Q9H0M0 (WWP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:

WWP1

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	922 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. 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. Ref.3 Ref.9 Ref.14
Enzyme regulation	Activated by NDFIP1- and NDFIP2-binding.
Pathway	Protein modification; protein ubiquitination.
Subunit structure	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 Probable; this interaction activates the E3 ubiquitin-protein ligase. Interacts with TGIF. Ref.3 Ref.6 Ref.7 Ref.8 Ref.9 Ref.11 Ref.13
Subcellular location	Cytoplasm By similarity. Cell membrane; Peripheral membrane protein By similarity. Nucleus By similarity.
Tissue specificity	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. Ref.2 Ref.7
Post-translational modification	Auto-ubiquitinated and ubiquitinated by RNF11.
Sequence similarities	Contains 1 C2 domain. Contains 1 HECT (E6AP-type E3 ubiquitin-protein ligase) domain. Contains 4 WW domains.

Ontologies

Keywords
Biological process	Host-virus interaction Ubl conjugation pathway
Cellular component	Cell membrane Cytoplasm Membrane Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Repeat
Molecular function	Ligase
PTM	Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	central nervous system development Non-traceable author statement Ref.7. Source: UniProtKB negative regulation of transcription, DNA-dependent Inferred from sequence or structural similarity. Source: UniProtKB proteasomal ubiquitin-dependent protein catabolic process Inferred from electronic annotation. Source: Compara protein ubiquitination involved in ubiquitin-dependent protein catabolic process Inferred from Biological aspect of Ancestor. Source: RefGenome signal transduction Non-traceable author statement Ref.6. Source: UniProtKB viral entry into host cell Traceable author statement Ref.8. Source: UniProtKB
Cellular_component	cytosol Traceable author statement. Source: Reactome nucleus Inferred from Biological aspect of Ancestor. Source: RefGenome plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell ubiquitin ligase complex Non-traceable author statement Ref.6. Source: UniProtKB
Molecular_function	ubiquitin-protein ligase activity Traceable author statement Ref.6. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CPSF6	Q16630	3	EBI-742157,EBI-358410

Alternative products

This entry describes 6 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist.

Isoform 1 (identifier: Q9H0M0-1)

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.

Isoform 2 (identifier: Q9H0M0-2)

Also known as: B;

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

Isoform 3 (identifier: Q9H0M0-3)

Also known as: C;

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

Isoform 4 (identifier: Q9H0M0-4)

Also known as: D;

The sequence of this isoform is not available.

Isoform 5 (identifier: Q9H0M0-5)

Also known as: E;

The sequence of this isoform is not available.

Isoform 6 (identifier: Q9H0M0-6)

Also known as: F;

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

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 922

922

NEDD4-like E3 ubiquitin-protein ligase WWP1

PRO_0000120336

Regions

Domain

5 – 98

94

C2

Domain

349 – 382

34

WW 1

Domain

381 – 414

34

WW 2

Domain

456 – 489

34

WW 3

Domain

496 – 529

34

WW 4

Domain

588 – 922

335

HECT

Sites

Active site

890

1

Glycyl thioester intermediate By similarity

Site

890

1

Required for ubiquitin-thioester formation By similarity

Natural variations

Alternative sequence

23 – 240

218

Missing in isoform 6.

VSP_007600

Alternative sequence

112 – 242

131

LERVK…ADDTV → F in isoform 3.

VSP_007602

Alternative sequence

112 – 120

9

LERVKEQLK → CWLLKARME in isoform 2.

VSP_007601

Alternative sequence

121 – 922

802

Missing in isoform 2.

VSP_007603

Natural variant

852

1

G → V.
Corresponds to variant rs1059901 [ dbSNP | Ensembl ].

VAR_052960

Experimental info

Mutagenesis

614

1

E → A: Reduces ubiquitin transfer. Ref.14

Mutagenesis

621

1

H → A: Strongly reduces ubiquitin transfer. Ref.14

Mutagenesis

675

1

D → A: Reduces ubiquitin transfer. Ref.14

Mutagenesis

798

1

E → A: Reduces ubiquitin transfer. Strongly reduces ubiquitin transfer; when associated with A-845. Ref.14

Mutagenesis

804

1

M → P: Strongly reduces ubiquitin transfer; when associated with P-806. Ref.14

Mutagenesis

806

1

E → P: Strongly reduces ubiquitin transfer; when associated with P-804. Ref.14

Mutagenesis

845

1

R → A: No effect. Ref.14

Mutagenesis

848

1

Q → A: Abolishes ubiquitin transfer; when associated with A-855. Ref.14

Mutagenesis

855

1

R → A: Abolishes ubiquitin transfer; when associated with A-848. Ref.14

Secondary structure

1

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922

Helix Strand Turn

Details...

Beta strand

500 – 505

6

Turn

509 – 511

3

Beta strand

513 – 518

6

Beta strand

521 – 523

3

Helix

547 – 560

14

Beta strand

564 – 571

8

Turn

573 – 575

3

Helix

576 – 585

10

Helix

589 – 593

5

Beta strand

594 – 600

7

Turn

601 – 603

3

Helix

610 – 623

14

Helix

626 – 628

3

Beta strand

629 – 638

10

Beta strand

641 – 643

3

Helix

645 – 649

5

Helix

653 – 669

17

Helix

680 – 686

7

Helix

693 – 697

5

Helix

701 – 711

11

Beta strand

723 – 726

4

Beta strand

730 – 733

4

Beta strand

737 – 740

4

Helix

743 – 745

3

Turn

750 – 752

3

Helix

753 – 766

14

Turn

767 – 769

3

Helix

770 – 783

14

Helix

786 – 789

4

Helix

794 – 802

9

Helix

809 – 814

6

Beta strand

816 – 820

5

Helix

826 – 837

12

Helix

840 – 851

12

Helix

861 – 863

3

Beta strand

873 – 876

4

Beta strand

886 – 888

3

Helix

889 – 891

3

Beta strand

893 – 895

3

Helix

902 – 914

13

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (A) [UniParc]. Last modified March 1, 2001. Version 1. Checksum: 35B6E1C03A3147DA	FASTA	922	105,202
	10 20 30 40 50 60 MATASPRSDT SNNHSGRLQL QVTVSSAKLK RKKNWFGTAI YTEVVVDGEI TKTAKSSSSS 70 80 90 100 110 120 NPKWDEQLTV NVTPQTTLEF QVWSHRTLKA DALLGKATID LKQALLIHNR KLERVKEQLK 130 140 150 160 170 180 LSLENKNGIA QTGELTVVLD GLVIEQENIT NCSSSPTIEI QENGDALHEN GEPSARTTAR 190 200 210 220 230 240 LAVEGTNGID NHVPTSTLVQ NSCCSYVVNG DNTPSSPSQV AARPKNTPAP KPLASEPADD 250 260 270 280 290 300 TVNGESSSFA PTDNASVTGT PVVSEENALS PNCTSTTVED PPVQEILTSS ENNECIPSTS 310 320 330 340 350 360 AELESEARSI LEPDTSNSRS SSAFEAAKSR QPDGCMDPVR QQSGNANTET LPSGWEQRKD 370 380 390 400 410 420 PHGRTYYVDH NTRTTTWERP QPLPPGWERR VDDRRRVYYV DHNTRTTTWQ RPTMESVRNF 430 440 450 460 470 480 EQWQSQRNQL QGAMQQFNQR YLYSASMLAA ENDPYGPLPP GWEKRVDSTD RVYFVNHNTK 490 500 510 520 530 540 TTQWEDPRTQ GLQNEEPLPE GWEIRYTREG VRYFVDHNTR TTTFKDPRNG KSSVTKGGPQ 550 560 570 580 590 600 IAYERGFRWK LAHFRYLCQS NALPSHVKIN VSRQTLFEDS FQQIMALKPY DLRRRLYVIF 610 620 630 640 650 660 RGEEGLDYGG LAREWFFLLS HEVLNPMYCL FEYAGKNNYC LQINPASTIN PDHLSYFCFI 670 680 690 700 710 720 GRFIAMALFH GKFIDTGFSL PFYKRMLSKK LTIKDLESID TEFYNSLIWI RDNNIEECGL 730 740 750 760 770 780 EMYFSVDMEI LGKVTSHDLK LGGSNILVTE ENKDEYIGLM TEWRFSRGVQ EQTKAFLDGF 790 800 810 820 830 840 NEVVPLQWLQ YFDEKELEVM LCGMQEVDLA DWQRNTVYRH YTRNSKQIIW FWQFVKETDN 850 860 870 880 890 900 EVRMRLLQFV TGTCRLPLGG FAELMGSNGP QKFCIEKVGK DTWLPRSHTC FNRLDLPPYK 910 920 SYEQLKEKLL FAIEETEGFG QE
	Isoform 2 (B) [UniParc]. Checksum: 952B6A78C5D4B93D	FASTA	120	13,453
	10 20 30 40 50 60 MATASPRSDT SNNHSGRLQL QVTVSSAKLK RKKNWFGTAI YTEVVVDGEI TKTAKSSSSS 70 80 90 100 110 120 NPKWDEQLTV NVTPQTTLEF QVWSHRTLKA DALLGKATID LKQALLIHNR KCWLLKARME
	Isoform 3 (C) [UniParc]. Checksum: 833D351CC08D9998	FASTA	792	91,548
	10 20 30 40 50 60 MATASPRSDT SNNHSGRLQL QVTVSSAKLK RKKNWFGTAI YTEVVVDGEI TKTAKSSSSS 70 80 90 100 110 120 NPKWDEQLTV NVTPQTTLEF QVWSHRTLKA DALLGKATID LKQALLIHNR KFNGESSSFA 130 140 150 160 170 180 PTDNASVTGT PVVSEENALS PNCTSTTVED PPVQEILTSS ENNECIPSTS AELESEARSI 190 200 210 220 230 240 LEPDTSNSRS SSAFEAAKSR QPDGCMDPVR QQSGNANTET LPSGWEQRKD PHGRTYYVDH 250 260 270 280 290 300 NTRTTTWERP QPLPPGWERR VDDRRRVYYV DHNTRTTTWQ RPTMESVRNF EQWQSQRNQL 310 320 330 340 350 360 QGAMQQFNQR YLYSASMLAA ENDPYGPLPP GWEKRVDSTD RVYFVNHNTK TTQWEDPRTQ 370 380 390 400 410 420 GLQNEEPLPE GWEIRYTREG VRYFVDHNTR TTTFKDPRNG KSSVTKGGPQ IAYERGFRWK 430 440 450 460 470 480 LAHFRYLCQS NALPSHVKIN VSRQTLFEDS FQQIMALKPY DLRRRLYVIF RGEEGLDYGG 490 500 510 520 530 540 LAREWFFLLS HEVLNPMYCL FEYAGKNNYC LQINPASTIN PDHLSYFCFI GRFIAMALFH 550 560 570 580 590 600 GKFIDTGFSL PFYKRMLSKK LTIKDLESID TEFYNSLIWI RDNNIEECGL EMYFSVDMEI 610 620 630 640 650 660 LGKVTSHDLK LGGSNILVTE ENKDEYIGLM TEWRFSRGVQ EQTKAFLDGF NEVVPLQWLQ 670 680 690 700 710 720 YFDEKELEVM LCGMQEVDLA DWQRNTVYRH YTRNSKQIIW FWQFVKETDN EVRMRLLQFV 730 740 750 760 770 780 TGTCRLPLGG FAELMGSNGP QKFCIEKVGK DTWLPRSHTC FNRLDLPPYK SYEQLKEKLL 790 FAIEETEGFG QE
	Isoform 4 (D) (Sequence not available).		–	–
	Isoform 5 (E) (Sequence not available).		–	–
	Isoform 6 (F) [UniParc]. Checksum: B39DCB6841290CF0	FASTA	704	81,649
	10 20 30 40 50 60 MATASPRSDT SNNHSGRLQL QVTVNGESSS FAPTDNASVT GTPVVSEENA LSPNCTSTTV 70 80 90 100 110 120 EDPPVQEILT SSENNECIPS TSAELESEAR SILEPDTSNS RSSSAFEAAK SRQPDGCMDP 130 140 150 160 170 180 VRQQSGNANT ETLPSGWEQR KDPHGRTYYV DHNTRTTTWE RPQPLPPGWE RRVDDRRRVY 190 200 210 220 230 240 YVDHNTRTTT WQRPTMESVR NFEQWQSQRN QLQGAMQQFN QRYLYSASML AAENDPYGPL 250 260 270 280 290 300 PPGWEKRVDS TDRVYFVNHN TKTTQWEDPR TQGLQNEEPL PEGWEIRYTR EGVRYFVDHN 310 320 330 340 350 360 TRTTTFKDPR NGKSSVTKGG PQIAYERGFR WKLAHFRYLC QSNALPSHVK INVSRQTLFE 370 380 390 400 410 420 DSFQQIMALK PYDLRRRLYV IFRGEEGLDY GGLAREWFFL LSHEVLNPMY CLFEYAGKNN 430 440 450 460 470 480 YCLQINPAST INPDHLSYFC FIGRFIAMAL FHGKFIDTGF SLPFYKRMLS KKLTIKDLES 490 500 510 520 530 540 IDTEFYNSLI WIRDNNIEEC GLEMYFSVDM EILGKVTSHD LKLGGSNILV TEENKDEYIG 550 560 570 580 590 600 LMTEWRFSRG VQEQTKAFLD GFNEVVPLQW LQYFDEKELE VMLCGMQEVD LADWQRNTVY 610 620 630 640 650 660 RHYTRNSKQI IWFWQFVKET DNEVRMRLLQ FVTGTCRLPL GGFAELMGSN GPQKFCIEKV 670 680 690 700 GKDTWLPRSH TCFNRLDLPP YKSYEQLKEK LLFAIEETEG FGQE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Towards a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs." Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., Ottenwaelder B., Obermaier B. , Tampe J., Heubner D., Wambutt R., Korn B., Klein M., Poustka A. Genome Res. 11:422-435(2001) [PubMed] [Europe PMC] [Abstract] 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.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00013009.
IPI00328376.
IPI00328377.
IPI00328378.

