O60858 (TRI13_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
E3 ubiquitin-protein ligase TRIM13
EC=6.3.2.-

Alternative name(s):
B-cell chronic lymphocytic leukemia tumor suppressor Leu5
Leukemia-associated protein 5
Putative tumor suppressor RFP2
RING finger protein 77
Ret finger protein 2
Tripartite motif-containing protein 13

Gene names

Name:	TRIM13
Synonyms:	LEU5, RFP2, RNF77

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

General annotation (Comments)

Function	E3 ubiquitin ligase involved in the retrotranslocation and turnover of membrane and secretory proteins from the ER through a set of processes named ER-associated degradation (ERAD). This process acts on misfolded proteins as well as in the regulated degradation of correctly folded proteins. Enhances ionizing radiation-induced p53/TP53 stability and apoptosis via ubiquitinating MDM2 and AKT1 and decreasing AKT1 kinase activity through MDM2 and AKT1 proteasomal degradation. Regulates ER stress-induced autophagy, and may act as a tumor suppressor. Ref.12 Ref.13 Ref.14
Pathway	Protein modification; protein ubiquitination.
Subunit structure	Interacts (via C-terminal domain) with VCP. Interacts with AKT1; the interaction ubiquitinates AKT1 and leads to its proteasomal degradation. Interacts with MDM2; the interaction ubiquitinates AKT1 and leads to its proteasomal degradation. Interacts with p62/SQSTM1. Ref.12 Ref.13 Ref.14
Subcellular location	Endoplasmic reticulum membrane; Single-pass membrane protein. Note: Concentrates and colocalizes with p62/SQSTM1 and ZFYVE1 at the perinuclear endoplasmic reticulum. Ref.12 Ref.13 Ref.14
Domain	The coiled-coil domain is required for the induction of autophagy during endoplasmic reticulum (ER) stress. The RING-type zinc finger is required for auto-polyubiquitination. The C-terminal domain transmembrane domain is indispensable for the localization to the ER.
Post-translational modification	Auto-ubiquitinated; requires the RING-type zinc finger. Auto-polyubiquitination leads to proteasomal degradation.
Miscellaneous	Located on chromosome 13 within the minimal deletion region for B-cell chronic lymphocytic leukemia.
Sequence similarities	Belongs to the TRIM/RBCC family. Contains 1 B box-type zinc finger. Contains 1 RING-type zinc finger.

Ontologies

Keywords
Biological process	Ubl conjugation pathway
Cellular component	Endoplasmic reticulum Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Coiled coil Transmembrane Transmembrane helix Zinc-finger
Ligand	Metal-binding Zinc
Molecular function	Ligase
PTM	Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	ER-associated protein catabolic process Inferred from direct assay Ref.12. Source: UniProtKB anatomical structure morphogenesis Traceable author statement Ref.1. Source: ProtInc positive regulation of I-kappaB kinase/NF-kappaB cascade Inferred from mutant phenotype PubMed 12761501. Source: UniProtKB positive regulation of cell death Inferred from direct assay Ref.13. Source: UniProtKB positive regulation of macroautophagy Inferred from direct assay Ref.14. Source: UniProtKB protein autoubiquitination Inferred from direct assay Ref.12. Source: UniProtKB response to gamma radiation Inferred from expression pattern Ref.13. Source: UniProtKB
Cellular_component	cytoplasm Inferred from direct assay Ref.3. Source: UniProtKB endoplasmic reticulum membrane Inferred from direct assay Ref.12. Source: UniProtKB integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW perinuclear endoplasmic reticulum Inferred from direct assay Ref.12Ref.14. Source: UniProtKB
Molecular_function	signal transducer activity Inferred from mutant phenotype PubMed 12761501. Source: UniProtKB ubiquitin-protein ligase activity Inferred from direct assay Ref.12. Source: UniProtKB zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: O60858-1)

Also known as: Alpha;

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: O60858-2)

Also known as: Beta;

The sequence of this isoform differs from the canonical sequence as follows:
     175-175: L → D
     176-407: Missing.

