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Protein

NEDD4-like E3 ubiquitin-protein ligase WWP2

Gene

WWP2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.2 Publications

Enzyme regulationi

Activated by NDFIP1- and NDFIP2-binding.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei838 – 8381Glycyl thioester intermediatePROSITE-ProRule annotation

GO - Molecular functioni

  1. ligase activity Source: UniProtKB-KW
  2. RNA polymerase II transcription factor binding Source: BHF-UCL
  3. transcription factor binding Source: UniProtKB
  4. ubiquitin-protein transferase activity Source: UniProtKB

GO - Biological processi

  1. cellular protein modification process Source: ProtInc
  2. negative regulation of gene expression Source: UniProtKB
  3. negative regulation of protein transport Source: UniProtKB
  4. negative regulation of sequence-specific DNA binding transcription factor activity Source: BHF-UCL
  5. negative regulation of transcription, DNA-templated Source: BHF-UCL
  6. negative regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  7. negative regulation of transporter activity Source: UniProtKB
  8. proteasome-mediated ubiquitin-dependent protein catabolic process Source: UniProtKB
  9. protein autoubiquitination Source: FlyBase
  10. protein K63-linked ubiquitination Source: UniProtKB
  11. protein ubiquitination Source: UniProtKB
  12. protein ubiquitination involved in ubiquitin-dependent protein catabolic process Source: GO_Central
  13. regulation of ion transmembrane transport Source: BHF-UCL
  14. regulation of membrane potential Source: BHF-UCL
  15. regulation of potassium ion transmembrane transporter activity Source: BHF-UCL
  16. viral entry into host cell Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Host-virus interaction, Ubl conjugation pathway

Enzyme and pathway databases

BRENDAi2.3.2.B9. 2681.
SignaLinkiO00308.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
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 namesi
Name:WWP2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 16

Organism-specific databases

HGNCiHGNC:16804. WWP2.

Subcellular locationi

Nucleus 2 Publications

GO - Cellular componenti

  1. cytoplasm Source: BHF-UCL
  2. extracellular vesicular exosome Source: UniProtKB
  3. membrane Source: UniProtKB
  4. nucleus Source: UniProtKB
  5. ubiquitin ligase complex Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi498 – 4981K → R: Does not affect FBXL15-mediated ubiquitination. 1 Publication
Mutagenesisi500 – 5001H → K: Does not affect FBXL15-mediated ubiquitination. 1 Publication
Mutagenesisi838 – 8381C → A: Abolishes ubiquitination of POU5F1. 1 Publication

Organism-specific databases

PharmGKBiPA134946925.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 870870NEDD4-like E3 ubiquitin-protein ligase WWP2PRO_0000120338Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei211 – 2111Phosphoserine2 Publications

Post-translational modificationi

Autoubiquitinated. Ubiquitinated by the SCF(FBXL15) complex, leading to its degradation by the proteasome.2 Publications

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiO00308.
PaxDbiO00308.
PRIDEiO00308.

PTM databases

PhosphoSiteiO00308.

Expressioni

Tissue specificityi

Detected in heart, throughout the brain, placenta, lung, liver, muscle, kidney and pancreas. Also detected in spleen and peripheral blood leukocytes.2 Publications

Developmental stagei

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.1 Publication

Gene expression databases

BgeeiO00308.
CleanExiHS_WWP2.
ExpressionAtlasiO00308. baseline and differential.
GenevestigatoriO00308.

Organism-specific databases

HPAiHPA041682.

Interactioni

Subunit structurei

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.By similarity8 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ADARB1P785635EBI-743923,EBI-2967304
POU5F1Q018604EBI-743923,EBI-475687
SMAD2Q157964EBI-743923,EBI-1040141
SMAD3P840224EBI-743923,EBI-347161
SMAD7O151055EBI-743923,EBI-3861591

Protein-protein interaction databases

BioGridi116244. 79 interactions.
IntActiO00308. 21 interactions.
MINTiMINT-148449.
STRINGi9606.ENSP00000348283.

Structurei

3D structure databases

SMRiO00308. Positions 17-143, 302-867.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini20 – 10081C2Add
BLAST
Domaini300 – 33334WW 1PROSITE-ProRule annotationAdd
BLAST
Domaini330 – 36334WW 2PROSITE-ProRule annotationAdd
BLAST
Domaini405 – 43733WW 3PROSITE-ProRule annotationAdd
BLAST
Domaini444 – 47734WW 4PROSITE-ProRule annotationAdd
BLAST
Domaini536 – 870335HECTPROSITE-ProRule annotationAdd
BLAST

Domaini

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

Sequence similaritiesi

Contains 1 C2 domain.Curated
Contains 1 HECT (E6AP-type E3 ubiquitin-protein ligase) domain.PROSITE-ProRule annotation
Contains 4 WW domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG5021.
GeneTreeiENSGT00760000118966.
HOGENOMiHOG000208453.
HOVERGENiHBG004134.
InParanoidiO00308.
KOiK05630.
OMAiPRINSYV.
OrthoDBiEOG7RFTGT.
PhylomeDBiO00308.
TreeFamiTF323658.

