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Q9HCM9

- TRI39_HUMAN

UniProt

Q9HCM9 - TRI39_HUMAN

Protein

E3 ubiquitin-protein ligase TRIM39

Gene

TRIM39

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 136 (01 Oct 2014)
      Sequence version 2 (07 Dec 2004)
      Previous versions | rss
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    Functioni

    E3 ubiquitin-protein ligase. May facilitate apoptosis by inhibiting APC/C-Cdh1-mediated poly-ubiquitination and subsequent proteasome-mediated degradation of the pro-apoptotic protein MOAP1.2 Publications

    Pathwayi

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri29 – 7042RING-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri102 – 14342B box-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. identical protein binding Source: IntAct
    2. ligase activity Source: UniProtKB-KW
    3. protein binding Source: IntAct
    4. zinc ion binding Source: InterPro

    GO - Biological processi

    1. apoptotic process Source: UniProtKB-KW
    2. negative regulation of protein ubiquitination involved in ubiquitin-dependent protein catabolic process Source: BHF-UCL
    3. positive regulation of apoptotic signaling pathway Source: BHF-UCL
    4. protein ubiquitination Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    Apoptosis, Ubl conjugation pathway

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    UniPathwayiUPA00143.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    E3 ubiquitin-protein ligase TRIM39 (EC:6.3.2.-)
    Alternative name(s):
    RING finger protein 23
    Testis-abundant finger protein
    Tripartite motif-containing protein 39
    Gene namesi
    Name:TRIM39
    Synonyms:RNF23, TFP
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:10065. TRIM39.

    Subcellular locationi

    Cytoplasmcytosol 1 Publication. Mitochondrion 1 Publication
    Note: Found predominantly in the cytosol. Partial shift from the cytosol to the mitochondria when colocalized with MOAP1.

    GO - Cellular componenti

    1. cytosol Source: BHF-UCL
    2. mitochondrion Source: BHF-UCL

    Keywords - Cellular componenti

    Cytoplasm, Mitochondrion

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA35535.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 518518E3 ubiquitin-protein ligase TRIM39PRO_0000056257Add
    BLAST

    Post-translational modificationi

    Autoubiquitinated.1 Publication

    Keywords - PTMi

    Ubl conjugation

    Proteomic databases

    PaxDbiQ9HCM9.
    PRIDEiQ9HCM9.

    PTM databases

    PhosphoSiteiQ9HCM9.

    Expressioni

    Tissue specificityi

    Ubiquitous; highly expressed in brain, heart, kidney, liver, skeletal muscle, spleen and testis.1 Publication

    Gene expression databases

    ArrayExpressiQ9HCM9.
    BgeeiQ9HCM9.
    CleanExiHS_TRIM39.
    GenevestigatoriQ9HCM9.

    Organism-specific databases

    HPAiHPA051120.

    Interactioni

    Subunit structurei

    Interacts with MOAP1.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself5EBI-739510,EBI-739510
    NCK1P163332EBI-739510,EBI-389883
    TRIM17Q9Y5773EBI-739510,EBI-743894
    UBE2D1P516683EBI-739510,EBI-743540

    Protein-protein interaction databases

    BioGridi121170. 37 interactions.
    IntActiQ9HCM9. 31 interactions.
    MINTiMINT-1433641.
    STRINGi9606.ENSP00000398355.

    Structurei

    Secondary structure

    1
    518
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi30 – 323
    Helixi50 – 567
    Turni108 – 1103
    Beta strandi116 – 1216
    Beta strandi123 – 1253
    Helixi127 – 1304
    Turni134 – 1374
    Beta strandi140 – 1423

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2DIDNMR-A104-143[»]
    2DIFNMR-A104-143[»]
    2ECJNMR-A19-69[»]
    ProteinModelPortaliQ9HCM9.
    SMRiQ9HCM9. Positions 13-69, 106-143, 338-513.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9HCM9.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini319 – 514196B30.2/SPRYPROSITE-ProRule annotationAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili181 – 25070Sequence AnalysisAdd
    BLAST

    Sequence similaritiesi

    Belongs to the TRIM/RBCC family.Curated
    Contains 1 B box-type zinc finger.PROSITE-ProRule annotation
    Contains 1 B30.2/SPRY domain.PROSITE-ProRule annotation
    Contains 1 RING-type zinc finger.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri29 – 7042RING-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri102 – 14342B box-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Coiled coil, Zinc-finger

    Phylogenomic databases

    eggNOGiNOG238084.
    HOGENOMiHOG000234133.
    HOVERGENiHBG001357.
    InParanoidiQ9HCM9.
    KOiK12015.
    OMAiVECRRQQ.
    PhylomeDBiQ9HCM9.
    TreeFamiTF342569.

    Family and domain databases

    Gene3Di3.30.40.10. 1 hit.
    4.10.45.10. 1 hit.
    InterProiIPR001870. 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.
    IPR001841. Znf_RING.
    IPR013083. Znf_RING/FYVE/PHD.
    IPR017907. Znf_RING_CS.
    [Graphical view]
    PfamiPF13765. PRY. 1 hit.
    PF00622. SPRY. 1 hit.
    PF00643. zf-B_box. 1 hit.
    [Graphical view]
    PRINTSiPR01407. BUTYPHLNCDUF.
    SMARTiSM00336. BBOX. 1 hit.
    SM00589. PRY. 1 hit.
    SM00184. RING. 1 hit.
    SM00449. SPRY. 1 hit.
    [Graphical view]
    SUPFAMiSSF49899. SSF49899. 1 hit.
    PROSITEiPS50188. B302_SPRY. 1 hit.
    PS50119. ZF_BBOX. 1 hit.
    PS00518. ZF_RING_1. 1 hit.
    PS50089. ZF_RING_2. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9HCM9-1) [UniParc]FASTAAdd to Basket

    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

    MAETSLLEAG ASAASTAAAL ENLQVEASCS VCLEYLKEPV IIECGHNFCK    50
    ACITRWWEDL ERDFPCPVCR KTSRYRSLRP NRQLGSMVEI AKQLQAVKRK 100
    IRDESLCPQH HEALSLFCYE DQEAVCLICA ISHTHRAHTV VPLDDATQEY 150
    KEKLQKCLEP LEQKLQEITR CKSSEEKKPG ELKRLVESRR QQILREFEEL 200
    HRRLDEEQQV LLSRLEEEEQ DILQRLRENA AHLGDKRRDL AHLAAEVEGK 250
    CLQSGFEMLK DVKSTLEKNI PRKFGGSLST ICPRDHKALL GLVKEINRCE 300
    KVKTMEVTSV SIELEKNFSN FPRQYFALRK ILKQLIADVT LDPETAHPNL 350
    VLSEDRKSVK FVETRLRDLP DTPRRFTFYP CVLATEGFTS GRHYWEVEVG 400
    DKTHWAVGVC RDSVSRKGEL TPLPETGYWR VRLWNGDKYA ATTTPFTPLH 450
    IKVKPKRVGI FLDYEAGTLS FYNVTDRSHI YTFTDTFTEK LWPLFYPGIR 500
    AGRKNAAPLT IRPPTDWE 518
    Length:518
    Mass (Da):59,690
    Last modified:December 7, 2004 - v2
    Checksum:i2F946F518B217153
    GO
    Isoform 2 (identifier: Q9HCM9-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         269-298: Missing.

