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Q9H0M0

- WWP1_HUMAN

UniProt

Q9H0M0 - WWP1_HUMAN

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Protein
NEDD4-like E3 ubiquitin-protein ligase WWP1
Gene
WWP1
Organism
Homo sapiens (Human)
Status
Reviewed - 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. Ubiquitinates ERBB4 isoforms JM-A CYT-1 and JM-B CYT-1, KLF2, KLF5 and TP63 and promotes their proteasomal degradation. Ubiquitinates RNF11 without targeting it for degradation. Ubiquitinates and promotes degradation of TGFBR1; the ubiquitination is enhanced by SMAD7. Ubiquitinates SMAD6 and SMAD7. Ubiquitinates and promotes degradation of SMAD2 in response to TGF-beta signaling, which requires interaction with TGIF.3 Publications

Enzyme regulationi

Activated by NDFIP1- and NDFIP2-binding.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei890 – 8901Glycyl thioester intermediate By similarity
Sitei890 – 8901Required for ubiquitin-thioester formation By similarity

GO - Molecular functioni

  1. ligase activity Source: UniProtKB-KW
  2. protein binding Source: UniProtKB
  3. ubiquitin-protein transferase activity Source: UniProtKB

GO - Biological processi

  1. central nervous system development Source: UniProtKB
  2. ion transmembrane transport Source: Reactome
  3. negative regulation of transcription, DNA-templated Source: UniProtKB
  4. proteasome-mediated ubiquitin-dependent protein catabolic process Source: Ensembl
  5. protein ubiquitination Source: UniProtKB
  6. protein ubiquitination involved in ubiquitin-dependent protein catabolic process Source: RefGenome
  7. signal transduction Source: UniProtKB
  8. transmembrane transport Source: Reactome
  9. 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

ReactomeiREACT_115828. Downregulation of ERBB4 signaling.
REACT_160189. Stimuli-sensing channels.
REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
SignaLinkiQ9H0M0.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
NEDD4-like E3 ubiquitin-protein ligase WWP1 (EC:6.3.2.-)
Alternative name(s):
Atrophin-1-interacting protein 5
Short name:
AIP5
TGIF-interacting ubiquitin ligase 1
Short name:
Tiul1
WW domain-containing protein 1
Gene namesi
Name:WWP1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 8

Organism-specific databases

HGNCiHGNC:17004. WWP1.

Subcellular locationi

Cytoplasm By similarity. Cell membrane; Peripheral membrane protein By similarity. Nucleus By similarity

GO - Cellular componenti

  1. cytoplasm Source: RefGenome
  2. cytosol Source: Reactome
  3. nucleus Source: RefGenome
  4. plasma membrane Source: UniProtKB-SubCell
  5. ubiquitin ligase complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi614 – 6141E → A: Reduces ubiquitin transfer. 1 Publication
Mutagenesisi621 – 6211H → A: Strongly reduces ubiquitin transfer. 1 Publication
Mutagenesisi675 – 6751D → A: Reduces ubiquitin transfer. 1 Publication
Mutagenesisi798 – 7981E → A: Reduces ubiquitin transfer. Strongly reduces ubiquitin transfer; when associated with A-845. 1 Publication
Mutagenesisi804 – 8041M → P: Strongly reduces ubiquitin transfer; when associated with P-806. 1 Publication
Mutagenesisi806 – 8061E → P: Strongly reduces ubiquitin transfer; when associated with P-804. 1 Publication
Mutagenesisi845 – 8451R → A: No effect. 1 Publication
Mutagenesisi848 – 8481Q → A: Abolishes ubiquitin transfer; when associated with A-855. 1 Publication
Mutagenesisi855 – 8551R → A: Abolishes ubiquitin transfer; when associated with A-848. 1 Publication

Organism-specific databases

PharmGKBiPA134960138.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 922922NEDD4-like E3 ubiquitin-protein ligase WWP1
PRO_0000120336Add
BLAST

Post-translational modificationi

Auto-ubiquitinated and ubiquitinated by RNF11.

Keywords - PTMi

Ubl conjugation

Proteomic databases

MaxQBiQ9H0M0.
PaxDbiQ9H0M0.
PRIDEiQ9H0M0.

PTM databases

PhosphoSiteiQ9H0M0.

Expressioni

Tissue specificityi

Detected in heart, placenta, pancreas, kidney, liver, skeletal muscle, bone marrow, fetal brain, and at much lower levels in adult brain and lung. Isoform 1 and isoform 5 predominate in all tissues tested, except in testis and bone marrow, where isoform 5 is expressed at much higher levels than isoform 1.2 Publications

Gene expression databases

ArrayExpressiQ9H0M0.
BgeeiQ9H0M0.
CleanExiHS_WWP1.
GenevestigatoriQ9H0M0.

Organism-specific databases

HPAiHPA023180.

Interactioni

Subunit structurei

Binds KLF2 AND HIVEP3 By similarity. Binds SCNN1A, SCNN1B, SCNN1G, WBP1, WBP2, DRPLA and adenovirus type 2 PIII. Interacts with RNF11 By similarity. Interacts with SPG20. Interacts with ERBB4 isoforms JM-B CYT-1 and JM-A CYT-1. Interacts with SMAD1, SMAD2, SMAD3, SMAD5, SMAD6, SMAD7, TGFBR1 AND TGFBR2. Associates with the TGFBR1:TGFBR2 receptor complex in presence of SMAD7. Interacts with SKIL isoform 1. Interacts with TP63 isoform 1 and isoform 2. Interacts with STAMBP and RNF11. Interacts with NDFIP1 and NDFIP2 Inferred; this interaction activates the E3 ubiquitin-protein ligase. Interacts with TGIF.7 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CPSF6Q166303EBI-742157,EBI-358410

Protein-protein interaction databases

BioGridi116243. 57 interactions.
IntActiQ9H0M0. 22 interactions.
MINTiMINT-199541.
STRINGi9606.ENSP00000265428.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi500 – 5056
Turni509 – 5113
Beta strandi513 – 5186
Beta strandi521 – 5233
Helixi547 – 56014
Beta strandi564 – 5718
Turni573 – 5753
Helixi576 – 58510
Helixi589 – 5935
Beta strandi594 – 6007
Turni601 – 6033
Helixi610 – 62314
Helixi626 – 6283
Beta strandi629 – 63810
Beta strandi641 – 6433
Helixi645 – 6495
Helixi653 – 66917
Helixi680 – 6867
Helixi693 – 6975
Helixi701 – 71111
Beta strandi723 – 7264
Beta strandi730 – 7334
Beta strandi737 – 7404
Helixi743 – 7453
Turni750 – 7523
Helixi753 – 76614
Turni767 – 7693
Helixi770 – 78314
Helixi786 – 7894
Helixi794 – 8029
Helixi809 – 8146
Beta strandi816 – 8205
Helixi826 – 83712
Helixi840 – 85112
Helixi861 – 8633
Beta strandi873 – 8764
Beta strandi886 – 8883
Helixi889 – 8913
Beta strandi893 – 8953
Helixi902 – 91413

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ND7X-ray2.10A546-917[»]
2OP7NMR-A494-532[»]
ProteinModelPortaliQ9H0M0.
SMRiQ9H0M0. Positions 19-145, 351-919.

Miscellaneous databases

EvolutionaryTraceiQ9H0M0.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini5 – 9894C2
Add
BLAST
Domaini349 – 38234WW 1
Add
BLAST
Domaini381 – 41434WW 2
Add
BLAST
Domaini456 – 48934WW 3
Add
BLAST
Domaini496 – 52934WW 4
Add
BLAST
Domaini588 – 922335HECT
Add
BLAST

Sequence similaritiesi

Contains 1 C2 domain.
Contains 4 WW domains.

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG5021.
HOGENOMiHOG000208453.
HOVERGENiHBG004134.
InParanoidiQ9H0M0.
KOiK05633.
OMAiKNGIVQT.
OrthoDBiEOG7RFTGT.
PhylomeDBiQ9H0M0.
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]
PfamiPF00168. C2. 1 hit.
PF00632. 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.
PROSITEiPS50004. C2. 1 hit.
PS50237. HECT. 1 hit.
PS01159. WW_DOMAIN_1. 4 hits.
PS50020. WW_DOMAIN_2. 4 hits.
[Graphical view]

Sequences (6)i

Sequence statusi: Complete.

This entry describes 6 isoformsi produced by alternative splicing. Align

Note: Additional isoforms seem to exist.

Isoform 1 (identifier: Q9H0M0-1) [UniParc]FASTAAdd to Basket

Also known as: A

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

MATASPRSDT SNNHSGRLQL QVTVSSAKLK RKKNWFGTAI YTEVVVDGEI    50
TKTAKSSSSS NPKWDEQLTV NVTPQTTLEF QVWSHRTLKA DALLGKATID 100
LKQALLIHNR KLERVKEQLK LSLENKNGIA QTGELTVVLD GLVIEQENIT 150
NCSSSPTIEI QENGDALHEN GEPSARTTAR LAVEGTNGID NHVPTSTLVQ 200
NSCCSYVVNG DNTPSSPSQV AARPKNTPAP KPLASEPADD TVNGESSSFA 250
PTDNASVTGT PVVSEENALS PNCTSTTVED PPVQEILTSS ENNECIPSTS 300
AELESEARSI LEPDTSNSRS SSAFEAAKSR QPDGCMDPVR QQSGNANTET 350
LPSGWEQRKD PHGRTYYVDH NTRTTTWERP QPLPPGWERR VDDRRRVYYV 400
DHNTRTTTWQ RPTMESVRNF EQWQSQRNQL QGAMQQFNQR YLYSASMLAA 450
ENDPYGPLPP GWEKRVDSTD RVYFVNHNTK TTQWEDPRTQ GLQNEEPLPE 500
GWEIRYTREG VRYFVDHNTR TTTFKDPRNG KSSVTKGGPQ IAYERGFRWK 550
LAHFRYLCQS NALPSHVKIN VSRQTLFEDS FQQIMALKPY DLRRRLYVIF 600
RGEEGLDYGG LAREWFFLLS HEVLNPMYCL FEYAGKNNYC LQINPASTIN 650
PDHLSYFCFI GRFIAMALFH GKFIDTGFSL PFYKRMLSKK LTIKDLESID 700
TEFYNSLIWI RDNNIEECGL EMYFSVDMEI LGKVTSHDLK LGGSNILVTE 750
ENKDEYIGLM TEWRFSRGVQ EQTKAFLDGF NEVVPLQWLQ YFDEKELEVM 800
LCGMQEVDLA DWQRNTVYRH YTRNSKQIIW FWQFVKETDN EVRMRLLQFV 850
TGTCRLPLGG FAELMGSNGP QKFCIEKVGK DTWLPRSHTC FNRLDLPPYK 900
SYEQLKEKLL FAIEETEGFG QE 922
Length:922
Mass (Da):105,202
Last modified:March 1, 2001 - v1
Checksum:i35B6E1C03A3147DA
GO
Isoform 2 (identifier: Q9H0M0-2) [UniParc]FASTAAdd to Basket

Also known as: B

The sequence of this isoform differs from the canonical sequence as follows:
     112-120: LERVKEQLK → CWLLKARME
     121-922: Missing.

Show »
Length:120
Mass (Da):13,453
Checksum:i952B6A78C5D4B93D
GO
Isoform 3 (identifier: Q9H0M0-3) [UniParc]FASTAAdd to Basket

Also known as: C

The sequence of this isoform differs from the canonical sequence as follows:
     112-242: LERVKEQLKL...LASEPADDTV → F

Show »
Length:792
Mass (Da):91,548
Checksum:i833D351CC08D9998
GO
Isoform 4 (identifier: Q9H0M0-4)

Also known as: D

Sequence is not available
Length:
Mass (Da):
Isoform 5 (identifier: Q9H0M0-5)

Also known as: E

Sequence is not available
Length:
Mass (Da):
Isoform 6 (identifier: Q9H0M0-6) [UniParc]FASTAAdd to Basket

Also known as: F

The sequence of this isoform differs from the canonical sequence as follows:
     23-240: Missing.

Show »
Length:704
Mass (Da):81,649
Checksum:iB39DCB6841290CF0
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti852 – 8521G → V.
Corresponds to variant rs1059901 [ dbSNP | Ensembl ].
VAR_052960

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei23 – 240218Missing in isoform 6.
VSP_007600Add
BLAST
Alternative sequencei112 – 242131LERVK…ADDTV → F in isoform 3.
VSP_007602Add
BLAST
Alternative sequencei112 – 1209LERVKEQLK → CWLLKARME in isoform 2.
VSP_007601
Alternative sequencei121 – 922802Missing in isoform 2.
VSP_007603Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AL136739 mRNA. Translation: CAB66673.1.
AY043361 mRNA. Translation: AAK94668.1.
AY345857 mRNA. Translation: AAQ22764.1.
AC083845 Genomic DNA. No translation available.
AC103817 Genomic DNA. No translation available.
BC015380 mRNA. Translation: AAH15380.2.
BC036065 mRNA. Translation: AAH36065.1.
U96113 mRNA. Translation: AAC51324.1.
CCDSiCCDS6242.1. [Q9H0M0-1]
RefSeqiNP_008944.1. NM_007013.3. [Q9H0M0-1]
XP_005250817.1. XM_005250760.2. [Q9H0M0-1]
UniGeneiHs.655189.

Genome annotation databases

EnsembliENST00000265428; ENSP00000265428; ENSG00000123124. [Q9H0M0-1]
ENST00000341922; ENSP00000340564; ENSG00000123124. [Q9H0M0-3]
ENST00000349423; ENSP00000342665; ENSG00000123124. [Q9H0M0-6]
ENST00000517970; ENSP00000427793; ENSG00000123124. [Q9H0M0-1]
GeneIDi11059.
KEGGihsa:11059.
UCSCiuc003ydt.3. human. [Q9H0M0-1]

Polymorphism databases

DMDMi32171908.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AL136739 mRNA. Translation: CAB66673.1 .
AY043361 mRNA. Translation: AAK94668.1 .
AY345857 mRNA. Translation: AAQ22764.1 .
AC083845 Genomic DNA. No translation available.
AC103817 Genomic DNA. No translation available.
BC015380 mRNA. Translation: AAH15380.2 .
BC036065 mRNA. Translation: AAH36065.1 .
U96113 mRNA. Translation: AAC51324.1 .
CCDSi CCDS6242.1. [Q9H0M0-1 ]
RefSeqi NP_008944.1. NM_007013.3. [Q9H0M0-1 ]
XP_005250817.1. XM_005250760.2. [Q9H0M0-1 ]
UniGenei Hs.655189.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1ND7 X-ray 2.10 A 546-917 [» ]
2OP7 NMR - A 494-532 [» ]
ProteinModelPortali Q9H0M0.
SMRi Q9H0M0. Positions 19-145, 351-919.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 116243. 57 interactions.
IntActi Q9H0M0. 22 interactions.
MINTi MINT-199541.
STRINGi 9606.ENSP00000265428.

PTM databases

PhosphoSitei Q9H0M0.

Polymorphism databases

DMDMi 32171908.

Proteomic databases

MaxQBi Q9H0M0.
PaxDbi Q9H0M0.
PRIDEi Q9H0M0.

Protocols and materials databases

DNASUi 11059.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000265428 ; ENSP00000265428 ; ENSG00000123124 . [Q9H0M0-1 ]
ENST00000341922 ; ENSP00000340564 ; ENSG00000123124 . [Q9H0M0-3 ]
ENST00000349423 ; ENSP00000342665 ; ENSG00000123124 . [Q9H0M0-6 ]
ENST00000517970 ; ENSP00000427793 ; ENSG00000123124 . [Q9H0M0-1 ]
GeneIDi 11059.
KEGGi hsa:11059.
UCSCi uc003ydt.3. human. [Q9H0M0-1 ]

Organism-specific databases

CTDi 11059.
GeneCardsi GC08P087424.
HGNCi HGNC:17004. WWP1.
HPAi HPA023180.
MIMi 602307. gene.
neXtProti NX_Q9H0M0.
PharmGKBi PA134960138.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5021.
HOGENOMi HOG000208453.
HOVERGENi HBG004134.
InParanoidi Q9H0M0.
KOi K05633.
OMAi KNGIVQT.
OrthoDBi EOG7RFTGT.
PhylomeDBi Q9H0M0.
TreeFami TF323658.

Enzyme and pathway databases

UniPathwayi UPA00143 .
Reactomei REACT_115828. Downregulation of ERBB4 signaling.
REACT_160189. Stimuli-sensing channels.
REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
SignaLinki Q9H0M0.

Miscellaneous databases

ChiTaRSi WWP1. human.
EvolutionaryTracei Q9H0M0.
GeneWikii WWP1.
GenomeRNAii 11059.
NextBioi 42019.
PROi Q9H0M0.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9H0M0.
Bgeei Q9H0M0.
CleanExi HS_WWP1.
Genevestigatori Q9H0M0.

Family and domain databases

Gene3Di 2.60.40.150. 1 hit.
InterProi IPR000008. C2_dom.
IPR024928. E3_ub_ligase_SMURF1.
IPR000569. HECT.
IPR001202. WW_dom.
[Graphical view ]
Pfami PF00168. C2. 1 hit.
PF00632. HECT. 1 hit.
PF00397. WW. 4 hits.
[Graphical view ]
PIRSFi PIRSF001569. E3_ub_ligase_SMURF1. 1 hit.
SMARTi SM00239. C2. 1 hit.
SM00119. HECTc. 1 hit.
SM00456. WW. 4 hits.
[Graphical view ]
SUPFAMi SSF49562. SSF49562. 1 hit.
SSF51045. SSF51045. 4 hits.
SSF56204. SSF56204. 1 hit.
PROSITEi PS50004. C2. 1 hit.
PS50237. HECT. 1 hit.
PS01159. WW_DOMAIN_1. 4 hits.
PS50020. WW_DOMAIN_2. 4 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Testis.
  2. "Alternative splicing determines the domain structure of WWP1, a Nedd4 family protein."
    Flasza M., Gorman P., Roylance R., Canfield A.E., Baron M.
    Biochem. Biophys. Res. Commun. 290:431-437(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3; 4; 5 AND 6), TISSUE SPECIFICITY.
    Tissue: Mammary cancer.
  3. "The novel E3 ubiquitin ligase Tiul1 associates with TGIF to target Smad2 for degradation."
    Seo S.R., Lallemand F., Ferrand N., Pessah M., L'Hoste S., Camonis J., Atfi A.
    EMBO J. 23:3780-3792(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, UBIQUITINATION OF SMAD2 AND TGFBR1, INTERACTION WITH SMAD7 AND TGIF.
  4. "DNA sequence and analysis of human chromosome 8."
    Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., Asakawa T.
    , Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., Lander E.S.
    Nature 439:331-335(2006) [PubMed] [Europe PMC] [Abstract]
    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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Lung and Testis.
  6. "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] OF 191-870, INTERACTION WITH WBP1; WBP2; SCNN1A; SCNN1B AND SCNN1G.
    Tissue: Bone marrow and Brain.
  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 DRPLA, TISSUE SPECIFICITY.
  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] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PIII.
  9. "Negative regulation of transforming growth factor-beta (TGF-beta) signaling by WW domain-containing protein 1 (WWP1)."
    Komuro A., Imamura T., Saitoh M., Yoshida Y., Yamori T., Miyazono K., Miyazawa K.
    Oncogene 23:6914-6923(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN UBIQUITINATION OF TGFBR1; SMAD6 AND SMAD7, INTERACTION WITH SMAD1; SMAD2; SMAD3; SMAD5; SMAD6; SMAD7; TGFBR1; TGFBR2 AND SKIL.
  10. "The WW domain containing E3 ubiquitin protein ligase 1 upregulates ErbB2 and EGFR through RING finger protein 11."
    Chen C., Zhou Z., Liu R., Li Y., Azmi P.B., Seth A.K.
    Oncogene 27:6845-6855(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: AUTOUBIQUITINATION.
  11. "Endogenous spartin (SPG20) is recruited to endosomes and lipid droplets and interacts with the ubiquitin E3 ligases AIP4 and AIP5."
    Edwards T.L., Clowes V.E., Tsang H.T., Connell J.W., Sanderson C.M., Luzio J.P., Reid E.
    Biochem. J. 423:31-39(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SPG20.
  12. "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.
  13. "WW domain containing E3 ubiquitin protein ligase 1 targets the full-length ErbB4 for ubiquitin-mediated degradation in breast cancer."
    Li Y., Zhou Z., Alimandi M., Chen C.
    Oncogene 28:2948-2958(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ERBB4.
  14. "Conformational flexibility underlies ubiquitin ligation mediated by the WWP1 HECT domain E3 ligase."
    Verdecia M.A., Joazeiro C.A.P., Wells N.J., Ferrer J.-L., Bowman M.E., Hunter T., Noel J.P.
    Mol. Cell 11:249-259(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 546-917, MUTAGENESIS OF GLU-614; HIS-621; ASP-675; GLU-798; MET-804; GLU-806; ARG-845; GLN-848 AND ARG-855, FUNCTION.

Entry informationi

Entry nameiWWP1_HUMAN
AccessioniPrimary (citable) accession number: Q9H0M0
Secondary accession number(s): O00307, Q5YLC1, Q96BP4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 20, 2003
Last sequence update: March 1, 2001
Last modified: September 3, 2014
This is version 134 of the entry and version 1 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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 8
    Human chromosome 8: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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