Family and domain databases

Gene3Di2.60.40.150. 1 hit.
InterProiIPR000008. C2_dom.
IPR024928. E3_ub_ligase_SMURF1.
IPR000569. HECT.
IPR001202. WW_dom.
[Graphical view]
PfamiPF00632. HECT. 1 hit.
PF00397. WW. 4 hits.
[Graphical view]
PIRSFiPIRSF001569. E3_ub_ligase_SMURF1. 1 hit.
SMARTiSM00239. C2. 1 hit.
SM00119. HECTc. 1 hit.
SM00456. WW. 4 hits.
[Graphical view]
SUPFAMiSSF49562. SSF49562. 1 hit.
SSF51045. SSF51045. 4 hits.
SSF56204. SSF56204. 1 hit.
PROSITEiPS50237. HECT. 1 hit.
PS01159. WW_DOMAIN_1. 4 hits.
PS50020. WW_DOMAIN_2. 4 hits.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: O00308-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MASASSSRAG VALPFEKSQL TLKVVSAKPK VHNRQPRINS YVEVAVDGLP
60 70 80 90 100
SETKKTGKRI GSSELLWNEI IILNVTAQSH LDLKVWSCHT LRNELLGTAS
110 120 130 140 150
VNLSNVLKNN GGKMENMQLT LNLQTENKGS VVSGGELTIF LDGPTVDLGN
160 170 180 190 200
VPNGSALTDG SQLPSRDSSG TAVAPENRHQ PPSTNCFGGR SRTHRHSGAS
210 220 230 240 250
ARTTPATGEQ SPGARSRHRQ PVKNSGHSGL ANGTVNDEPT TATDPEEPSV
260 270 280 290 300
VGVTSPPAAP LSVTPNPNTT SLPAPATPAE GEEPSTSGTQ QLPAAAQAPD
310 320 330 340 350
ALPAGWEQRE LPNGRVYYVD HNTKTTTWER PLPPGWEKRT DPRGRFYYVD
360 370 380 390 400
HNTRTTTWQR PTAEYVRNYE QWQSQRNQLQ GAMQHFSQRF LYQSSSASTD
410 420 430 440 450
HDPLGPLPPG WEKRQDNGRV YYVNHNTRTT QWEDPRTQGM IQEPALPPGW
460 470 480 490 500
EMKYTSEGVR YFVDHNTRTT TFKDPRPGFE SGTKQGSPGA YDRSFRWKYH
510 520 530 540 550
QFRFLCHSNA LPSHVKISVS RQTLFEDSFQ QIMNMKPYDL RRRLYIIMRG
560 570 580 590 600
EEGLDYGGIA REWFFLLSHE VLNPMYCLFE YAGKNNYCLQ INPASSINPD
610 620 630 640 650
HLTYFRFIGR FIAMALYHGK FIDTGFTLPF YKRMLNKRPT LKDLESIDPE
660 670 680 690 700
FYNSIVWIKE NNLEECGLEL YFIQDMEILG KVTTHELKEG GESIRVTEEN
710 720 730 740 750
KEEYIMLLTD WRFTRGVEEQ TKAFLDGFNE VAPLEWLRYF DEKELELMLC
760 770 780 790 800
GMQEIDMSDW QKSTIYRHYT KNSKQIQWFW QVVKEMDNEK RIRLLQFVTG
810 820 830 840 850
TCRLPVGGFA ELIGSNGPQK FCIDKVGKET WLPRSHTCFN RLDLPPYKSY
860 870
EQLREKLLYA IEETEGFGQE
Length:870
Mass (Da):98,912
Last modified:June 19, 2003 - v2
Checksum:iFCCD75CBA61F2204
GO
Isoform 2 (identifier: O00308-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-116: Missing.

Note: No experimental confirmation available.

Show »
Length:754
Mass (Da):86,308
Checksum:iEB1D2F174EEE0676
GO
Isoform 3 (identifier: O00308-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-439: Missing.

Note: No experimental confirmation available.

Show »
Length:431
Mass (Da):51,079
Checksum:i31464D3E9B6A8F77
GO
Isoform 4 (identifier: O00308-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     336-870: Missing.

Note: No experimental confirmation available.

Show »
Length:335
Mass (Da):35,248
Checksum:i4FDE005EDF329841
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti136 – 1361E → K in AAC51325 (PubMed:9169421).Curated
Sequence conflicti390 – 3901F → L in BAG62027 (PubMed:14702039).Curated
Sequence conflicti394 – 3952SS → FW in AAC51325 (PubMed:9169421).Curated
Sequence conflicti545 – 5451Y → F in BAC86528 (PubMed:14702039).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 439439Missing in isoform 3. 1 PublicationVSP_046461Add
BLAST
Alternative sequencei1 – 116116Missing in isoform 2. 1 PublicationVSP_044706Add
BLAST
Alternative sequencei336 – 870535Missing in isoform 4. 1 PublicationVSP_054711Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS10885.1. [O00308-1]
CCDS58475.1. [O00308-4]
CCDS58476.1. [O00308-2]
CCDS58477.1. [O00308-3]
RefSeqiNP_001257382.1. NM_001270453.1. [O00308-2]
NP_001257383.1. NM_001270454.1. [O00308-1]
NP_001257384.1. NM_001270455.1. [O00308-4]
NP_008945.2. NM_007014.4. [O00308-1]
NP_955456.1. NM_199424.2. [O00308-3]
XP_005255835.1. XM_005255778.2. [O00308-1]
UniGeneiHs.408458.

