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Q9Y577 (TRI17_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 128. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
E3 ubiquitin-protein ligase TRIM17

EC=6.3.2.-
Alternative name(s):
RING finger protein 16
Testis RING finger protein
Tripartite motif-containing protein 17
Gene names
Name:TRIM17
Synonyms:RBCC, RNF16, TERF
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length477 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May function as a ubiquitin E3 ligase. Ref.5

Pathway

Protein modification; protein ubiquitination.

Subunit structure

Interacts (via coiled coil) with TRIM44 (via coiled coil). Ref.5

Tissue specificity

Almost exclusively in the testis. Ref.5

Post-translational modification

Auto-ubiquitinated.

Sequence similarities

Belongs to the TRIM/RBCC family.

Contains 1 B box-type zinc finger.

Contains 1 B30.2/SPRY domain.

Contains 1 RING-type zinc finger.

Ontologies

Keywords
   Biological processUbl conjugation pathway
   Coding sequence diversityAlternative splicing
   DomainCoiled coil
Zinc-finger
   LigandMetal-binding
Zinc
   Molecular functionLigase
   PTMUbl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processprotein autoubiquitination

Inferred from direct assay Ref.5. Source: UniProtKB

   Cellular_componentintracellular

Inferred from electronic annotation. Source: InterPro

   Molecular_functionprotein binding

Inferred from physical interaction Ref.5. Source: UniProtKB

ubiquitin-protein transferase activity

Inferred from direct assay Ref.5. Source: UniProtKB

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

TRIM39Q9HCM93EBI-743894,EBI-739510

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9Y577-1)

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: Q9Y577-2)

The sequence of this isoform differs from the canonical sequence as follows:
     295-343: EDVVPDATSA...FVAYPCAVGQ → GKWAPRARTS...DGHWLFTVPS
     344-477: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 477477E3 ubiquitin-protein ligase TRIM17
PRO_0000056224

Regions

Domain277 – 475199B30.2/SPRY
Zinc finger16 – 6651RING-type
Zinc finger94 – 13542B box-type
Coiled coil135 – 22389 Potential

Natural variations

Alternative sequence295 – 34349EDVVP…CAVGQ → GKWAPRARTSDPGSLGDAPL YPLASEATNGGGSTSALPGD GHWLFTVPS in isoform 2.
VSP_040994
Alternative sequence344 – 477134Missing in isoform 2.
VSP_040995

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: ECA4010661ADD28A

FASTA47754,418
        10         20         30         40         50         60 
MEAVELARKL QEEATCSICL DYFTDPVMTT CGHNFCRACI QLSWEKARGK KGRRKRKGSF 

        70         80         90        100        110        120 
PCPECREMSP QRNLLPNRLL TKVAEMAQQH PGLQKQDLCQ EHHEPLKLFC QKDQSPICVV 

       130        140        150        160        170        180 
CRESREHRLH RVLPAEEAVQ GYKLKLEEDM EYLREQITRT GNLQAREEQS LAEWQGKVKE 

       190        200        210        220        230        240 
RRERIVLEFE KMNLYLVEEE QRLLQALETE EEETASRLRE SVACLDRQGH SLELLLLQLE 

       250        260        270        280        290        300 
ERSTQGPLQM LQDMKEPLSR KNNVSVQCPE VAPPTRPRTV CRVPGQIEVL RGFLEDVVPD 

       310        320        330        340        350        360 
ATSAYPYLLL YESRQRRYLG SSPEGSGFCS KDRFVAYPCA VGQTAFSSGR HYWEVGMNIT 

       370        380        390        400        410        420 
GDALWALGVC RDNVSRKDRV PKCPENGFWV VQLSKGTKYL STFSALTPVM LMEPPSHMGI 

       430        440        450        460        470 
FLDFEAGEVS FYSVSDGSHL HTYSQATFPG PLQPFFCLGA PKSGQMVIST VTMWVKG 

« Hide

Isoform 2 [UniParc].