    Show »
    Length:488
    Mass (Da):56,374
    Checksum:i102AA8E5C8786A3E
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti137 – 1371A → P in BAB16374. (PubMed:11006080)Curated
    Sequence conflicti419 – 4191E → K in BAD13703. 1 PublicationCurated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei269 – 29830Missing in isoform 2. 2 PublicationsVSP_005755Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB046381 mRNA. Translation: BAB16374.1.
    BT007370 mRNA. Translation: AAP36034.1.
    AB110937 Genomic DNA. Translation: BAD13703.1.
    AK292512 mRNA. Translation: BAF85201.1.
    AB110938 Genomic DNA. Translation: BAD13704.1.
    AB202089 Genomic DNA. Translation: BAE78608.1.
    AL662832 Genomic DNA. Translation: CAI17501.1.
    AL662795 Genomic DNA. Translation: CAI18251.1.
    AL773535 Genomic DNA. Translation: CAI41818.1.
    AL773535 Genomic DNA. Translation: CAI41819.1.
    BX248580 Genomic DNA. Translation: CAM25899.1.
    BX248580 Genomic DNA. Translation: CAM25900.1.
    CR759928 Genomic DNA. Translation: CAQ08313.1.
    CR759928 Genomic DNA. Translation: CAQ08314.1.
    BX927214 Genomic DNA. Translation: CAQ08383.1.
    BX927214 Genomic DNA. Translation: CAQ08384.1.
    CR759281 Genomic DNA. Translation: CAQ09020.1.
    CR759281 Genomic DNA. Translation: CAQ09021.1.
    CH471081 Genomic DNA. Translation: EAX03283.1.
    CH471081 Genomic DNA. Translation: EAX03284.1.
    BC007661 mRNA. Translation: AAH07661.1.
    BC034985 mRNA. Translation: AAH34985.1.
    CCDSiCCDS34377.1. [Q9HCM9-1]
    CCDS34378.1. [Q9HCM9-2]
    PIRiJC7387.
    RefSeqiNP_067076.2. NM_021253.3. [Q9HCM9-1]
    NP_742013.1. NM_172016.2. [Q9HCM9-2]
    UniGeneiHs.413493.

    Genome annotation databases

    EnsembliENST00000376656; ENSP00000365844; ENSG00000204599. [Q9HCM9-1]
    ENST00000376659; ENSP00000365847; ENSG00000204599. [Q9HCM9-2]
    ENST00000383601; ENSP00000373095; ENSG00000206495. [Q9HCM9-2]
    ENST00000383602; ENSP00000373096; ENSG00000206495. [Q9HCM9-1]
    ENST00000383603; ENSP00000373097; ENSG00000206495. [Q9HCM9-2]
    ENST00000396547; ENSP00000379796; ENSG00000204599. [Q9HCM9-1]
    ENST00000396548; ENSP00000379797; ENSG00000204599. [Q9HCM9-2]
    ENST00000396551; ENSP00000379800; ENSG00000204599. [Q9HCM9-2]
    ENST00000400644; ENSP00000383486; ENSG00000206495. [Q9HCM9-2]
    ENST00000413715; ENSP00000411949; ENSG00000224994. [Q9HCM9-1]
    ENST00000414015; ENSP00000401071; ENSG00000224994. [Q9HCM9-2]
    ENST00000419790; ENSP00000401184; ENSG00000229929. [Q9HCM9-2]
    ENST00000424575; ENSP00000409902; ENSG00000230308. [Q9HCM9-1]
    ENST00000426469; ENSP00000397043; ENSG00000229929. [Q9HCM9-1]
    ENST00000430502; ENSP00000398956; ENSG00000232839. [Q9HCM9-2]
    ENST00000431272; ENSP00000396986; ENSG00000230308. [Q9HCM9-2]
    ENST00000433900; ENSP00000389852; ENSG00000232839. [Q9HCM9-2]
    ENST00000438076; ENSP00000389198; ENSG00000232839. [Q9HCM9-2]
    ENST00000438859; ENSP00000411582; ENSG00000226437. [Q9HCM9-2]
    ENST00000440117; ENSP00000392130; ENSG00000224994. [Q9HCM9-2]
    ENST00000443109; ENSP00000414525; ENSG00000229929. [Q9HCM9-2]
    ENST00000445206; ENSP00000391917; ENSG00000226437. [Q9HCM9-1]
    ENST00000446397; ENSP00000412743; ENSG00000230308. [Q9HCM9-2]
    ENST00000449318; ENSP00000404904; ENSG00000224994. [Q9HCM9-2]
    ENST00000450778; ENSP00000387445; ENSG00000226437. [Q9HCM9-2]
    ENST00000451132; ENSP00000394353; ENSG00000226437. [Q9HCM9-2]
    ENST00000451715; ENSP00000398355; ENSG00000232839. [Q9HCM9-1]
    ENST00000452705; ENSP00000415259; ENSG00000229929. [Q9HCM9-2]
    ENST00000458607; ENSP00000404340; ENSG00000230308. [Q9HCM9-2]
    ENST00000547030; ENSP00000449847; ENSG00000224994. [Q9HCM9-1]
    ENST00000548002; ENSP00000447835; ENSG00000232839. [Q9HCM9-1]
    ENST00000549841; ENSP00000448572; ENSG00000230308. [Q9HCM9-1]
    ENST00000550282; ENSP00000449272; ENSG00000206495. [Q9HCM9-1]
    ENST00000552337; ENSP00000450288; ENSG00000226437. [Q9HCM9-1]
    ENST00000552520; ENSP00000448462; ENSG00000229929. [Q9HCM9-1]
    GeneIDi56658.
    KEGGihsa:56658.
    UCSCiuc003npz.3. human. [Q9HCM9-2]
    uc010jrz.3. human. [Q9HCM9-1]

