O00308 (WWP2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

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	870 AA.
Sequence status	Complete.
Protein existence	Evidence 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 process	Host-virus interaction Ubl conjugation pathway
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing
Domain	Repeat
Molecular function	Ligase
PTM	Phosphoprotein Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	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 transporter activity Inferred from direct assay PubMed 18776082. Source: UniProtKB proteasomal 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 involved in ubiquitin-dependent protein catabolic process Inferred from Biological aspect of Ancestor. Source: RefGenome 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_component	cytoplasm 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_function	RNA polymerase II transcription factor binding Inferred from sequence or structural similarity PubMed 15047715. Source: BHF-UCL ubiquitin-protein ligase activity Inferred from direct assay Ref.13Ref.15. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
SMAD2	Q15796	4	EBI-743923,EBI-1040141
SMAD3	P84022	4	EBI-743923,EBI-347161
SMAD7	O15105	5	EBI-743923,EBI-3861591

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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 870	870	NEDD4-like E3 ubiquitin-protein ligase WWP2		PRO_0000120338
Regions
	Domain	20 – 100	81	C2
	Domain	300 – 333	34	WW 1
	Domain	330 – 363	34	WW 2
	Domain	405 – 437	33	WW 3
	Domain	444 – 477	34	WW 4
	Domain	536 – 870	335	HECT
Sites
	Active site	838	1	Glycyl thioester intermediate By similarity
Amino acid modifications
	Modified residue	211	1	Phosphoserine Ref.11 Ref.19
Natural variations
	Alternative sequence	1 – 439	439	Missing in isoform 3.		VSP_046461
	Alternative sequence	1 – 116	116	Missing in isoform 2.		VSP_044706
Experimental info
	Mutagenesis	498	1	K → R: Does not affect FBXL15-mediated ubiquitination. Ref.18
	Mutagenesis	500	1	H → K: Does not affect FBXL15-mediated ubiquitination. Ref.18
	Mutagenesis	838	1	C → A: Abolishes ubiquitination of POU5F1. Ref.13
	Sequence conflict	136	1	E → K in AAC51325. Ref.1
	Sequence conflict	390	1	F → L in BAG62027. Ref.3
	Sequence conflict	394 – 395	2	SS → FW in AAC51325. Ref.1
	Sequence conflict	545	1	Y → F in BAC86528. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified June 20, 2003. Version 2. Checksum: FCCD75CBA61F2204	FASTA	870	98,912
	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
	Isoform 2 [UniParc]. Checksum: EB1D2F174EEE0676	FASTA	754	86,308
	10 20 30 40 50 60 MQLTLNLQTE NKGSVVSGGE LTIFLDGPTV DLGNVPNGSA LTDGSQLPSR DSSGTAVAPE 70 80 90 100 110 120 NRHQPPSTNC FGGRSRTHRH SGASARTTPA TGEQSPGARS RHRQPVKNSG HSGLANGTVN 130 140 150 160 170 180 DEPTTATDPE EPSVVGVTSP PAAPLSVTPN PNTTSLPAPA TPAEGEEPST SGTQQLPAAA 190 200 210 220 230 240 QAPDALPAGW EQRELPNGRV YYVDHNTKTT TWERPLPPGW EKRTDPRGRF YYVDHNTRTT 250 260 270 280 290 300 TWQRPTAEYV RNYEQWQSQR NQLQGAMQHF SQRFLYQSSS ASTDHDPLGP LPPGWEKRQD 310 320 330 340 350 360 NGRVYYVNHN TRTTQWEDPR TQGMIQEPAL PPGWEMKYTS EGVRYFVDHN TRTTTFKDPR 370 380 390 400 410 420 PGFESGTKQG SPGAYDRSFR WKYHQFRFLC HSNALPSHVK ISVSRQTLFE DSFQQIMNMK 430 440 450 460 470 480 PYDLRRRLYI IMRGEEGLDY GGIAREWFFL LSHEVLNPMY CLFEYAGKNN YCLQINPASS 490 500 510 520 530 540 INPDHLTYFR FIGRFIAMAL YHGKFIDTGF TLPFYKRMLN KRPTLKDLES IDPEFYNSIV 550 560 570 580 590 600 WIKENNLEEC GLELYFIQDM EILGKVTTHE LKEGGESIRV TEENKEEYIM LLTDWRFTRG 610 620 630 640 650 660 VEEQTKAFLD GFNEVAPLEW LRYFDEKELE LMLCGMQEID MSDWQKSTIY RHYTKNSKQI 670 680 690 700 710 720 QWFWQVVKEM DNEKRIRLLQ FVTGTCRLPV GGFAELIGSN GPQKFCIDKV GKETWLPRSH 730 740 750 TCFNRLDLPP YKSYEQLREK LLYAIEETEG FGQE
	Isoform 3 [UniParc]. Checksum: 31464D3E9B6A8F77	FASTA	431	51,079
	10 20 30 40 50 60 MIQEPALPPG WEMKYTSEGV RYFVDHNTRT TTFKDPRPGF ESGTKQGSPG AYDRSFRWKY 70 80 90 100 110 120 HQFRFLCHSN ALPSHVKISV SRQTLFEDSF QQIMNMKPYD LRRRLYIIMR GEEGLDYGGI 130 140 150 160 170 180 AREWFFLLSH EVLNPMYCLF EYAGKNNYCL QINPASSINP DHLTYFRFIG RFIAMALYHG 190 200 210 220 230 240 KFIDTGFTLP FYKRMLNKRP TLKDLESIDP EFYNSIVWIK ENNLEECGLE LYFIQDMEIL 250 260 270 280 290 300 GKVTTHELKE GGESIRVTEE NKEEYIMLLT DWRFTRGVEE QTKAFLDGFN EVAPLEWLRY 310 320 330 340 350 360 FDEKELELML CGMQEIDMSD WQKSTIYRHY TKNSKQIQWF WQVVKEMDNE KRIRLLQFVT 370 380 390 400 410 420 GTCRLPVGGF AELIGSNGPQ KFCIDKVGKE TWLPRSHTCF NRLDLPPYKS YEQLREKLLY 430 AIEETEGFGQ E

References

	« Hide 'large scale' referencesShow '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. , 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. , 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. , 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY.
+	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.
IPI	IPI00013010. IPI00399310. IPI00902762.
RefSeq	NP_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.
UniGene	Hs.408458.
3D structure databases
ProteinModelPortal	O00308.
ModBase	Search...
Protein-protein interaction databases
IntAct	O00308. 12 interactions.
MINT	MINT-148449.
STRING	9606.ENSP00000348283.
PTM databases
PhosphoSite	O00308.
Proteomic databases
PaxDb	O00308.
PRIDE	O00308.
Protocols and materials databases
DNASU	11060.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000356003; ENSP00000348283; ENSG00000198373. ENST00000359154; ENSP00000352069; ENSG00000198373. ENST00000448661; ENSP00000396871; ENSG00000198373. ENST00000542271; ENSP00000445616; ENSG00000198373. ENST00000568684; ENSP00000456216; ENSG00000198373. ENST00000569174; ENSP00000455311; ENSG00000198373.
GeneID	11060.
KEGG	hsa:11060.
UCSC	uc002exu.1. human.
Organism-specific databases
CTD	11060.
GeneCards	GC16P069796.
HGNC	HGNC:16804. WWP2.
HPA	HPA041682.
MIM	602308. gene.
neXtProt	NX_O00308.
PharmGKB	PA134946925.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG5021.
HOGENOM	HOG000208453.
HOVERGEN	HBG004134.
InParanoid	O00308.
KO	K05630.
OMA	INSYVEV.
OrthoDB	EOG4S7JP8.
Enzyme and pathway databases
UniPathway	UPA00143.
Gene expression databases
ArrayExpress	O00308.
Bgee	O00308.
CleanEx	HS_WWP2.
Genevestigator	O00308.
GermOnline	ENSG00000198373. Homo sapiens.
Family and domain databases
InterPro	IPR000008. C2_Ca-dep. IPR008973. C2_Ca/lipid-bd_dom_CaLB. IPR024928. E3_ub_ligase_SMURF1. IPR000569. HECT. IPR001202. WW_dom. [Graphical view]
Pfam	PF00632. HECT. 1 hit. PF00397. WW. 4 hits. [Graphical view]
PIRSF	PIRSF001569. E3_ub_ligase_SMURF1. 1 hit.
SMART	SM00239. C2. 1 hit. SM00119. HECTc. 1 hit. SM00456. WW. 4 hits. [Graphical view]
SUPFAM	SSF49562. C2_CaLB. 1 hit. SSF56204. HECT. 1 hit. SSF51045. WW_Rsp5_WWP. 4 hits.
PROSITE	PS50004. C2. False negative. PS50237. HECT. 1 hit. PS01159. WW_DOMAIN_1. 4 hits. PS50020. WW_DOMAIN_2. 4 hits. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	WWP2. human.
GenomeRNAi	11060.
NextBio	35474965.
SOURCE	Search...

Entry information

Entry name

WWP2_HUMAN

Accession

Primary (citable) accession number: O00308
Secondary accession number(s): A6NEP1 , 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:	May 1, 2013
This is version 126 of the entry and version 2 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.