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Protein

E3 ubiquitin-protein ligase TRIM62

Gene

TRIM62

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

Functioni

E3 ubiquitin ligase whose activity is dependent on E2 ubiquitin-conjugating enzyme UBE2D2.1 Publication

Pathwayi: protein ubiquitination

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

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri11 – 5444RING-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri88 – 12841B box-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  • ligase activity Source: UniProtKB-KW
  • ubiquitin-protein transferase activity Source: CACAO
  • zinc ion binding Source: InterPro

GO - Biological processi

  • innate immune response Source: UniProtKB
  • interferon-gamma-mediated signaling pathway Source: Reactome
  • negative regulation of epithelial to mesenchymal transition Source: Ensembl
  • negative regulation of viral transcription Source: UniProtKB
  • positive regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
  • positive regulation of NF-kappaB transcription factor activity Source: UniProtKB
  • positive regulation of sequence-specific DNA binding transcription factor activity Source: UniProtKB
  • regulation of viral entry into host cell Source: UniProtKB
  • regulation of viral release from host cell Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-HSA-877300. Interferon gamma signaling.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
E3 ubiquitin-protein ligase TRIM62 (EC:6.3.2.-)
Alternative name(s):
Tripartite motif-containing protein 62
Gene namesi
Name:TRIM62
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:25574. TRIM62.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: CACAO
  • cytosol Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134890243.

Polymorphism and mutation databases

BioMutaiTRIM62.
DMDMi74752380.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 475475E3 ubiquitin-protein ligase TRIM62PRO_0000249574Add
BLAST

Post-translational modificationi

Polyubiquitinated, autoubiquitinated in the presence of UBE2D2.1 Publication

Keywords - PTMi

Ubl conjugation

Proteomic databases

PaxDbiQ9BVG3.
PRIDEiQ9BVG3.

PTM databases

iPTMnetiQ9BVG3.
PhosphoSiteiQ9BVG3.

Expressioni

Gene expression databases

BgeeiQ9BVG3.
CleanExiHS_TRIM62.
GenevisibleiQ9BVG3. HS.

Interactioni

Subunit structurei

Interacts with the ubiquitin-conjugating enzyme, UBE2D2.1 Publication

Protein-protein interaction databases

BioGridi120518. 11 interactions.
IntActiQ9BVG3. 5 interactions.
MINTiMINT-1181483.
STRINGi9606.ENSP00000291416.

Structurei

3D structure databases

ProteinModelPortaliQ9BVG3.
SMRiQ9BVG3. Positions 5-73, 93-472.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini277 – 475199B30.2/SPRYPROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili127 – 241115Sequence analysisAdd
BLAST

Domaini

The RING finger is required for ubiquitin ligase activity.

Sequence similaritiesi

Belongs to the TRIM/RBCC family.Curated
Contains 1 B box-type zinc finger.PROSITE-ProRule annotation
Contains 1 B30.2/SPRY domain.PROSITE-ProRule annotation
Contains 1 RING-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri11 – 5444RING-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri88 – 12841B box-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Coiled coil, Zinc-finger