    Polymorphism databases

    DMDMi56405385.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB046381 mRNA. Translation: BAB16374.1 .
    BT007370 mRNA. Translation: AAP36034.1 .
    AB110937 Genomic DNA. Translation: BAD13703.1 .
    AK292512 mRNA. Translation: BAF85201.1 .
    AB110938 Genomic DNA. Translation: BAD13704.1 .
    AB202089 Genomic DNA. Translation: BAE78608.1 .
    AL662832 Genomic DNA. Translation: CAI17501.1 .
    AL662795 Genomic DNA. Translation: CAI18251.1 .
    AL773535 Genomic DNA. Translation: CAI41818.1 .
    AL773535 Genomic DNA. Translation: CAI41819.1 .
    BX248580 Genomic DNA. Translation: CAM25899.1 .
    BX248580 Genomic DNA. Translation: CAM25900.1 .
    CR759928 Genomic DNA. Translation: CAQ08313.1 .
    CR759928 Genomic DNA. Translation: CAQ08314.1 .
    BX927214 Genomic DNA. Translation: CAQ08383.1 .
    BX927214 Genomic DNA. Translation: CAQ08384.1 .
    CR759281 Genomic DNA. Translation: CAQ09020.1 .
    CR759281 Genomic DNA. Translation: CAQ09021.1 .
    CH471081 Genomic DNA. Translation: EAX03283.1 .
    CH471081 Genomic DNA. Translation: EAX03284.1 .
    BC007661 mRNA. Translation: AAH07661.1 .
    BC034985 mRNA. Translation: AAH34985.1 .
    CCDSi CCDS34377.1. [Q9HCM9-1 ]
    CCDS34378.1. [Q9HCM9-2 ]
    PIRi JC7387.
    RefSeqi NP_067076.2. NM_021253.3. [Q9HCM9-1 ]
    NP_742013.1. NM_172016.2. [Q9HCM9-2 ]
    UniGenei Hs.413493.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2DID NMR - A 104-143 [» ]
    2DIF NMR - A 104-143 [» ]
    2ECJ NMR - A 19-69 [» ]
    ProteinModelPortali Q9HCM9.
    SMRi Q9HCM9. Positions 13-69, 106-143, 338-513.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 121170. 37 interactions.
    IntActi Q9HCM9. 31 interactions.
    MINTi MINT-1433641.
    STRINGi 9606.ENSP00000398355.

    PTM databases

    PhosphoSitei Q9HCM9.

    Polymorphism databases

    DMDMi 56405385.

    Proteomic databases

    PaxDbi Q9HCM9.
    PRIDEi Q9HCM9.

