

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents