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O60858

- TRI13_HUMAN

UniProt

O60858 - TRI13_HUMAN

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Protein

E3 ubiquitin-protein ligase TRIM13

Gene
TRIM13, LEU5, RFP2, RNF77
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.3 Publications

Pathwayi

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri10 – 5849RING-typeAdd
BLAST
Zinc fingeri89 – 13143B box-typeAdd
BLAST

GO - Molecular functioni

  1. ligase activity Source: UniProtKB-KW
  2. protein binding Source: UniProtKB
  3. signal transducer activity Source: UniProtKB
  4. ubiquitin-protein transferase activity Source: UniProtKB
  5. zinc ion binding Source: InterPro

GO - Biological processi

  1. anatomical structure morphogenesis Source: ProtInc
  2. ER-associated ubiquitin-dependent protein catabolic process Source: UniProtKB
  3. innate immune response Source: UniProt
  4. negative regulation of viral release from host cell Source: UniProt
  5. negative regulation of viral transcription Source: UniProt
  6. positive regulation of cell death Source: UniProtKB
  7. positive regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
  8. positive regulation of macroautophagy Source: UniProtKB
  9. positive regulation of NF-kappaB transcription factor activity Source: UniProt
  10. proteasome-mediated ubiquitin-dependent protein catabolic process Source: UniProtKB
  11. protein autoubiquitination Source: UniProtKB
  12. response to gamma radiation Source: UniProtKB
  13. signal transduction Source: GOC
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
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 namesi
Name:TRIM13
Synonyms:LEU5, RFP2, RNF77
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 13

Organism-specific databases

HGNCiHGNC:9976. TRIM13.

Subcellular locationi

Endoplasmic reticulum membrane; Single-pass membrane protein
Note: Concentrates and colocalizes with p62/SQSTM1 and ZFYVE1 at the perinuclear endoplasmic reticulum.3 Publications

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei317 – 33721Helical; Reviewed predictionAdd
BLAST

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. endoplasmic reticulum membrane Source: UniProtKB
  3. integral component of membrane Source: UniProtKB-KW
  4. perinuclear endoplasmic reticulum Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi13 – 131C → 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. 3 Publications

Organism-specific databases

PharmGKBiPA162406947.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 407407E3 ubiquitin-protein ligase TRIM13PRO_0000056028Add
BLAST

Post-translational modificationi

Auto-ubiquitinated; requires the RING-type zinc finger. Auto-polyubiquitination leads to proteasomal degradation.

Keywords - PTMi

Ubl conjugation

Proteomic databases

MaxQBiO60858.
PaxDbiO60858.
PRIDEiO60858.

PTM databases

PhosphoSiteiO60858.

Expressioni

Gene expression databases

BgeeiO60858.
CleanExiHS_TRIM13.
GenevestigatoriO60858.

Organism-specific databases

HPAiHPA000367.

Interactioni

Subunit structurei

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/SQSTM1.3 Publications

Protein-protein interaction databases

BioGridi115501. 14 interactions.
STRINGi9606.ENSP00000298772.

Structurei

3D structure databases

ProteinModelPortaliO60858.
SMRiO60858. Positions 4-57.

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili172 – 20029 Reviewed predictionAdd
BLAST

Domaini

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.

Sequence similaritiesi

Belongs to the TRIM/RBCC family.

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri10 – 5849RING-typeAdd
BLAST
Zinc fingeri89 – 13143B box-typeAdd
BLAST

Keywords - Domaini

Coiled coil, Transmembrane, Transmembrane helix, Zinc-finger

Phylogenomic databases

eggNOGiNOG238872.
HOVERGENiHBG056536.
InParanoidiO60858.
KOiK12003.
OMAiICCSLFD.
OrthoDBiEOG7KWSHJ.
PhylomeDBiO60858.
TreeFamiTF331669.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
4.10.45.10. 1 hit.
InterProiIPR000315. Znf_B-box.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
PfamiPF00643. zf-B_box. 1 hit.
PF13639. zf-RING_2. 1 hit.
[Graphical view]
SMARTiSM00336. BBOX. 1 hit.
SM00184. RING. 1 hit.
[Graphical view]
PROSITEiPS50119. ZF_BBOX. 1 hit.
PS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: O60858-1) [UniParc]FASTAAdd to Basket

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.

« Hide

MELLEEDLTC PICCSLFDDP RVLPCSHNFC KKCLEGILEG SVRNSLWRPA    50
PFKCPTCRKE TSATGINSLQ VNYSLKGIVE KYNKIKISPK MPVCKGHLGQ 100
PLNIFCLTDM QLICGICATR GEHTKHVFCS IEDAYAQERD AFESLFQSFE 150
TWRRGDALSR LDTLETSKRK SLQLLTKDSD KVKEFFEKLQ HTLDQKKNEI 200
LSDFETMKLA VMQAYDPEIN KLNTILQEQR MAFNIAEAFK DVSEPIVFLQ 250
QMQEFREKIK VIKETPLPPS NLPASPLMKN FDTSQWEDIK LVDVDKLSLP 300
QDTGTFISKI PWSFYKLFLL ILLLGLVIVF GPTMFLEWSL FDDLATWKGC 350
LSNFSSYLTK TADFIEQSVF YWEQVTDGFF IFNERFKNFT LVVLNNVAEF 400
VCKYKLL 407
Length:407
Mass (Da):46,988
Last modified:July 19, 2005 - v2
Checksum:i94B624345124AEBF
GO
Isoform 2 (identifier: O60858-2) [UniParc]FASTAAdd to Basket

Also known as: Beta

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

Show »
Length:175
Mass (Da):19,841
Checksum:i006850E437E0D9B9
GO
Isoform 3 (identifier: O60858-3) [UniParc]FASTAAdd to Basket

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

Show »
Length:410
Mass (Da):47,333
Checksum:iE37CAD3F938C6C93
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti355 – 3551S → T.4 Publications
Corresponds to variant rs1056543 [ dbSNP | Ensembl ].
VAR_013512

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 11M → MDVM in isoform 3. VSP_038142
Alternative sequencei175 – 1751L → D in isoform 2. VSP_005746
Alternative sequencei176 – 407232Missing in isoform 2. VSP_005747Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS41888.1. [O60858-3]
CCDS9423.1. [O60858-1]
RefSeqiNP_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]
UniGeneiHs.436922.

Genome annotation databases

EnsembliENST00000298772; ENSP00000298772; ENSG00000204977. [O60858-3]
ENST00000356017; ENSP00000348299; ENSG00000204977. [O60858-3]
ENST00000378182; ENSP00000367424; ENSG00000204977. [O60858-1]
ENST00000420995; ENSP00000412943; ENSG00000204977. [O60858-1]
ENST00000457662; ENSP00000399206; ENSG00000204977. [O60858-1]
GeneIDi10206.
KEGGihsa:10206.
UCSCiuc001vdp.1. human. [O60858-3]
uc001vdq.1. human. [O60858-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS41888.1. [O60858-3 ]
CCDS9423.1. [O60858-1 ]
RefSeqi NP_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 ]
UniGenei Hs.436922.

3D structure databases

ProteinModelPortali O60858.
SMRi O60858. Positions 4-57.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115501. 14 interactions.
STRINGi 9606.ENSP00000298772.

PTM databases

PhosphoSitei O60858.

Proteomic databases

MaxQBi O60858.
PaxDbi O60858.
PRIDEi O60858.

Protocols and materials databases

DNASUi 10206.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000298772 ; ENSP00000298772 ; ENSG00000204977 . [O60858-3 ]
ENST00000356017 ; ENSP00000348299 ; ENSG00000204977 . [O60858-3 ]
ENST00000378182 ; ENSP00000367424 ; ENSG00000204977 . [O60858-1 ]
ENST00000420995 ; ENSP00000412943 ; ENSG00000204977 . [O60858-1 ]
ENST00000457662 ; ENSP00000399206 ; ENSG00000204977 . [O60858-1 ]
GeneIDi 10206.
KEGGi hsa:10206.
UCSCi uc001vdp.1. human. [O60858-3 ]
uc001vdq.1. human. [O60858-1 ]

Organism-specific databases

CTDi 10206.
GeneCardsi GC13P050570.
HGNCi HGNC:9976. TRIM13.
HPAi HPA000367.
MIMi 605661. gene.
neXtProti NX_O60858.
PharmGKBi PA162406947.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG238872.
HOVERGENi HBG056536.
InParanoidi O60858.
KOi K12003.
OMAi ICCSLFD.
OrthoDBi EOG7KWSHJ.
PhylomeDBi O60858.
TreeFami TF331669.

Enzyme and pathway databases

UniPathwayi UPA00143 .

Miscellaneous databases

GenomeRNAii 10206.
NextBioi 38634.
PROi O60858.
SOURCEi Search...

Gene expression databases

Bgeei O60858.
CleanExi HS_TRIM13.
Genevestigatori O60858.

Family and domain databases

Gene3Di 3.30.40.10. 1 hit.
4.10.45.10. 1 hit.
InterProi IPR000315. Znf_B-box.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view ]
Pfami PF00643. zf-B_box. 1 hit.
PF13639. zf-RING_2. 1 hit.
[Graphical view ]
SMARTi SM00336. BBOX. 1 hit.
SM00184. RING. 1 hit.
[Graphical view ]
PROSITEi PS50119. ZF_BBOX. 1 hit.
PS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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. 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.

Entry informationi

Entry nameiTRI13_HUMAN
AccessioniPrimary (citable) accession number: O60858
Secondary accession number(s): B2RB49
, Q5UBW0, Q5W0U8, Q5W0U9, Q9BQ47, Q9C021
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: July 19, 2005
Last modified: September 3, 2014
This is version 138 of the entry and version 2 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

Miscellaneous

Located on chromosome 13 within the minimal deletion region for B-cell chronic lymphocytic leukemia.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 13
    Human chromosome 13: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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