Q9Y577 (TRI17_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

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	477 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	May function as an 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 process	Ubl conjugation pathway
Coding sequence diversity	Alternative splicing
Domain	Coiled coil Zinc-finger
Ligand	Metal-binding Zinc
Molecular function	Ligase
PTM	Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	protein autoubiquitination Inferred from direct assay Ref.5. Source: UniProtKB
Cellular_component	intracellular Inferred from electronic annotation. Source: InterPro
Molecular_function	ubiquitin-protein ligase 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
TRIM39	Q9HCM9	3	EBI-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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 477	477	E3 ubiquitin-protein ligase TRIM17		PRO_0000056224
Regions
	Domain	277 – 475	199	B30.2/SPRY
	Zinc finger	16 – 66	51	RING-type
	Zinc finger	94 – 135	42	B box-type
	Coiled coil	135 – 223	89	Potential
Natural variations
	Alternative sequence	295 – 343	49	EDVVP…CAVGQ → GKWAPRARTSDPGSLGDAPL YPLASEATNGGGSTSALPGD GHWLFTVPS in isoform 2.		VSP_040994
	Alternative sequence	344 – 477	134	Missing in isoform 2.		VSP_040995

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 1, 1999. Version 1. Checksum: ECA4010661ADD28A	FASTA	477	54,418
	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
	Isoform 2 [UniParc]. Checksum: A57AD2D4185048EF	FASTA	343	39,153
	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 RGFLGKWAPR 310 320 330 340 ARTSDPGSLG DAPLYPLASE ATNGGGSTSA LPGDGHWLFT VPS

References

	« Hide 'large scale' referencesShow '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. , 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. , 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.
IPI	IPI00479218. IPI00913955.
RefSeq	NP_001020111.1. NM_001024940.2. NP_001128327.1. NM_001134855.1. NP_057186.1. NM_016102.3.
UniGene	Hs.121748.
3D structure databases
ProteinModelPortal	Q9Y577.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9Y577. 12 interactions.
MINT	MINT-1433750.
STRING	9606.ENSP00000347794.
PTM databases
PhosphoSite	Q9Y577.
Polymorphism databases
DMDM	38605530.
Proteomic databases
PaxDb	Q9Y577.
PRIDE	Q9Y577.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000295033; ENSP00000295033; ENSG00000162931. ENST00000366697; ENSP00000355658; ENSG00000162931. ENST00000366698; ENSP00000355659; ENSG00000162931. ENST00000456946; ENSP00000403312; ENSG00000162931.
GeneID	51127.
KEGG	hsa:51127.
UCSC	uc001hsu.3. human. uc009xfb.2. human.
Organism-specific databases
CTD	51127.
GeneCards	GC01M228595.
HGNC	HGNC:13430. TRIM17.
HPA	HPA054908.
MIM	606123. gene.
neXtProt	NX_Q9Y577.
PharmGKB	PA37768.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG317461.
HOGENOM	HOG000234134.
HOVERGEN	HBG001357.
InParanoid	Q9Y577.
KO	K12007.
OMA	HYWEVGL.
PhylomeDB	Q9Y577.
Enzyme and pathway databases
UniPathway	UPA00143.
Gene expression databases
ArrayExpress	Q9Y577.
Bgee	Q9Y577.
CleanEx	HS_TRIM17.
Genevestigator	Q9Y577.
GermOnline	ENSG00000162931. Homo sapiens.
Family and domain databases
Gene3D	3.30.40.10. 1 hit.
InterPro	IPR001870. 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. IPR018957. Znf_C3HC4_RING-type. IPR001841. Znf_RING. IPR013083. Znf_RING/FYVE/PHD. IPR017907. Znf_RING_CS. [Graphical view]
Pfam	PF00622. SPRY. 1 hit. PF00643. zf-B_box. 1 hit. PF00097. zf-C3HC4. 1 hit. [Graphical view]
PRINTS	PR01407. BUTYPHLNCDUF.
SMART	SM00336. BBOX. 1 hit. SM00589. PRY. 1 hit. SM00184. RING. 1 hit. SM00449. SPRY. 1 hit. [Graphical view]
SUPFAM	SSF49899. ConA_like_lec_gl. 1 hit.
PROSITE	PS50188. B302_SPRY. 1 hit. PS50119. ZF_BBOX. 1 hit. PS00518. ZF_RING_1. 1 hit. PS50089. ZF_RING_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	51127.
NextBio	53935.
SOURCE	Search...

Entry information

Entry name

TRI17_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 116 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.