RefSeq

NP_008944.1. NM_007013.3.

UniGene

Hs.655189.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1ND7	X-ray	2.10	A	546-917	[»]
2OP7	NMR	-	A	494-532	[»]

ProteinModelPortal

Q9H0M0.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9H0M0. 16 interactions.

MINT

MINT-199541.

STRING

9606.ENSP00000265428.

PTM databases

PhosphoSite

Q9H0M0.

Polymorphism databases

DMDM

32171908.

Proteomic databases

PaxDb

Q9H0M0.

PRIDE

Q9H0M0.

Protocols and materials databases

DNASU

11059.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000265428; ENSP00000265428; ENSG00000123124.
ENST00000341922; ENSP00000340564; ENSG00000123124.
ENST00000349423; ENSP00000342665; ENSG00000123124.
ENST00000517970; ENSP00000427793; ENSG00000123124.

GeneID

11059.

KEGG

hsa:11059.

UCSC

uc003ydt.3. human.

Organism-specific databases

CTD

11059.

GeneCards

GC08P087424.

HGNC

HGNC:17004. WWP1.

HPA

HPA023180.

MIM

602307. gene.

neXtProt

NX_Q9H0M0.

PharmGKB

PA134960138.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG5021.

HOGENOM

HOG000208453.

HOVERGEN

HBG004134.

InParanoid

Q9H0M0.

KO

K05633.

OMA

EQLTVNV.

Enzyme and pathway databases

Pathway_Interaction_DB

tgfbrpathway. TGF-beta receptor signaling.

Reactome

REACT_111102. Signal Transduction.
REACT_6900. Immune System.

UniPathway

UPA00143.

Gene expression databases

ArrayExpress

Q9H0M0.

Bgee

Q9H0M0.

CleanEx

HS_WWP1.

Genevestigator

Q9H0M0.

GermOnline

ENSG00000123124. Homo sapiens.

Family and domain databases

InterPro

IPR000008. C2_Ca-dep.
IPR008973. C2_Ca/lipid-bd_dom_CaLB.
IPR018029. C2_membr_targeting.
IPR024928. E3_ub_ligase_SMURF1.
IPR000569. HECT.
IPR001202. WW_dom.
[Graphical view]

Pfam

PF00168. C2. 1 hit.
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. 1 hit.
PS50237. HECT. 1 hit.
PS01159. WW_DOMAIN_1. 4 hits.
PS50020. WW_DOMAIN_2. 4 hits.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

WWP1. human.

EvolutionaryTrace

Q9H0M0.

GenomeRNAi

11059.

NextBio

42019.

SOURCE

Search...

Entry information

Entry name

WWP1_HUMAN

Accession

Primary (citable) accession number: Q9H0M0
Secondary accession number(s): O00307, Q5YLC1, Q96BP4

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 20, 2003
Last sequence update:	March 1, 2001
Last modified:	May 1, 2013
This is version 121 of the entry and version 1 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.