Genome annotation databases

EnsembliENST00000356003; ENSP00000348283; ENSG00000198373. [O00308-2]
ENST00000359154; ENSP00000352069; ENSG00000198373. [O00308-1]
ENST00000568684; ENSP00000456216; ENSG00000198373. [O00308-3]
ENST00000569174; ENSP00000455311; ENSG00000198373. [O00308-4]
GeneIDi11060.
KEGGihsa:11060.
UCSCiuc002exu.2. human. [O00308-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS10885.1. [O00308-1]
CCDS58475.1. [O00308-4]
CCDS58476.1. [O00308-2]
CCDS58477.1. [O00308-3]
RefSeqiNP_001257382.1. NM_001270453.1. [O00308-2]
NP_001257383.1. NM_001270454.1. [O00308-1]
NP_001257384.1. NM_001270455.1. [O00308-4]
NP_008945.2. NM_007014.4. [O00308-1]
NP_955456.1. NM_199424.2. [O00308-3]
XP_005255835.1. XM_005255778.2. [O00308-1]
UniGeneiHs.408458.

3D structure databases

SMRiO00308. Positions 17-143, 302-867.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116244. 79 interactions.
IntActiO00308. 21 interactions.
MINTiMINT-148449.
STRINGi9606.ENSP00000348283.

PTM databases

PhosphoSiteiO00308.

Proteomic databases

MaxQBiO00308.
PaxDbiO00308.
PRIDEiO00308.

Protocols and materials databases

DNASUi11060.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000356003; ENSP00000348283; ENSG00000198373. [O00308-2]
ENST00000359154; ENSP00000352069; ENSG00000198373. [O00308-1]
ENST00000568684; ENSP00000456216; ENSG00000198373. [O00308-3]
ENST00000569174; ENSP00000455311; ENSG00000198373. [O00308-4]
GeneIDi11060.
KEGGihsa:11060.
UCSCiuc002exu.2. human. [O00308-1]

Organism-specific databases

CTDi11060.
GeneCardsiGC16P069796.
HGNCiHGNC:16804. WWP2.
HPAiHPA041682.
MIMi602308. gene.
neXtProtiNX_O00308.
PharmGKBiPA134946925.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5021.
GeneTreeiENSGT00760000118966.
HOGENOMiHOG000208453.
HOVERGENiHBG004134.
InParanoidiO00308.
KOiK05630.
OMAiPRINSYV.
OrthoDBiEOG7RFTGT.
PhylomeDBiO00308.
TreeFamiTF323658.

Enzyme and pathway databases

UniPathwayiUPA00143.
BRENDAi2.3.2.B9. 2681.
SignaLinkiO00308.

Miscellaneous databases

ChiTaRSiWWP2. human.
GeneWikiiWWP2.
GenomeRNAii11060.
NextBioi13633274.
PROiO00308.
SOURCEiSearch...

Gene expression databases

BgeeiO00308.
CleanExiHS_WWP2.
ExpressionAtlasiO00308. baseline and differential.
GenevestigatoriO00308.

Family and domain databases

Gene3Di2.60.40.150. 1 hit.
InterProiIPR000008. C2_dom.
IPR024928. E3_ub_ligase_SMURF1.
IPR000569. HECT.
IPR001202. WW_dom.
[Graphical view]
PfamiPF00632. HECT. 1 hit.
PF00397. WW. 4 hits.
[Graphical view]
PIRSFiPIRSF001569. E3_ub_ligase_SMURF1. 1 hit.
SMARTiSM00239. C2. 1 hit.
SM00119. HECTc. 1 hit.
SM00456. WW. 4 hits.
[Graphical view]
SUPFAMiSSF49562. SSF49562. 1 hit.
SSF51045. SSF51045. 4 hits.
SSF56204. SSF56204. 1 hit.
PROSITEiPS50237. HECT. 1 hit.
PS01159. WW_DOMAIN_1. 4 hits.
PS50020. WW_DOMAIN_2. 4 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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(1996) [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 (AUG-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(2003) [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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. 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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4).
    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(1997) [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(2001) [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(2001) [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(2001) [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(2005) [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(2006) [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(2008) [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(2008) [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(2008) [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(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH ERBB4, SUBCELLULAR LOCATION.
  17. 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(2010) [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(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-211, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiWWP2_HUMAN
AccessioniPrimary (citable) accession number: O00308
Secondary accession number(s): A6NEP1
, B2R706, B4DTL5, F5H213, H3BRF3, I3RSG8, Q6ZTQ5, Q96CZ2, Q9BWN6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 19, 2003
Last sequence update: June 19, 2003
Last modified: March 31, 2015
This is version 145 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Miscellaneous

A cysteine residue is required for ubiquitin-thioester formation.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 16
    Human chromosome 16: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.