    Protocols and materials databases

    DNASUi 56658.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000376656 ; ENSP00000365844 ; ENSG00000204599 . [Q9HCM9-1 ]
    ENST00000376659 ; ENSP00000365847 ; ENSG00000204599 . [Q9HCM9-2 ]
    ENST00000383601 ; ENSP00000373095 ; ENSG00000206495 . [Q9HCM9-2 ]
    ENST00000383602 ; ENSP00000373096 ; ENSG00000206495 . [Q9HCM9-1 ]
    ENST00000383603 ; ENSP00000373097 ; ENSG00000206495 . [Q9HCM9-2 ]
    ENST00000396547 ; ENSP00000379796 ; ENSG00000204599 . [Q9HCM9-1 ]
    ENST00000396548 ; ENSP00000379797 ; ENSG00000204599 . [Q9HCM9-2 ]
    ENST00000396551 ; ENSP00000379800 ; ENSG00000204599 . [Q9HCM9-2 ]
    ENST00000400644 ; ENSP00000383486 ; ENSG00000206495 . [Q9HCM9-2 ]
    ENST00000413715 ; ENSP00000411949 ; ENSG00000224994 . [Q9HCM9-1 ]
    ENST00000414015 ; ENSP00000401071 ; ENSG00000224994 . [Q9HCM9-2 ]
    ENST00000419790 ; ENSP00000401184 ; ENSG00000229929 . [Q9HCM9-2 ]
    ENST00000424575 ; ENSP00000409902 ; ENSG00000230308 . [Q9HCM9-1 ]
    ENST00000426469 ; ENSP00000397043 ; ENSG00000229929 . [Q9HCM9-1 ]
    ENST00000430502 ; ENSP00000398956 ; ENSG00000232839 . [Q9HCM9-2 ]
    ENST00000431272 ; ENSP00000396986 ; ENSG00000230308 . [Q9HCM9-2 ]
    ENST00000433900 ; ENSP00000389852 ; ENSG00000232839 . [Q9HCM9-2 ]
    ENST00000438076 ; ENSP00000389198 ; ENSG00000232839 . [Q9HCM9-2 ]
    ENST00000438859 ; ENSP00000411582 ; ENSG00000226437 . [Q9HCM9-2 ]
    ENST00000440117 ; ENSP00000392130 ; ENSG00000224994 . [Q9HCM9-2 ]
    ENST00000443109 ; ENSP00000414525 ; ENSG00000229929 . [Q9HCM9-2 ]
    ENST00000445206 ; ENSP00000391917 ; ENSG00000226437 . [Q9HCM9-1 ]
    ENST00000446397 ; ENSP00000412743 ; ENSG00000230308 . [Q9HCM9-2 ]
    ENST00000449318 ; ENSP00000404904 ; ENSG00000224994 . [Q9HCM9-2 ]
    ENST00000450778 ; ENSP00000387445 ; ENSG00000226437 . [Q9HCM9-2 ]
    ENST00000451132 ; ENSP00000394353 ; ENSG00000226437 . [Q9HCM9-2 ]
    ENST00000451715 ; ENSP00000398355 ; ENSG00000232839 . [Q9HCM9-1 ]
    ENST00000452705 ; ENSP00000415259 ; ENSG00000229929 . [Q9HCM9-2 ]
    ENST00000458607 ; ENSP00000404340 ; ENSG00000230308 . [Q9HCM9-2 ]
    ENST00000547030 ; ENSP00000449847 ; ENSG00000224994 . [Q9HCM9-1 ]
    ENST00000548002 ; ENSP00000447835 ; ENSG00000232839 . [Q9HCM9-1 ]
    ENST00000549841 ; ENSP00000448572 ; ENSG00000230308 . [Q9HCM9-1 ]
    ENST00000550282 ; ENSP00000449272 ; ENSG00000206495 . [Q9HCM9-1 ]
    ENST00000552337 ; ENSP00000450288 ; ENSG00000226437 . [Q9HCM9-1 ]
    ENST00000552520 ; ENSP00000448462 ; ENSG00000229929 . [Q9HCM9-1 ]
    GeneIDi 56658.
    KEGGi hsa:56658.
    UCSCi uc003npz.3. human. [Q9HCM9-2 ]
    uc010jrz.3. human. [Q9HCM9-1 ]

    Organism-specific databases

    CTDi 56658.
    GeneCardsi GC06P030294.
    GC06Pi30302.
    GC06Pj30284.
    GC06Pk30284.
    GC06Pl30338.
    GC06Pn30283.
    GC06Po30283.
    HGNCi HGNC:10065. TRIM39.
    HPAi HPA051120.
    MIMi 605700. gene.
    neXtProti NX_Q9HCM9.
    PharmGKBi PA35535.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG238084.
    HOGENOMi HOG000234133.
    HOVERGENi HBG001357.
    InParanoidi Q9HCM9.
    KOi K12015.
    OMAi VECRRQQ.
    PhylomeDBi Q9HCM9.
    TreeFami TF342569.

    Enzyme and pathway databases

    UniPathwayi UPA00143 .

    Miscellaneous databases

    EvolutionaryTracei Q9HCM9.
    GenomeRNAii 56658.
    NextBioi 62129.
    PROi Q9HCM9.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9HCM9.
    Bgeei Q9HCM9.
    CleanExi HS_TRIM39.
    Genevestigatori Q9HCM9.

    Family and domain databases

    Gene3Di 3.30.40.10. 1 hit.
    4.10.45.10. 1 hit.
    InterProi 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.
    IPR001841. Znf_RING.
    IPR013083. Znf_RING/FYVE/PHD.
    IPR017907. Znf_RING_CS.
    [Graphical view ]
    Pfami PF13765. PRY. 1 hit.
    PF00622. SPRY. 1 hit.
    PF00643. zf-B_box. 1 hit.
    [Graphical view ]
    PRINTSi PR01407. BUTYPHLNCDUF.
    SMARTi SM00336. BBOX. 1 hit.
    SM00589. PRY. 1 hit.
    SM00184. RING. 1 hit.
    SM00449. SPRY. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49899. SSF49899. 1 hit.
    PROSITEi PS50188. B302_SPRY. 1 hit.
    PS50119. ZF_BBOX. 1 hit.
    PS00518. ZF_RING_1. 1 hit.
    PS50089. ZF_RING_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning of testis-abundant finger protein/ring finger protein 23 (RNF23), a novel RING-B box-coiled coil-B30.2 protein on the class I region of the human MHC."
      Orimo A., Yamagishi T., Tominaga N., Yamauchi Y., Hishinuma T., Okada K., Suzuki M., Sato M., Nogi Y., Suzuki H., Inoue S., Yoshimura K., Shimizu Y., Muramatsu M.
      Biochem. Biophys. Res. Commun. 276:45-51(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Testis.
    2. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    3. "Genome diversity in HLA: a new strategy for detection of genetic polymorphisms in expressed genes within the HLA class III and class I regions."
      Shiina T., Ota M., Katsuyama Y., Hashimoto N., Siamak B., Inoko H.
      Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "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: Testis.
    5. "Rapid evolution of major histocompatibility complex class I genes in primates generates new disease alleles in humans via hitchhiking diversity."
      Shiina T., Ota M., Shimizu S., Katsuyama Y., Hashimoto N., Takasu M., Anzai T., Kulski J.K., Kikkawa E., Naruse T., Kimura N., Yanagiya K., Watanabe A., Hosomichi K., Kohara S., Iwamoto C., Umehara Y., Meyer A.
      , Wanner V., Sano K., Macquin C., Ikeo K., Tokunaga K., Gojobori T., Inoko H., Bahram S.
      Genetics 173:1555-1570(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Tissue: Peripheral blood leukocyte.
    6. "The DNA sequence and analysis of human chromosome 6."
      Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
      Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "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 2).
      Tissue: Colon and Testis.
    9. "TRIM39 is a MOAP-1-binding protein that stabilizes MOAP-1 through inhibition of its poly-ubiquitination process."
      Lee S.S., Fu N.Y., Sukumaran S.K., Wan K.F., Wan Q., Yu V.C.
      Exp. Cell Res. 315:1313-1325(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, INTERACTION WITH MOAP1.
    10. "The Trim39 ubiquitin ligase inhibits APC/CCdh1-mediated degradation of the Bax activator MOAP-1."
      Huang N.J., Zhang L., Tang W., Chen C., Yang C.S., Kornbluth S.
      J. Cell Biol. 197:361-367(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, AUTOUBIQUITINATION.
    11. "One sequence two fold ? correct fold of the ZF-B-box domain from human tripartite motif protein 39."
      RIKEN structural genomics initiative (RSGI)
      Submitted (SEP-2006) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 104-143.

    Entry informationi

    Entry nameiTRI39_HUMAN
    AccessioniPrimary (citable) accession number: Q9HCM9
    Secondary accession number(s): Q5STG3
    , Q5STG4, Q76BL3, Q8IYT9, Q96IB6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 26, 2001
    Last sequence update: December 7, 2004
    Last modified: October 1, 2014
    This is version 136 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

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 6
      Human chromosome 6: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    4. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

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