Isoform 3 (identifier: O60858-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MDVM

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 407	407	E3 ubiquitin-protein ligase TRIM13		PRO_0000056028
Regions
	Transmembrane	317 – 337	21	Helical; Potential
	Zinc finger	10 – 58	49	RING-type
	Zinc finger	89 – 131	43	B box-type
	Coiled coil	172 – 200	29	Potential
Natural variations
	Alternative sequence	1	1	M → MDVM in isoform 3.		VSP_038142
	Alternative sequence	175	1	L → D in isoform 2.		VSP_005746
	Alternative sequence	176 – 407	232	Missing in isoform 2.		VSP_005747
	Natural variant	355	1	S → T. Ref.1 Ref.3 Ref.5 Ref.9 Corresponds to variant rs1056543 [ dbSNP | Ensembl ].		VAR_013512
Experimental info
	Mutagenesis	13	1	C → A: Absence of polyubiquitination. Stability of protein increased. No enhanced apoptosis on ionizing radiation induction. No ubiquitination of AKT1 or MDM2. Decreased p53/TP53 stability. No effect on induction of autophagy during ER stress. Ref.12 Ref.13 Ref.14

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (Alpha) [UniParc]. Last modified July 19, 2005. Version 2. Checksum: 94B624345124AEBF	FASTA	407	46,988
	10 20 30 40 50 60 MELLEEDLTC PICCSLFDDP RVLPCSHNFC KKCLEGILEG SVRNSLWRPA PFKCPTCRKE 70 80 90 100 110 120 TSATGINSLQ VNYSLKGIVE KYNKIKISPK MPVCKGHLGQ PLNIFCLTDM QLICGICATR 130 140 150 160 170 180 GEHTKHVFCS IEDAYAQERD AFESLFQSFE TWRRGDALSR LDTLETSKRK SLQLLTKDSD 190 200 210 220 230 240 KVKEFFEKLQ HTLDQKKNEI LSDFETMKLA VMQAYDPEIN KLNTILQEQR MAFNIAEAFK 250 260 270 280 290 300 DVSEPIVFLQ QMQEFREKIK VIKETPLPPS NLPASPLMKN FDTSQWEDIK LVDVDKLSLP 310 320 330 340 350 360 QDTGTFISKI PWSFYKLFLL ILLLGLVIVF GPTMFLEWSL FDDLATWKGC LSNFSSYLTK 370 380 390 400 TADFIEQSVF YWEQVTDGFF IFNERFKNFT LVVLNNVAEF VCKYKLL
	Isoform 2 (Beta) [UniParc]. Checksum: 006850E437E0D9B9	FASTA	175	19,841
	10 20 30 40 50 60 MELLEEDLTC PICCSLFDDP RVLPCSHNFC KKCLEGILEG SVRNSLWRPA PFKCPTCRKE 70 80 90 100 110 120 TSATGINSLQ VNYSLKGIVE KYNKIKISPK MPVCKGHLGQ PLNIFCLTDM QLICGICATR 130 140 150 160 170 GEHTKHVFCS IEDAYAQERD AFESLFQSFE TWRRGDALSR LDTLETSKRK SLQLD
	Isoform 3 [UniParc]. Checksum: E37CAD3F938C6C93	FASTA	410	47,333
	10 20 30 40 50 60 MDVMELLEED LTCPICCSLF DDPRVLPCSH NFCKKCLEGI LEGSVRNSLW RPAPFKCPTC 70 80 90 100 110 120 RKETSATGIN SLQVNYSLKG IVEKYNKIKI SPKMPVCKGH LGQPLNIFCL TDMQLICGIC 130 140 150 160 170 180 ATRGEHTKHV FCSIEDAYAQ ERDAFESLFQ SFETWRRGDA LSRLDTLETS KRKSLQLLTK 190 200 210 220 230 240 DSDKVKEFFE KLQHTLDQKK NEILSDFETM KLAVMQAYDP EINKLNTILQ EQRMAFNIAE 250 260 270 280 290 300 AFKDVSEPIV FLQQMQEFRE KIKVIKETPL PPSNLPASPL MKNFDTSQWE DIKLVDVDKL 310 320 330 340 350 360 SLPQDTGTFI SKIPWSFYKL FLLILLLGLV IVFGPTMFLE WSLFDDLATW KGCLSNFSSY 370 380 390 400 410 LTKTADFIEQ SVFYWEQVTD GFFIFNERFK NFTLVVLNNV AEFVCKYKLL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A cosmid and cDNA fine physical map of a human chromosome 13q14 region frequently lost in B-cell chronic lymphocytic leukemia and identification of a new putative tumor suppressor gene, Leu5." Kapanadze B., Kashuba V., Baranova A., Rasool O., van Everdink W.J., Liu Y., Syomov A., Corcoran M., Poltaraus A., Brodyansky V., Syomova N., Kazakov A., Ibbotson R., van den Berg A., Gizatullin R., Fedorova L., Sulimova G., Zelenin A. , Deaven L., Lehrach H., Grander D., Buys C., Oscier D., Zabarovsky E.R., Einhorn S., Yankovsky N. FEBS Lett. 426:266-270(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT THR-355. Tissue: Leukemia.
[2]	"Nucleotide sequence, transcription map, and mutation analysis of the 13q14 chromosomal region deleted in B-cell chronic lymphocytic leukemia." Migliazza A., Bosch F., Komatsu H., Cayanis E., Martinotti S., Toniato E., Guccione E., Qu X., Chien M., Murty V.V., Gaidano G., Inghirami G., Zhang P., Fischer S., Kalachikov S.M., Russo J., Edelman I., Efstratiadis A., Dalla-Favera R. Blood 97:2098-2104(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORM 1).
[3]	"The tripartite motif family identifies cell compartments." Reymond A., Meroni G., Fantozzi A., Merla G., Cairo S., Luzi L., Riganelli D., Zanaria E., Messali S., Cainarca S., Guffanti A., Minucci S., Pelicci P.G., Ballabio A. EMBO J. 20:2140-2151(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), VARIANT THR-355.
[4]	"RFP2, c13ORF1, and FAM10A4 are the most likely tumor suppressor gene candidates for B-cell chronic lymphocytic leukemia." van Everdink W.J., Baranova A., Lummen C., Tyazhelova T., Looman M.W., Ivanov D., Verlind E., Pestova A., Faber H., van der Veen A.Y., Yankovsky N., Vellenga E., Buys C.H. Cancer Genet. Cytogenet. 146:48-57(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[5]	"RFP2 putative tumor suppressor gene: genomic organization, multiple mRNA isoforms and evaluation as a B-cell chronic lymphocytic leukaemia candidate." Baranova A.V., Sangfelt O., Ivanov D.V., Borodina T.A., Yankovsky N.K. Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), VARIANT THR-355.
[6]	Corcoran M.M., Hammarsund M., Grander D., Oscier D., Kapanadze B., Einhorn S., Sangfelt O. Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[7]	"Alternative isoform of candidate tumor suppressor RFP2." Corcoran M.M., Lerner M., Sangfelt O. Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
[8]	"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 1). Tissue: Brain.
[9]	"The DNA sequence and analysis of human chromosome 13." Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T. , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L., Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T. Nature 428:522-528(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT THR-355.
[10]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[11]	"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: Blood and Lung.
[12]	"The RBCC gene RFP2 (Leu5) encodes a novel transmembrane E3 ubiquitin ligase involved in ERAD." Lerner M., Corcoran M., Cepeda D., Nielsen M.L., Zubarev R., Ponten F., Uhlen M., Hober S., Grander D., Sangfelt O. Mol. Biol. Cell 18:1670-1682(2007) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION AS AN E3 UBIQUITIN LIGASE, AUTOUBIQUITINATION, SUBCELLULAR LOCATION, MUTAGENESIS OF CYS-13, MASS SPECTROMETRY, INTERACTION WITH VCP.
[13]	"Ret finger protein 2 enhances ionizing radiation-induced apoptosis via degradation of AKT and MDM2." Joo H.M., Kim J.Y., Jeong J.B., Seong K.M., Nam S.Y., Yang K.H., Kim C.S., Kim H.S., Jeong M., An S., Jin Y.W. Eur. J. Cell Biol. 90:420-431(2011) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION AS AN E3 UBIQUITIN LIGASE, AUTOUBIQUITINATION, SUBCELLULAR LOCATION, MUTAGENESIS OF CYS-13, MASS SPECTROMETRY, INTERACTION WITH MDM2 AND AKT1.
[14]	"TRIM13 regulates ER stress induced autophagy and clonogenic ability of the cells." Tomar D., Singh R., Singh A.K., Pandya C.D., Singh R. Biochim. Biophys. Acta 1823:316-326(2012) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, AUTOUBIQUITINATION, SUBCELLULAR LOCATION, MUTAGENESIS OF CYS-13, INTERACTION WITH SQSTM1.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AJ224819 mRNA. Translation: CAA12136.1. AF279660 Genomic DNA. Translation: AAK13059.1. AF220127 mRNA. Translation: AAG53500.1. AF220128 mRNA. Translation: AAG53501.1. AY191002 mRNA. Translation: AAO38979.1. AF241849 Genomic DNA. Translation: AAK51624.1. AF241850 mRNA. Translation: AAF91315.1. AY455758 mRNA. Translation: AAR31110.1. AY764035 mRNA. Translation: AAV51406.1. AK314496 mRNA. Translation: BAG37096.1. AL137060 Genomic DNA. Translation: CAC43391.1. AL137060 Genomic DNA. Translation: CAH72825.1. AL137060 Genomic DNA. Translation: CAH72826.1. CH471075 Genomic DNA. Translation: EAX08844.1. CH471075 Genomic DNA. Translation: EAX08845.1. BC003579 mRNA. Translation: AAH03579.1. BC063407 mRNA. Translation: AAH63407.1.
IPI	IPI00477161. IPI00607858. IPI00944555.
RefSeq	NP_001007279.1. NM_001007278.1. NP_005789.2. NM_005798.3. NP_434698.1. NM_052811.2. NP_998755.1. NM_213590.1.
UniGene	Hs.436922.
3D structure databases
ProteinModelPortal	O60858.
ModBase	Search...
Protein-protein interaction databases
STRING	9606.ENSP00000298772.
PTM databases
PhosphoSite	O60858.
Proteomic databases
PaxDb	O60858.
PRIDE	O60858.
Protocols and materials databases
DNASU	10206.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000298772; ENSP00000298772; ENSG00000204977. ENST00000356017; ENSP00000348299; ENSG00000204977. ENST00000378182; ENSP00000367424; ENSG00000204977. ENST00000378183; ENSP00000367425; ENSG00000204977. ENST00000420995; ENSP00000412943; ENSG00000204977. ENST00000442421; ENSP00000404586; ENSG00000204977. ENST00000457662; ENSP00000399206; ENSG00000204977.
GeneID	10206.
KEGG	hsa:10206.
UCSC	uc001vdp.1. human. uc001vdq.1. human.
Organism-specific databases
CTD	10206.
GeneCards	GC13P050570.
HGNC	HGNC:9976. TRIM13.
HPA	HPA000367.
MIM	605661. gene.
neXtProt	NX_O60858.
PharmGKB	PA162406947.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG238872.
HOVERGEN	HBG056536.
InParanoid	O60858.
KO	K12003.
OMA	QPLNIFC.
OrthoDB	EOG46MBJP.
PhylomeDB	O60858.
Enzyme and pathway databases
UniPathway	UPA00143.
Gene expression databases
Bgee	O60858.
CleanEx	HS_TRIM13.
Genevestigator	O60858.
GermOnline	ENSG00000204977. Homo sapiens.
Family and domain databases
Gene3D	3.30.40.10. 1 hit.
InterPro	IPR000315. Znf_B-box. IPR001841. Znf_RING. IPR013083. Znf_RING/FYVE/PHD. IPR017907. Znf_RING_CS. [Graphical view]
Pfam	PF00643. zf-B_box. 1 hit. [Graphical view]
SMART	SM00336. BBOX. 1 hit. SM00184. RING. 1 hit. [Graphical view]
PROSITE	PS50119. ZF_BBOX. 1 hit. PS00518. ZF_RING_1. 1 hit. PS50089. ZF_RING_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	10206.
NextBio	38634.
SOURCE	Search...

Entry information

Entry name

TRI13_HUMAN

Accession

Primary (citable) accession number: O60858
Secondary accession number(s): B2RB49 , Q5UBW0, Q5W0U8, Q5W0U9, Q9BQ47, Q9C021

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	July 19, 2005
Last modified:	May 1, 2013
This is version 125 of the entry and version 2 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.