Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

O60858

- TRI13_HUMAN

UniProt

O60858 - TRI13_HUMAN

Protein

E3 ubiquitin-protein ligase TRIM13

Gene

TRIM13

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 139 (01 Oct 2014)
      Sequence version 2 (19 Jul 2005)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri89 – 13143B box-typePROSITE-ProRule annotationAdd
    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

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

    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

    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.3 Publications

    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei317 – 33721HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili172 – 20029Sequence AnalysisAdd
    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.Curated
    Contains 1 B box-type zinc finger.PROSITE-ProRule annotation
    Contains 1 RING-type zinc finger.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri10 – 5849RING-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri89 – 13143B box-typePROSITE-ProRule annotationAdd
    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. 1 PublicationVSP_038142
    Alternative sequencei175 – 1751L → D in isoform 2. 1 PublicationVSP_005746
    Alternative sequencei176 – 407232Missing in isoform 2. 1 PublicationVSP_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

    EnsembliENST00000356017; 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 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

    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: October 1, 2014
    This is version 139 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