Phylogenomic databases

eggNOGiENOG410ITEQ. Eukaryota.
ENOG410XNZK. LUCA.
GeneTreeiENSGT00760000118838.
HOGENOMiHOG000234133.
HOVERGENiHBG103330.
InParanoidiQ9BVG3.
KOiK12030.
OMAiFQDISPV.
OrthoDBiEOG7M98FZ.
PhylomeDBiQ9BVG3.
TreeFamiTF342569.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
4.10.45.10. 1 hit.
InterProiIPR001870. B30.2/SPRY.
IPR003879. Butyrophylin.
IPR013320. ConA-like_dom.
IPR006574. PRY.
IPR003877. SPRY_dom.
IPR000315. Znf_B-box.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
PfamiPF13765. PRY. 1 hit.
PF00622. SPRY. 1 hit.
PF00643. zf-B_box. 1 hit.
[Graphical view]
PRINTSiPR01407. BUTYPHLNCDUF.
SMARTiSM00589. PRY. 1 hit.
SM00184. RING. 1 hit.
SM00449. SPRY. 1 hit.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 1 hit.
PROSITEiPS50188. B302_SPRY. 1 hit.
PS50119. ZF_BBOX. 1 hit.
PS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9BVG3-1) [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
MACSLKDELL CSICLSIYQD PVSLGCEHYF CRRCITEHWV RQEAQGARDC
60 70 80 90 100
PECRRTFAEP ALAPSLKLAN IVERYSSFPL DAILNARRAA RPCQAHDKVK
110 120 130 140 150
LFCLTDRALL CFFCDEPALH EQHQVTGIDD AFDELQRELK DQLQALQDSE
160 170 180 190 200
REHTEALQLL KRQLAETKSS TKSLRTTIGE AFERLHRLLR ERQKAMLEEL
210 220 230 240 250
EADTARTLTD IEQKVQRYSQ QLRKVQEGAQ ILQERLAETD RHTFLAGVAS
260 270 280 290 300
LSERLKGKIH ETNLTYEDFP TSKYTGPLQY TIWKSLFQDI HPVPAALTLD
310 320 330 340 350
PGTAHQRLIL SDDCTIVAYG NLHPQPLQDS PKRFDVEVSV LGSEAFSSGV
360 370 380 390 400
HYWEVVVAEK TQWVIGLAHE AASRKGSIQI QPSRGFYCIV MHDGNQYSAC
410 420 430 440 450
TEPWTRLNVR DKLDKVGVFL DYDQGLLIFY NADDMSWLYT FREKFPGKLC
460 470
SYFSPGQSHA NGKNVQPLRI NTVRI
Length:475
Mass (Da):54,268
Last modified:June 1, 2001 - v1
Checksum:iDC15CA9B795DFBB0
GO
Isoform 2 (identifier: Q9BVG3-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-15: MACSLKDELLCSICL → MPEKTAVDQPWTQAL
     16-136: Missing.

Note: No experimental confirmation available.
Show »
Length:354
Mass (Da):40,490
Checksum:iED5ED8F092F7EDA9
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti102 – 1021F → L in BAA91792 (PubMed:14702039).Curated
Sequence conflicti474 – 4741R → L in BAA91792 (PubMed:14702039).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 1515MACSL…CSICL → MPEKTAVDQPWTQAL in isoform 2. 1 PublicationVSP_055441Add
BLAST
Alternative sequencei16 – 136121Missing in isoform 2. 1 PublicationVSP_055442Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK001621 mRNA. Translation: BAA91792.1.
AK122896 mRNA. Translation: BAG53787.1.
AK300177 mRNA. Translation: BAG61956.1.
AL662907 Genomic DNA. Translation: CAH70402.1.
CH471059 Genomic DNA. Translation: EAX07466.1.
CH471059 Genomic DNA. Translation: EAX07467.1.
BC001222 mRNA. Translation: AAH01222.1.
BC007999 mRNA. Translation: AAH07999.1.
BC011689 mRNA. Translation: AAH11689.1.
BC012152 mRNA. Translation: AAH12152.1.
CCDSiCCDS376.1. [Q9BVG3-1]
RefSeqiNP_060677.2. NM_018207.2. [Q9BVG3-1]
XP_011540007.1. XM_011541705.1. [Q9BVG3-2]
UniGeneiHs.656006.

Genome annotation databases

EnsembliENST00000291416; ENSP00000291416; ENSG00000116525. [Q9BVG3-1]
ENST00000543586; ENSP00000441173; ENSG00000116525. [Q9BVG3-2]
GeneIDi55223.
KEGGihsa:55223.
UCSCiuc001bxb.4. human. [Q9BVG3-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK001621 mRNA. Translation: BAA91792.1.
AK122896 mRNA. Translation: BAG53787.1.
AK300177 mRNA. Translation: BAG61956.1.
AL662907 Genomic DNA. Translation: CAH70402.1.
CH471059 Genomic DNA. Translation: EAX07466.1.
CH471059 Genomic DNA. Translation: EAX07467.1.
BC001222 mRNA. Translation: AAH01222.1.
BC007999 mRNA. Translation: AAH07999.1.
BC011689 mRNA. Translation: AAH11689.1.
BC012152 mRNA. Translation: AAH12152.1.
CCDSiCCDS376.1. [Q9BVG3-1]
RefSeqiNP_060677.2. NM_018207.2. [Q9BVG3-1]
XP_011540007.1. XM_011541705.1. [Q9BVG3-2]
UniGeneiHs.656006.

3D structure databases

ProteinModelPortaliQ9BVG3.
SMRiQ9BVG3. Positions 5-73, 93-472.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi120518. 11 interactions.
IntActiQ9BVG3. 5 interactions.
MINTiMINT-1181483.
STRINGi9606.ENSP00000291416.

PTM databases

iPTMnetiQ9BVG3.
PhosphoSiteiQ9BVG3.

Polymorphism and mutation databases

BioMutaiTRIM62.
DMDMi74752380.

Proteomic databases

PaxDbiQ9BVG3.
PRIDEiQ9BVG3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000291416; ENSP00000291416; ENSG00000116525. [Q9BVG3-1]
ENST00000543586; ENSP00000441173; ENSG00000116525. [Q9BVG3-2]
GeneIDi55223.
KEGGihsa:55223.
UCSCiuc001bxb.4. human. [Q9BVG3-1]

Organism-specific databases

CTDi55223.
GeneCardsiTRIM62.
HGNCiHGNC:25574. TRIM62.
neXtProtiNX_Q9BVG3.
PharmGKBiPA134890243.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410ITEQ. Eukaryota.
ENOG410XNZK. LUCA.
GeneTreeiENSGT00760000118838.
HOGENOMiHOG000234133.
HOVERGENiHBG103330.
InParanoidiQ9BVG3.
KOiK12030.
OMAiFQDISPV.
OrthoDBiEOG7M98FZ.
PhylomeDBiQ9BVG3.
TreeFamiTF342569.

Enzyme and pathway databases

UniPathwayiUPA00143.
ReactomeiR-HSA-877300. Interferon gamma signaling.

Miscellaneous databases

GenomeRNAii55223.
PROiQ9BVG3.

Gene expression databases

BgeeiQ9BVG3.
CleanExiHS_TRIM62.
GenevisibleiQ9BVG3. HS.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
4.10.45.10. 1 hit.
InterProiIPR001870. B30.2/SPRY.
IPR003879. Butyrophylin.
IPR013320. ConA-like_dom.
IPR006574. PRY.
IPR003877. SPRY_dom.
IPR000315. Znf_B-box.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
PfamiPF13765. PRY. 1 hit.
PF00622. SPRY. 1 hit.
PF00643. zf-B_box. 1 hit.
[Graphical view]
PRINTSiPR01407. BUTYPHLNCDUF.
SMARTiSM00589. PRY. 1 hit.
SM00184. RING. 1 hit.
SM00449. SPRY. 1 hit.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 1 hit.
PROSITEiPS50188. B302_SPRY. 1 hit.
PS50119. ZF_BBOX. 1 hit.
PS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Tissue: Placenta and Synovium.
  2. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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: Eye.
  5. "Characterization of TRIM62 as a RING finger E3 ubiquitin ligase and its subcellular localization."
    Huang F., Xiao H., Sun B.L., Yang R.G.
    Biochem. Biophys. Res. Commun. 432:208-213(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, POLYUBIQUITINATION, SUBCELLULAR LOCATION, INTERACTION WITH UBE2D2.

Entry informationi

Entry nameiTRI62_HUMAN
AccessioniPrimary (citable) accession number: Q9BVG3
Secondary accession number(s): B3KVH5
, B4DTE4, D3DPR1, Q9NVG0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 19, 2006
Last sequence update: June 1, 2001
Last modified: June 8, 2016
This is version 132 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

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 one 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.