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O60858 (TRI13_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 137. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length407 AA.
Sequence statusComplete.
Protein existenceEvidence 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 processUbl conjugation pathway
   Cellular componentEndoplasmic reticulum
Membrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainCoiled coil
Transmembrane
Transmembrane helix
Zinc-finger
   LigandMetal-binding
Zinc
   Molecular functionLigase
   PTMUbl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processER-associated ubiquitin-dependent protein catabolic process

Inferred from direct assay Ref.12. Source: UniProtKB

anatomical structure morphogenesis

Traceable author statement Ref.1. Source: ProtInc

innate immune response

Inferred from direct assay PubMed 18248090. Source: UniProt

negative regulation of viral release from host cell

Inferred from direct assay PubMed 18248090. Source: UniProt

negative regulation of viral transcription

Inferred from direct assay PubMed 18248090. Source: UniProt

positive regulation of I-kappaB kinase/NF-kappaB signaling

Inferred from mutant phenotype PubMed 12761501. Source: UniProtKB

positive regulation of NF-kappaB transcription factor activity

Inferred from mutant phenotype PubMed 23077300. Source: UniProt

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

proteasome-mediated ubiquitin-dependent protein catabolic process

Inferred from direct assay Ref.12. Source: UniProtKB

protein autoubiquitination

Inferred from direct assay Ref.12. Source: UniProtKB

response to gamma radiation

Inferred from expression pattern Ref.13. Source: UniProtKB

signal transduction

Inferred from mutant phenotype PubMed 12761501. Source: GOC

   Cellular_componentcytoplasm

Inferred from direct assay Ref.3. Source: UniProtKB

endoplasmic reticulum membrane

Inferred from direct assay Ref.12. Source: UniProtKB

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

perinuclear endoplasmic reticulum

Inferred from direct assay Ref.12Ref.14. Source: UniProtKB

   Molecular_functionprotein binding

Inferred from physical interaction Ref.12Ref.13Ref.14. Source: UniProtKB

signal transducer activity

Inferred from mutant phenotype PubMed 12761501. Source: UniProtKB

ubiquitin-protein transferase 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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 407407E3 ubiquitin-protein ligase TRIM13
PRO_0000056028

Regions

Transmembrane317 – 33721Helical; Potential
Zinc finger10 – 5849RING-type
Zinc finger89 – 13143B box-type
Coiled coil172 – 20029 Potential

Natural variations

Alternative sequence11M → MDVM in isoform 3.
VSP_038142
Alternative sequence1751L → D in isoform 2.
VSP_005746
Alternative sequence176 – 407232Missing in isoform 2.
VSP_005747
Natural variant3551S → T. Ref.1 Ref.3 Ref.5 Ref.9
Corresponds to variant rs1056543 [ dbSNP | Ensembl ].
VAR_013512

Experimental info

Mutagenesis131C → 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 LengthMass (Da)Tools
Isoform 1 (Alpha) [UniParc].

Last modified July 19, 2005. Version 2.
Checksum: 94B624345124AEBF

FASTA40746,988
        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 

« Hide

Isoform 2 (Beta) [UniParc].

Checksum: 006850E437E0D9B9
Show »

FASTA17519,841
Isoform 3 [UniParc].

Checksum: E37CAD3F938C6C93
Show »

FASTA41047,333

References

« Hide '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. expand/collapse author list , 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. 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 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. expand/collapse author list , 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. expand/collapse author list , 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, IDENTIFICATION BY 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, IDENTIFICATION BY 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.
CCDSCCDS41888.1. [O60858-3]
CCDS9423.1. [O60858-1]
RefSeqNP_001007279.1. NM_001007278.2. [O60858-3]
NP_005789.2. NM_005798.4. [O60858-1]
NP_434698.1. NM_052811.3. [O60858-1]
NP_998755.1. NM_213590.2. [O60858-1]
UniGeneHs.436922.

3D structure databases

ProteinModelPortalO60858.
SMRO60858. Positions 4-57.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115501. 14 interactions.
STRING9606.ENSP00000298772.

PTM databases

PhosphoSiteO60858.

Proteomic databases

MaxQBO60858.
PaxDbO60858.
PRIDEO60858.

Protocols and materials databases

DNASU10206.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000298772; ENSP00000298772; ENSG00000204977. [O60858-3]
ENST00000356017; ENSP00000348299; ENSG00000204977. [O60858-3]
ENST00000378182; ENSP00000367424; ENSG00000204977. [O60858-1]
ENST00000420995; ENSP00000412943; ENSG00000204977. [O60858-1]
ENST00000457662; ENSP00000399206; ENSG00000204977. [O60858-1]
GeneID10206.
KEGGhsa:10206.
UCSCuc001vdp.1. human. [O60858-3]
uc001vdq.1. human. [O60858-1]

Organism-specific databases

CTD10206.
GeneCardsGC13P050570.
HGNCHGNC:9976. TRIM13.
HPAHPA000367.
MIM605661. gene.
neXtProtNX_O60858.
PharmGKBPA162406947.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG238872.
HOVERGENHBG056536.
InParanoidO60858.
KOK12003.
OMAICCSLFD.
OrthoDBEOG7KWSHJ.
PhylomeDBO60858.
TreeFamTF331669.

Enzyme and pathway databases

UniPathwayUPA00143.

Gene expression databases

BgeeO60858.
CleanExHS_TRIM13.
GenevestigatorO60858.

Family and domain databases

Gene3D3.30.40.10. 1 hit.
4.10.45.10. 1 hit.
InterProIPR000315. Znf_B-box.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
PfamPF00643. zf-B_box. 1 hit.
PF13639. zf-RING_2. 1 hit.
[Graphical view]
SMARTSM00336. BBOX. 1 hit.
SM00184. RING. 1 hit.
[Graphical view]
PROSITEPS50119. ZF_BBOX. 1 hit.
PS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi10206.
NextBio38634.
PROO60858.
SOURCESearch...

Entry information

Entry nameTRI13_HUMAN
AccessionPrimary (citable) accession number: O60858
Secondary accession number(s): B2RB49 expand/collapse secondary AC list , Q5UBW0, Q5W0U8, Q5W0U9, Q9BQ47, Q9C021
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: July 19, 2005
Last modified: July 9, 2014
This is version 137 of the entry and version 2 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 polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 13

Human chromosome 13: entries, gene names and cross-references to MIM