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Protein

E3 ubiquitin-protein ligase Itchy

Gene

Itch

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Acts as an 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 (PubMed:15358865, PubMed:16446428, PubMed:17592138, PubMed:18628966, PubMed:20392206, PubMed:25632008). It catalyzes 'Lys-29'-, 'Lys-48'- and 'Lys-63'-linked ubiquitin conjugation (By similarity). Involved in the control of inflammatory signaling pathways (By similarity). Is an essential component of a ubiquitin-editing protein complex, comprising also TNFAIP3, TAX1BP1 and RNF11, that ensures the transient nature of inflammatory signaling pathways (By similarity). Promotes the association of the complex after TNF stimulation (By similarity). Once the complex is formed, TNFAIP3 deubiquitinates 'Lys-63' polyubiquitin chains on RIPK1 and catalyzes the formation of 'Lys-48'-polyubiquitin chains (By similarity). This leads to RIPK1 proteasomal degradation and consequently termination of the TNF- or LPS-mediated activation of NFKB1 (By similarity). Ubiquitinates RIPK2 by 'Lys-63'-linked conjugation and influences NOD2-dependent signal transduction pathways (By similarity). Regulates the transcriptional activity of several transcription factors involved in immune response (PubMed:15358865, PubMed:11828324). Ubiquitinates NFE2 by 'Lys-63' linkages and is implicated in the control of the development of hematopoietic lineages (By similarity). Mediates JUN ubiquitination and degradation (PubMed:15358865). Mediates JUNB ubiquitination and degradation (PubMed:11828324, PubMed:15358865). Critical regulator of type 2 helper T (Th2) cell cytokine production by inducing JUNB ubiquitination and degradation (PubMed:11828324). Involved in the negative regulation of MAVS-dependent cellular antiviral responses (By similarity). Ubiquitinates MAVS through 'Lys-48'-linked conjugation resulting in MAVS proteasomal degradation (By similarity). Following ligand stimulation, regulates sorting of Wnt receptor FZD4 to the degradative endocytic pathway probably by modulating PI42KA activity (By similarity). Ubiquitinates PI4K2A and negatively regulates its catalytic activity (By similarity). Ubiquitinates chemokine receptor CXCR4 and regulates sorting of CXCR4 to the degradative endocytic pathway following ligand stimulation by ubiquitinating endosomal sorting complex required for transport ESCRT-0 components HGS and STAM (By similarity). Targets DTX1 for lysosomal degradation and controls NOTCH1 degradation, in the absence of ligand, through 'Lys-29'-linked polyubiquitination (PubMed:18628966). Ubiquitinates SNX9 (By similarity). Ubiquitinates MAP3K7 through 'Lys-48'-linked conjugation (PubMed:25632008). Involved in the regulation of apoptosis and reactive oxygen species levels through the ubiquitination and proteasomal degradation of TXNIP (By similarity). Mediates the antiapoptotic activity of epidermal growth factor through the ubiquitination and proteasomal degradation of p15 BID (PubMed:20392206). Ubiquitinates BRAT1 and this ubiquitination is enhanced in the presence of NDFIP1 (By similarity).By similarity6 Publications

Caution

It is uncertain whether Met-1 or Met-11 is the initiator.Curated

Catalytic activityi

S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N6-ubiquitinyl-[acceptor protein]-L-lysine.6 Publications

Activity regulationi

Activated by NDFIP1- and NDFIP2-binding (PubMed:25632008). Activated by PI4K2A-binding (By similarity). Inhibited by DTX3L-binding (By similarity). Inhibited by N4BP1 binding (PubMed:17592138).By similarity2 Publications

Pathwayi: protein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.6 Publications
View all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei832Glycyl thioester intermediatePROSITE-ProRule annotation1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionTransferase
Biological processAntiviral defense, Apoptosis, Immunity, Innate immunity, Ubl conjugation pathway

Enzyme and pathway databases

BRENDAi6.3.2.19 3474
ReactomeiR-MMU-1253288 Downregulation of ERBB4 signaling
R-MMU-168638 NOD1/2 Signaling Pathway
R-MMU-2122948 Activated NOTCH1 Transmits Signal to the Nucleus
R-MMU-5610780 Degradation of GLI1 by the proteasome
R-MMU-5632684 Hedgehog 'on' state
R-MMU-8939236 RUNX1 regulates transcription of genes involved in differentiation of HSCs
R-MMU-983168 Antigen processing: Ubiquitination & Proteasome degradation
UniPathwayi
UPA00143

Names & Taxonomyi

Protein namesi
Recommended name:
E3 ubiquitin-protein ligase Itchy (EC:2.3.2.266 Publications)
Alternative name(s):
HECT-type E3 ubiquitin transferase Itchy homolog
Gene namesi
Name:Itch
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:1202301 Itch

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Endosome, Membrane, Nucleus

Pathology & Biotechi

Involvement in diseasei

Defects in Itch are the cause of the itchy phenotype which is an inflammatory and immunological condition characterized by inflammation in the lung and stomach, hyperplasia in lymphoid and hematopoietic cells and constant itching in the skin.1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi199S → A: No loss of MAPK8-mediated phosphorylation and no effect on ligase activity. Almost complete inactivation of ligase activity; when associated with A-232. Greatly reduced MAPK8-mediated phosphorylation; when associated with A-222 or A-232. Completely abolishes MAPK8-mediated phosphorylation; when associated with A-222 and A-232. 1 Publication1
Mutagenesisi199S → D: More sensitive to in vitro proteolysis. 1 Publication1
Mutagenesisi222T → A: No loss of MAPK8-mediated phosphorylation. Greatly reduced MAPK8-mediated phosphorylation; when associated with A-199 or A-232. Completely abolishes MAPK8-mediated phosphorylation; when associated with A-199 and A-232. 1 Publication1
Mutagenesisi222T → D: Inhibits in vitro interaction between ITCH HECT domain and PRR/WW motifs. More sensitive to in vitro proteolysis. 1 Publication1
Mutagenesisi232S → A: No loss of MAPK8-mediated phosphorylation and no effect on ligase activity. Almost complete inactivation of ligase activity; when associated with A-199. Greatly reduced MAPK8-mediated phosphorylation; when associated with A-199 or A-222. Completely abolishes MAPK8-mediated phosphorylation; when associated with A-199 and A-222. 1 Publication1
Mutagenesisi232S → D: More sensitive to in vitro proteolysis. 1 Publication1
Mutagenesisi535 – 540RRRLWV → AAALWA: Abolishes interaction with MAPK8. 1 Publication6
Mutagenesisi535 – 537RRR → AAA: Almost complete loss of interaction with MAPK8. 3
Mutagenesisi535 – 536RR → AA: Greatly decreased interaction with MAPK8 and ligase activity. 2
Mutagenesisi832C → A: Loss of ubiquitin protein ligase activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00001203182 – 864E3 ubiquitin-protein ligase ItchyAdd BLAST863

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserineBy similarity1
Modified residuei199Phosphoserine; by MAPK81 Publication1
Modified residuei222Phosphothreonine; by MAPK81 Publication1
Modified residuei232Phosphoserine; by MAPK81 Publication1
Modified residuei346Phosphothreonine; by SGK3By similarity1
Modified residuei381Phosphotyrosine; by FYNBy similarity1
Modified residuei411Phosphoserine; by SGK3By similarity1

Post-translational modificationi

On T-cell activation, phosphorylation by the JNK cascade on serine and threonine residues surrounding the PRR domain accelerates the ubiquitination and degradation of JUN and JUNB. The increased ITCH catalytic activity due to phosphorylation by JNK1 may occur due to a conformational change disrupting the interaction between the PRR/WW motifs domain and the HECT domain and, thus exposing the HECT domain. Phosphorylation by FYN reduces interaction with JUNB and negatively controls JUN ubiquitination and degradation.4 Publications
Monoubiquitinated. Autopolyubiquitinated with 'Lys-63' linkages which does not lead to protein degradation.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ8C863
PaxDbiQ8C863
PeptideAtlasiQ8C863
PRIDEiQ8C863

PTM databases

iPTMnetiQ8C863
PhosphoSitePlusiQ8C863

Expressioni

Tissue specificityi

Detected in uterus (at protein level) (PubMed:23146885). Widely expressed (PubMed:9462742).2 Publications

Gene expression databases

BgeeiENSMUSG00000027598 Expressed in 288 organ(s), highest expression level in rostral migratory stream
CleanExiMM_ITCH
GenevisibleiQ8C863 MM

Interactioni

Subunit structurei

Monomer. Interacts (via WW domains) with OCNL (PubMed:11782481). Interacts (via WW domains) with NOTCH1 (PubMed:10940313, PubMed:18628966). Interacts (via WW domains) JUN (PubMed:11828324). Interacts with JUNB; the interaction promotes ITCH-mediated ubiquitination and degradation of JUNB (PubMed:11828324). Interacts with FYN; the interaction phosphorylates ITCH on Tyr-381 decreasing binding of JUNB (By similarity). Interacts (via WW domain 2) with N4BP1; the interaction inhibits the E3 ubiquitin-protein ligase activity (PubMed:17592138). Interacts with NDFIP1 and NDFIP2; the interaction with NDFIP proteins activates the E3 ubiquitin-protein ligase and may induce its recruitment to exosomes (PubMed:11748237, PubMed:17137798, PubMed:25632008). Interacts with ARHGEF7 (By similarity). Interacts with RNF11 (By similarity). Interacts (via the WW 1 domain) with NFE2 (via the PXY motif 1); the interaction promotes 'Lys-63'-linked ubiquitination of NFE2, retains it in the cytoplasm and prevents its transactivation activity (By similarity). Interacts (via WW domains) with CXCR4 (via C-terminus); the interaction depends on CXCR4 phosphorylation (By similarity). Found in a complex with E3 ligase DTX3L and ESCRT-0 components HGS and STAM (By similarity). Interacts with DTX3L (via C-terminus); the interaction is increased upon CXCL12 stimulation and inhibits ITCH catalytic activity (the interaction is direct) (By similarity). Interacts with HGS (By similarity). Interacts (via WW domains) with PCBP2 within a complex containing ITCH, MAVS and PCBP2 (By similarity). Interacts (via WW domains) with TXNIP (via C-terminus) (By similarity). Interacts with p15 BID (PubMed:20392206). Interacts with ERBB4 (By similarity).Interacts with DTX1 (By similarity). Interacts with SPART (By similarity). Interacts with SNX9 and SNX18 (By similarity). Interacts (via its WW domains) with ATN1 (By similarity). Interacts (via WW domains) with SGK3 (By similarity). Interacts with CBLC (By similarity). Interacts with OTUD7B (By similarity). Interacts (via WW domain 1,2 and 3) with PI4K2A; the interaction inhibits PI4K2A catalytic activity and promotes ITCH catalytic activity (PubMed:23146885). Interacts with ARRDC4 (By similarity). Part of a complex containing ITCH, NDFIP1 and MAP3K7 (PubMed:25632008). Interacts with UBE2L3; the interaction is mediated by NDFIP1 (PubMed:25632008). Interacts with MAPK8/JNK1 (PubMed:16446428). Interacts (via WW domains) with ARRDC1 (via PPxY motifs); the interaction is direct and participates to the recruitment of the ubiquitin-protein ligase ITCH to the NOTCH1 receptor (By similarity). Interacts (via WW domains) with ARRDC2 (By similarity). Interacts (via WW domains) with ARRDC3 (By similarity).By similarity10 Publications
(Microbial infection) Interacts with Epstein-Barr virus LMP2A.1 Publication

Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

BioGridi200813, 24 interactors
DIPiDIP-29318N
ELMiQ8C863
IntActiQ8C863, 13 interactors
MINTiQ8C863
STRINGi10090.ENSMUSP00000029126

Structurei

Secondary structure

1864
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliQ8C863
SMRiQ8C863
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8C863

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini5 – 99C2PROSITE-ProRule annotationAdd BLAST95
Domaini287 – 320WW 1PROSITE-ProRule annotationAdd BLAST34
Domaini319 – 352WW 2PROSITE-ProRule annotationAdd BLAST34
Domaini399 – 432WW 3PROSITE-ProRule annotationAdd BLAST34
Domaini439 – 472WW 4PROSITE-ProRule annotationAdd BLAST34
Domaini530 – 864HECTPROSITE-ProRule annotationAdd BLAST335

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni356 – 432Required for interaction with FYNBy similarityAdd BLAST77
Regioni535 – 544MAP kinase docking site10

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi211 – 226Arg/Pro-rich (PRR domain)Add BLAST16

Domaini

The WW domains mediate interaction with PPxY motif-containing proteins.By similarity

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG0940 Eukaryota
COG5021 LUCA
GeneTreeiENSGT00760000118966
HOVERGENiHBG004134
InParanoidiQ8C863
KOiK05632
OMAiETRVNTN
OrthoDBiEOG091G0SS8
PhylomeDBiQ8C863
TreeFamiTF323658

Family and domain databases

CDDicd00078 HECTc, 1 hit
cd00201 WW, 4 hits
Gene3Di2.60.40.150, 1 hit
InterProiView protein in InterPro
IPR000008 C2_dom
IPR035892 C2_domain_sf
IPR024928 E3_ub_ligase_SMURF1
IPR000569 HECT_dom
IPR035983 Hect_E3_ubiquitin_ligase
IPR001202 WW_dom
IPR036020 WW_dom_sf
PfamiView protein in Pfam
PF00168 C2, 1 hit
PF00632 HECT, 1 hit
PF00397 WW, 3 hits
PIRSFiPIRSF001569 E3_ub_ligase_SMURF1, 1 hit
SMARTiView protein in SMART
SM00239 C2, 1 hit
SM00119 HECTc, 1 hit
SM00456 WW, 4 hits
SUPFAMiSSF51045 SSF51045, 4 hits
SSF56204 SSF56204, 1 hit
PROSITEiView protein in PROSITE
PS50004 C2, 1 hit
PS50237 HECT, 1 hit
PS01159 WW_DOMAIN_1, 4 hits
PS50020 WW_DOMAIN_2, 4 hits

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket
Isoform 1 (identifier: Q8C863-1) [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
MSDSGPQLDS MGSLTMKSQL QITVISAKLK ENKKNWFGPS PYVEVTVDGQ
60 70 80 90 100
SKKTEKCNNT NSPKWKQPLT VIVTPTSKLC FRVWSHQTLK SDVLLGTAGL
110 120 130 140 150
DIYETLKSNN MKLEEVVMTL QLVGDKEPTE TMGDLSVCLD GLQVEAEVVT
160 170 180 190 200
NGETSCSEST TQNDDGCRTR DDTRVSTNGS EDPEVAASGE NKRANGNNSP
210 220 230 240 250
SLSNGGFKPS RPPRPSRPPP PTPRRPASVN GSPSTNSDSD GSSTGSLPPT
260 270 280 290 300
NTNVNTSTSE GATSGLIIPL TISGGSGPRP LNTVSQAPLP PGWEQRVDQH
310 320 330 340 350
GRVYYVDHVE KRTTWDRPEP LPPGWERRVD NMGRIYYVDH FTRTTTWQRP
360 370 380 390 400
TLESVRNYEQ WQLQRSQLQG AMQQFNQRFI YGNQDLFATS QNKEFDPLGP
410 420 430 440 450
LPPGWEKRTD SNGRVYFVNH NTRITQWEDP RSQGQLNEKP LPEGWEMRFT
460 470 480 490 500
VDGIPYFVDH NRRATTYIDP RTGKSALDNG PQIAYVRDFK AKVQYFRFWC
510 520 530 540 550
QQLAMPQHIK ITVTRKTLFE DSFQQIMSFS PQDLRRRLWV IFPGEEGLDY
560 570 580 590 600
GGVAREWFFL LSHEVLNPMY CLFEYAGKDN YCLQINPASY INPDHLKYFR
610 620 630 640 650
FIGRFIAMAL FHGKFIDTGF SLPFYKRILN KPVGLKDLES IDPEFYNSLI
660 670 680 690 700
WVKENNIEEC GLEMYFSVDK EILGEIKSHD LKPNGGNILV TEENKEEYIR
710 720 730 740 750
MVAEWRLSRG VEEQTQAFFE GFNEILPQQY LQYFDAKELE VLLCGMQEID
760 770 780 790 800
LNDWQRHAIY RHYTRTSKQI MWFWQFVKEI DNEKRMRLLQ FVTGTCRLPV
810 820 830 840 850
GGFADLMGSN GPQKFCIEKV GKENWLPRSH TCFNRLDLPP YKSYEQLKEK
860
LLFAIEETEG FGQE
Note: Major form.
Length:864
Mass (Da):98,994
Last modified:October 3, 2003 - v2
Checksum:i905FDBE00A1EA7EA
GO
Isoform 2 (identifier: Q8C863-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     742-759: LLCGMQEIDLNDWQRHAI → MNFYLLKHTSKYSFRYLF
     760-864: Missing.

Show »
Length:759
Mass (Da):86,702
Checksum:iB1820795111F666B
GO

Sequence cautioni

The sequence AAB99764 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_008452742 – 759LLCGM…QRHAI → MNFYLLKHTSKYSFRYLF in isoform 2. 1 PublicationAdd BLAST18
Alternative sequenceiVSP_008453760 – 864Missing in isoform 2. 1 PublicationAdd BLAST105

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF037454 mRNA Translation: AAB99764.1 Different initiation.
AK048303 mRNA Translation: BAC33298.1
BC062934 mRNA Translation: AAH62934.1
CCDSiCCDS38293.1 [Q8C863-1]
RefSeqiNP_001230641.1, NM_001243712.1 [Q8C863-1]
NP_032421.2, NM_008395.3 [Q8C863-1]
UniGeneiMm.208286
Mm.490088