Checksum: A57AD2D4185048EF
Show »

FASTA34339,153

References

« Hide 'large scale' references
[1]"Molecular cloning of a novel RING finger-B box-coiled coil (RBCC) protein, terf, expressed in the testis."
Ogawa S., Goto W., Orimo A., Hosoi T., Ouchi Y., Muramatsu M., Inoue S.
Biochem. Biophys. Res. Commun. 251:515-519(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Testis.
[2]"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. expand/collapse author list , 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] (ISOFORM 2).
Tissue: Spleen.
[3]"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. expand/collapse author list , 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].
[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: Brain.
[5]"TRIM44 interacts with and stabilizes terf, a TRIM ubiquitin E3 ligase."
Urano T., Usui T., Takeda S., Ikeda K., Okada A., Ishida Y., Iwayanagi T., Otomo J., Ouchi Y., Inoue S.
Biochem. Biophys. Res. Commun. 383:263-268(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY, AUTOUBIQUITINATION, INTERACTION WITH TRIM44.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF156271 mRNA. Translation: AAD40286.1.
AK301105 mRNA. Translation: BAG62704.1.
AL670729, AL139288 Genomic DNA. Translation: CAH71674.1.
AL139288, AL670729 Genomic DNA. Translation: CAI23334.1.
BC033788 mRNA. Translation: AAH33788.1.
CCDSCCDS1571.1. [Q9Y577-1]
CCDS44327.1. [Q9Y577-2]
RefSeqNP_001020111.1. NM_001024940.2. [Q9Y577-1]
NP_001128327.1. NM_001134855.1. [Q9Y577-2]
NP_057186.1. NM_016102.3. [Q9Y577-1]
XP_006711842.1. XM_006711779.1. [Q9Y577-1]
UniGeneHs.121748.

3D structure databases

ProteinModelPortalQ9Y577.
SMRQ9Y577. Positions 10-65, 96-134, 300-465.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid119314. 18 interactions.
IntActQ9Y577. 12 interactions.
MINTMINT-1433750.
STRING9606.ENSP00000347794.

PTM databases

PhosphoSiteQ9Y577.

Polymorphism databases

DMDM38605530.

Proteomic databases

MaxQBQ9Y577.
PaxDbQ9Y577.
PRIDEQ9Y577.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000295033; ENSP00000295033; ENSG00000162931. [Q9Y577-1]
ENST00000366697; ENSP00000355658; ENSG00000162931. [Q9Y577-1]
ENST00000366698; ENSP00000355659; ENSG00000162931. [Q9Y577-1]
ENST00000456946; ENSP00000403312; ENSG00000162931. [Q9Y577-2]
GeneID51127.
KEGGhsa:51127.
UCSCuc001hsu.3. human. [Q9Y577-1]
uc009xfb.2. human. [Q9Y577-2]

Organism-specific databases

CTD51127.
GeneCardsGC01M228595.
HGNCHGNC:13430. TRIM17.
HPAHPA054908.
MIM606123. gene.
neXtProtNX_Q9Y577.
PharmGKBPA37768.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG317461.
HOGENOMHOG000234134.
HOVERGENHBG001357.
InParanoidQ9Y577.
KOK12007.
OMACAVGQET.
OrthoDBEOG7V49Z8.
PhylomeDBQ9Y577.
TreeFamTF338674.

Enzyme and pathway databases

UniPathwayUPA00143.

Gene expression databases

BgeeQ9Y577.
CleanExHS_TRIM17.
GenevestigatorQ9Y577.

Family and domain databases

Gene3D3.30.40.10. 1 hit.
4.10.45.10. 1 hit.
InterProIPR001870. B30.2/SPRY.
IPR003879. Butyrophylin.
IPR008985. ConA-like_lec_gl_sf.
IPR006574. PRY.
IPR018355. SPla/RYanodine_receptor_subgr.
IPR003877. SPRY_rcpt.
IPR000315. Znf_B-box.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
PfamPF00622. SPRY. 1 hit.
PF00643. zf-B_box. 1 hit.
[Graphical view]
PRINTSPR01407. BUTYPHLNCDUF.
SMARTSM00336. BBOX. 1 hit.
SM00589. PRY. 1 hit.
SM00184. RING. 1 hit.
SM00449. SPRY. 1 hit.
[Graphical view]
SUPFAMSSF49899. SSF49899. 1 hit.
PROSITEPS50188. B302_SPRY. 1 hit.
PS50119. ZF_BBOX. 1 hit.
PS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi51127.
NextBio53935.
PROQ9Y577.
SOURCESearch...

Entry information

Entry nameTRI17_HUMAN
AccessionPrimary (citable) accession number: Q9Y577
Secondary accession number(s): B4DVJ2, Q5VST8
Entry history
Integrated into UniProtKB/Swiss-Prot: November 28, 2003
Last sequence update: November 1, 1999
Last modified: July 9, 2014
This is version 128 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM