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Q9C026

- TRIM9_HUMAN

UniProt

Q9C026 - TRIM9_HUMAN

Protein

E3 ubiquitin-protein ligase TRIM9

Gene

TRIM9

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 138 (01 Oct 2014)
      Sequence version 1 (01 Jun 2001)
      Previous versions | rss
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    Functioni

    E3 ubiquitin-protein ligase which ubiquitinates itself in cooperation with an E2 enzyme UBE2D2/UBC4 and serves as a targeting signal for proteasomal degradation. May play a role in regulation of neuronal functions and may also participate in the formation or breakdown of abnormal inclusions in neurodegenerative disorders. May act as a regulator of synaptic vesicle exocytosis by controlling the availability of SNAP25 for the SNARE complex formation.1 Publication

    Pathwayi

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri10 – 5041RING-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri163 – 21250B box-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri224 – 26643B box-type 2PROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

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

    GO - Biological processi

    1. negative regulation of calcium ion-dependent exocytosis Source: Ensembl
    2. negative regulation of SNARE complex assembly Source: Ensembl
    3. proteasome-mediated ubiquitin-dependent protein catabolic process Source: UniProtKB
    4. synaptic vesicle exocytosis Source: Ensembl

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    Ubl conjugation pathway

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
    UniPathwayiUPA00143.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    E3 ubiquitin-protein ligase TRIM9 (EC:6.3.2.-)
    Alternative name(s):
    RING finger protein 91
    Tripartite motif-containing protein 9
    Gene namesi
    Name:TRIM9
    Synonyms:KIAA0282, RNF91
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 14

    Organism-specific databases

    HGNCiHGNC:16288. TRIM9.

    Subcellular locationi

    Cytoplasm 1 Publication. Cell projectiondendrite 1 Publication. Cytoplasmic vesiclesecretory vesiclesynaptic vesicle By similarity. Cell junctionsynapse By similarity. Cytoplasmcytoskeleton By similarity
    Note: Enriched at synaptic terminals where it exists in a soluble form and a synaptic vesicle-associated form. Associated with the cytoskeleton By similarity. Found in proximal dendrites of pyramidal neurons in the cerebral cortex and hippocampus, and Purkinje cells in the cerebellum.By similarity

    GO - Cellular componenti

    1. cell junction Source: UniProtKB-KW
    2. cytoplasm Source: UniProtKB
    3. cytoskeleton Source: UniProtKB-SubCell
    4. dendrite Source: UniProtKB
    5. synaptic vesicle Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell junction, Cell projection, Cytoplasm, Cytoplasmic vesicle, Cytoskeleton, Synapse

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA38116.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 710710E3 ubiquitin-protein ligase TRIM9PRO_0000056208Add
    BLAST

    Post-translational modificationi

    Auto-ubiquitinated. Poly-ubiquitinated in cultured cells, whereas it is monoubiquitinated in vitro.1 Publication

    Keywords - PTMi

    Ubl conjugation

    Proteomic databases

    MaxQBiQ9C026.
    PaxDbiQ9C026.
    PRIDEiQ9C026.

    2D gel databases

    REPRODUCTION-2DPAGEQ9C026.

    PTM databases

    PhosphoSiteiQ9C026.

    Expressioni

    Tissue specificityi

    Brain. Highly expressed in the cerebral cortex (at protein level). Severely decreased in the affected brain areas in Parkinson disease and dementia with Lewy bodies.1 Publication

    Gene expression databases

    BgeeiQ9C026.
    CleanExiHS_TRIM9.
    GenevestigatoriQ9C026.

    Interactioni

    Subunit structurei

    Interacts with SNAP25.By similarity

    Protein-protein interaction databases

    BioGridi125280. 24 interactions.
    IntActiQ9C026. 15 interactions.
    MINTiMINT-1478450.
    STRINGi9606.ENSP00000298355.

    Structurei

    Secondary structure

    1
    710
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi454 – 4607
    Beta strandi473 – 4797
    Beta strandi482 – 4854
    Beta strandi488 – 4947
    Beta strandi498 – 5014
    Beta strandi505 – 5073
    Beta strandi510 – 5167

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2DB8NMR-A439-534[»]
    ProteinModelPortaliQ9C026.
    SMRiQ9C026. Positions 2-38, 163-266, 436-534.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9C026.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini374 – 43259COSPROSITE-ProRule annotationAdd
    BLAST
    Domaini440 – 53596Fibronectin type-IIIPROSITE-ProRule annotationAdd
    BLAST
    Domaini533 – 702170B30.2/SPRYPROSITE-ProRule annotationAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili273 – 34068Sequence AnalysisAdd
    BLAST

    Domaini

    The coiled coil domain mediates the interaction with the N-terminal t-SNARE domain of SNAP25.By similarity

    Sequence similaritiesi

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

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri10 – 5041RING-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri163 – 21250B box-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri224 – 26643B box-type 2PROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Coiled coil, Repeat, Zinc-finger

    Phylogenomic databases

    eggNOGiNOG260378.
    HOVERGENiHBG062305.
    KOiK10649.
    OMAiPCSHNIC.
    OrthoDBiEOG7SJD63.
    PhylomeDBiQ9C026.
    TreeFamiTF315216.

    Family and domain databases

    Gene3Di2.60.40.10. 1 hit.
    3.30.40.10. 2 hits.
    4.10.45.10. 1 hit.
    InterProiIPR001870. B30.2/SPRY.
    IPR003649. Bbox_C.
    IPR008985. ConA-like_lec_gl_sf.
    IPR017903. COS_domain.
    IPR003961. Fibronectin_type3.
    IPR013783. Ig-like_fold.
    IPR003877. SPRY_rcpt.
    IPR000315. Znf_B-box.
    IPR018957. Znf_C3HC4_RING-type.
    IPR001841. Znf_RING.
    IPR013083. Znf_RING/FYVE/PHD.
    IPR017907. Znf_RING_CS.
    [Graphical view]
    PfamiPF00041. fn3. 1 hit.
    PF00622. SPRY. 1 hit.
    PF00643. zf-B_box. 1 hit.
    PF00097. zf-C3HC4. 1 hit.
    [Graphical view]
    SMARTiSM00502. BBC. 1 hit.
    SM00336. BBOX. 2 hits.
    SM00060. FN3. 1 hit.
    SM00184. RING. 1 hit.
    [Graphical view]
    SUPFAMiSSF49265. SSF49265. 1 hit.
    SSF49899. SSF49899. 1 hit.
    PROSITEiPS50188. B302_SPRY. 1 hit.
    PS51262. COS. 1 hit.
    PS50853. FN3. 1 hit.
    PS50119. ZF_BBOX. 2 hits.
    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: Q9C026-1) [UniParc]FASTAAdd to Basket

    Also known as: Beta

    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

    MEEMEEELKC PVCGSFYREP IILPCSHNLC QACARNILVQ TPESESPQSH    50
    RAAGSGVSDY DYLDLDKMSL YSEADSGYGS YGGFASAPTT PCQKSPNGVR 100
    VFPPAMPPPA THLSPALAPV PRNSCITCPQ CHRSLILDDR GLRGFPKNRV 150
    LEGVIDRYQQ SKAAALKCQL CEKAPKEATV MCEQCDVFYC DPCRLRCHPP 200
    RGPLAKHRLV PPAQGRVSRR LSPRKVSTCT DHELENHSMY CVQCKMPVCY 250
    QCLEEGKHSS HEVKALGAMW KLHKSQLSQA LNGLSDRAKE AKEFLVQLRN 300
    MVQQIQENSV EFEACLVAQC DALIDALNRR KAQLLARVNK EHEHKLKVVR 350
    DQISHCTVKL RQTTGLMEYC LEVIKENDPS GFLQISDALI RRVHLTEDQW 400
    GKGTLTPRMT TDFDLSLDNS PLLQSIHQLD FVQVKASSPV PATPILQLEE 450
    CCTHNNSATL SWKQPPLSTV PADGYILELD DGNGGQFREV YVGKETMCTV 500
    DGLHFNSTYN ARVKAFNKTG VSPYSKTLVL QTSEVAWFAF DPGSAHSDII 550
    LSNDNLTVTC SSYDDRVVLG KTGFSKGIHY WELTVDRYDN HPDPAFGVAR 600
    MDVMKDVMLG KDDKAWAMYV DNNRSWFMHN NSHTNRTEGG ITKGATIGVL 650
    LDLNRKNLTF FINDEQQGPI AFDNVEGLFF PAVSLNRNVQ VTLHTGLPVP 700
    DFYSSRASIA 710
    Length:710
    Mass (Da):79,177
    Last modified:June 1, 2001 - v1
    Checksum:iAEAB24807C89D0E2
    GO
    Isoform 4 (identifier: Q9C026-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         436-439: Missing.
         534-534: E → EDTDSEEQTL...QLVDIKKLLA
         692-710: TLHTGLPVPDFYSSRASIA → STLPLRLNSCCWLPVQRLPRAVQSNRREGS

    Note: May be due to a competing donor splice site, to exon inclusion and to intron retention.

    Show »
    Length:802
    Mass (Da):89,762
    Checksum:i38ABF6696A12C84C
    GO
    Isoform 5 (identifier: Q9C026-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         535-550: VAWFAFDPGSAHSDII → GKALQQYPSERELRGI
         551-710: Missing.

    Note: May be due to intron retention.

    Show »
    Length:550
    Mass (Da):61,346
    Checksum:i47ACD9147C1BE651
    GO

    Sequence cautioni

    The sequence AAG53490.1 differs from that shown. Reason: Frameshift at position 660.
    The sequence AAG53492.1 differs from that shown. Reason: Frameshift at position 655.
    The sequence BAA13398.2 differs from that shown. Reason: Frameshift at position 660.
    The sequence BAA13398.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti314 – 3141A → V in BAB70913. (PubMed:9179496)Curated
    Sequence conflicti384 – 3841Q → R in BAB70913. (PubMed:9179496)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti653 – 6531L → F.3 Publications
    Corresponds to variant rs2275462 [ dbSNP | Ensembl ].
    VAR_016202

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei436 – 4394Missing in isoform 4. 1 PublicationVSP_007922
    Alternative sequencei534 – 5341E → EDTDSEEQTLPFPVPSERLP LRRMSPFSSTLNLQPSFPGR SYFDFRSSPHQLSLHSSLQS LNAPGCNFETQSAPYSQLVD IKKLLA in isoform 4. 1 PublicationVSP_007923
    Alternative sequencei535 – 55016VAWFA…HSDII → GKALQQYPSERELRGI in isoform 5. 1 PublicationVSP_007925Add
    BLAST
    Alternative sequencei551 – 710160Missing in isoform 5. 1 PublicationVSP_007926Add
    BLAST
    Alternative sequencei692 – 71019TLHTG…RASIA → STLPLRLNSCCWLPVQRLPR AVQSNRREGS in isoform 4. 1 PublicationVSP_007924Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF220036 mRNA. Translation: AAG53490.1. Frameshift.
    AF220037 mRNA. Translation: AAG53491.1.
    AF220038 mRNA. Translation: AAG53492.1. Frameshift.
    D87458 mRNA. Translation: BAA13398.2. Sequence problems.
    AK055388 mRNA. Translation: BAB70913.1.
    CH471078 Genomic DNA. Translation: EAW65680.1.
    CH471078 Genomic DNA. Translation: EAW65681.1.
    CH471078 Genomic DNA. Translation: EAW65682.1.
    CH471078 Genomic DNA. Translation: EAW65684.1.
    BC013414 mRNA. Translation: AAH13414.1.
    BC063872 mRNA. Translation: AAH63872.1.
    CCDSiCCDS45105.1. [Q9C026-5]
    CCDS9703.1. [Q9C026-1]
    RefSeqiNP_055978.4. NM_015163.5. [Q9C026-1]
    NP_443210.1. NM_052978.4. [Q9C026-5]
    UniGeneiHs.654750.

    Genome annotation databases

    EnsembliENST00000298355; ENSP00000298355; ENSG00000100505. [Q9C026-1]
    ENST00000338969; ENSP00000342970; ENSG00000100505. [Q9C026-4]
    ENST00000360392; ENSP00000353561; ENSG00000100505. [Q9C026-5]
    GeneIDi114088.
    KEGGihsa:114088.
    UCSCiuc001wyx.4. human. [Q9C026-1]
    uc001wyy.2. human. [Q9C026-4]
    uc001wyz.4. human. [Q9C026-5]

    Polymorphism databases

    DMDMi33516964.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF220036 mRNA. Translation: AAG53490.1 . Frameshift.
    AF220037 mRNA. Translation: AAG53491.1 .
    AF220038 mRNA. Translation: AAG53492.1 . Frameshift.
    D87458 mRNA. Translation: BAA13398.2 . Sequence problems.
    AK055388 mRNA. Translation: BAB70913.1 .
    CH471078 Genomic DNA. Translation: EAW65680.1 .
    CH471078 Genomic DNA. Translation: EAW65681.1 .
    CH471078 Genomic DNA. Translation: EAW65682.1 .
    CH471078 Genomic DNA. Translation: EAW65684.1 .
    BC013414 mRNA. Translation: AAH13414.1 .
    BC063872 mRNA. Translation: AAH63872.1 .
    CCDSi CCDS45105.1. [Q9C026-5 ]
    CCDS9703.1. [Q9C026-1 ]
    RefSeqi NP_055978.4. NM_015163.5. [Q9C026-1 ]
    NP_443210.1. NM_052978.4. [Q9C026-5 ]
    UniGenei Hs.654750.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2DB8 NMR - A 439-534 [» ]
    ProteinModelPortali Q9C026.
    SMRi Q9C026. Positions 2-38, 163-266, 436-534.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 125280. 24 interactions.
    IntActi Q9C026. 15 interactions.
    MINTi MINT-1478450.
    STRINGi 9606.ENSP00000298355.

    PTM databases

    PhosphoSitei Q9C026.

    Polymorphism databases

    DMDMi 33516964.

    2D gel databases

    REPRODUCTION-2DPAGE Q9C026.

    Proteomic databases

    MaxQBi Q9C026.
    PaxDbi Q9C026.
    PRIDEi Q9C026.

    Protocols and materials databases

    DNASUi 114088.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000298355 ; ENSP00000298355 ; ENSG00000100505 . [Q9C026-1 ]
    ENST00000338969 ; ENSP00000342970 ; ENSG00000100505 . [Q9C026-4 ]
    ENST00000360392 ; ENSP00000353561 ; ENSG00000100505 . [Q9C026-5 ]
    GeneIDi 114088.
    KEGGi hsa:114088.
    UCSCi uc001wyx.4. human. [Q9C026-1 ]
    uc001wyy.2. human. [Q9C026-4 ]
    uc001wyz.4. human. [Q9C026-5 ]

    Organism-specific databases

    CTDi 114088.
    GeneCardsi GC14M051441.
    HGNCi HGNC:16288. TRIM9.
    MIMi 606555. gene.
    neXtProti NX_Q9C026.
    PharmGKBi PA38116.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG260378.
    HOVERGENi HBG062305.
    KOi K10649.
    OMAi PCSHNIC.
    OrthoDBi EOG7SJD63.
    PhylomeDBi Q9C026.
    TreeFami TF315216.

    Enzyme and pathway databases

    UniPathwayi UPA00143 .
    Reactomei REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.

    Miscellaneous databases

    EvolutionaryTracei Q9C026.
    GeneWikii TRIM9.
    GenomeRNAii 114088.
    NextBioi 78980.
    PROi Q9C026.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9C026.
    CleanExi HS_TRIM9.
    Genevestigatori Q9C026.

    Family and domain databases

    Gene3Di 2.60.40.10. 1 hit.
    3.30.40.10. 2 hits.
    4.10.45.10. 1 hit.
    InterProi IPR001870. B30.2/SPRY.
    IPR003649. Bbox_C.
    IPR008985. ConA-like_lec_gl_sf.
    IPR017903. COS_domain.
    IPR003961. Fibronectin_type3.
    IPR013783. Ig-like_fold.
    IPR003877. SPRY_rcpt.
    IPR000315. Znf_B-box.
    IPR018957. Znf_C3HC4_RING-type.
    IPR001841. Znf_RING.
    IPR013083. Znf_RING/FYVE/PHD.
    IPR017907. Znf_RING_CS.
    [Graphical view ]
    Pfami PF00041. fn3. 1 hit.
    PF00622. SPRY. 1 hit.
    PF00643. zf-B_box. 1 hit.
    PF00097. zf-C3HC4. 1 hit.
    [Graphical view ]
    SMARTi SM00502. BBC. 1 hit.
    SM00336. BBOX. 2 hits.
    SM00060. FN3. 1 hit.
    SM00184. RING. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49265. SSF49265. 1 hit.
    SSF49899. SSF49899. 1 hit.
    PROSITEi PS50188. B302_SPRY. 1 hit.
    PS51262. COS. 1 hit.
    PS50853. FN3. 1 hit.
    PS50119. ZF_BBOX. 2 hits.
    PS00518. ZF_RING_1. 1 hit.
    PS50089. ZF_RING_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT PHE-653.
    2. "Construction and characterization of human brain cDNA libraries suitable for analysis of cDNA clones encoding relatively large proteins."
      Ohara O., Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Nomura N.
      DNA Res. 4:53-59(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT PHE-653.
      Tissue: Brain.
    3. "Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
      Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
      DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: SEQUENCE REVISION.
    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 4).
      Tissue: Fetal brain.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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] (ISOFORMS 1 AND 5), VARIANT PHE-653.
      Tissue: Brain and Uterus.
    7. "TRIM9, a novel brain-specific E3 ubiquitin ligase, is repressed in the brain of Parkinson's disease and dementia with Lewy bodies."
      Tanji K., Kamitani T., Mori F., Kakita A., Takahashi H., Wakabayashi K.
      Neurobiol. Dis. 38:210-218(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, AUTOUBIQUITINATION, TISSUE SPECIFICITY.
    8. "Solution structures of the FN3 domain of human tripartite motif protein 9."
      RIKEN structural genomics initiative (RSGI)
      Submitted (JUN-2006) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 437-534.

    Entry informationi

    Entry nameiTRIM9_HUMAN
    AccessioniPrimary (citable) accession number: Q9C026
    Secondary accession number(s): D3DSB7
    , D3DSB8, Q92557, Q96D24, Q96NI4, Q9C025, Q9C027
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 4, 2003
    Last sequence update: June 1, 2001
    Last modified: October 1, 2014
    This is version 138 of the entry and version 1 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 14
      Human chromosome 14: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3