Genome annotation databases

EnsembliENSMUST00000029126; ENSMUSP00000029126; ENSMUSG00000027598 [Q8C863-1]
ENSMUST00000109685; ENSMUSP00000105307; ENSMUSG00000027598 [Q8C863-1]
GeneIDi16396
KEGGimmu:16396
UCSCiuc008nkd.1 mouse [Q8C863-2]
uc008nke.2 mouse [Q8C863-1]

Keywords - Coding sequence diversityi

Alternative splicing

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF037454 mRNA Translation: AAB99764.1 Different initiation.
AK048303 mRNA Translation: BAC33298.1
BC062934 mRNA Translation: AAH62934.1
CCDSiCCDS38293.1 [Q8C863-1]
RefSeqiNP_001230641.1, NM_001243712.1 [Q8C863-1]
NP_032421.2, NM_008395.3 [Q8C863-1]
UniGeneiMm.208286
Mm.490088

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1YIUNMR-A399-432[»]
2JO9NMR-A399-432[»]
2JOCNMR-A399-432[»]
5XMCX-ray2.60A143-864[»]
ProteinModelPortaliQ8C863
SMRiQ8C863
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi200813, 24 interactors
DIPiDIP-29318N
ELMiQ8C863
IntActiQ8C863, 13 interactors
MINTiQ8C863
STRINGi10090.ENSMUSP00000029126

PTM databases

iPTMnetiQ8C863
PhosphoSitePlusiQ8C863

Proteomic databases

EPDiQ8C863
PaxDbiQ8C863
PeptideAtlasiQ8C863
PRIDEiQ8C863

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000029126; ENSMUSP00000029126; ENSMUSG00000027598 [Q8C863-1]
ENSMUST00000109685; ENSMUSP00000105307; ENSMUSG00000027598 [Q8C863-1]
GeneIDi16396
KEGGimmu:16396
UCSCiuc008nkd.1 mouse [Q8C863-2]
uc008nke.2 mouse [Q8C863-1]

Organism-specific databases

CTDi83737
MGIiMGI:1202301 Itch

Phylogenomic databases

eggNOGiKOG0940 Eukaryota
COG5021 LUCA
GeneTreeiENSGT00760000118966
HOVERGENiHBG004134
InParanoidiQ8C863
KOiK05632
OMAiETRVNTN
OrthoDBiEOG091G0SS8
PhylomeDBiQ8C863
TreeFamiTF323658

Enzyme and pathway databases

UniPathwayi
UPA00143

BRENDAi6.3.2.19 3474
ReactomeiR-MMU-1253288 Downregulation of ERBB4 signaling
R-MMU-168638 NOD1/2 Signaling Pathway
R-MMU-2122948 Activated NOTCH1 Transmits Signal to the Nucleus
R-MMU-5610780 Degradation of GLI1 by the proteasome
R-MMU-5632684 Hedgehog 'on' state
R-MMU-8939236 RUNX1 regulates transcription of genes involved in differentiation of HSCs
R-MMU-983168 Antigen processing: Ubiquitination & Proteasome degradation

Miscellaneous databases

ChiTaRSiItch mouse
EvolutionaryTraceiQ8C863
PROiPR:Q8C863
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000027598 Expressed in 288 organ(s), highest expression level in rostral migratory stream
CleanExiMM_ITCH
GenevisibleiQ8C863 MM

Family and domain databases

CDDicd00078 HECTc, 1 hit
cd00201 WW, 4 hits
Gene3Di2.60.40.150, 1 hit
InterProiView protein in InterPro
IPR000008 C2_dom
IPR035892 C2_domain_sf
IPR024928 E3_ub_ligase_SMURF1
IPR000569 HECT_dom
IPR035983 Hect_E3_ubiquitin_ligase
IPR001202 WW_dom
IPR036020 WW_dom_sf
PfamiView protein in Pfam
PF00168 C2, 1 hit
PF00632 HECT, 1 hit
PF00397 WW, 3 hits
PIRSFiPIRSF001569 E3_ub_ligase_SMURF1, 1 hit
SMARTiView protein in SMART
SM00239 C2, 1 hit
SM00119 HECTc, 1 hit
SM00456 WW, 4 hits
SUPFAMiSSF51045 SSF51045, 4 hits
SSF56204 SSF56204, 1 hit
PROSITEiView protein in PROSITE
PS50004 C2, 1 hit
PS50237 HECT, 1 hit
PS01159 WW_DOMAIN_1, 4 hits
PS50020 WW_DOMAIN_2, 4 hits
ProtoNetiSearch...

Entry informationi

Entry nameiITCH_MOUSE
AccessioniPrimary (citable) accession number: Q8C863
Secondary accession number(s): O54971
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 3, 2003
Last sequence update: October 3, 2003
Last modified: November 7, 2018
This is version 164 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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