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Q9C026

- TRIM9_HUMAN

UniProt

Q9C026 - TRIM9_HUMAN

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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

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
Complete GO annotation...

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-KW
  4. dendrite Source: UniProtKB
  5. synaptic vesicle Source: Ensembl
Complete GO annotation...

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. 25 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 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.
GeneTreeiENSGT00760000118878.
HOVERGENiHBG062305.
InParanoidiQ9C026.
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.
IPR013320. ConA-like_dom.
IPR017903. COS_domain.
IPR003961. Fibronectin_type3.
IPR013783. Ig-like_fold.
IPR003877. SPRY_dom.
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

        10         20         30         40         50
MEEMEEELKC PVCGSFYREP IILPCSHNLC QACARNILVQ TPESESPQSH
60 70 80 90 100
RAAGSGVSDY DYLDLDKMSL YSEADSGYGS YGGFASAPTT PCQKSPNGVR
110 120 130 140 150
VFPPAMPPPA THLSPALAPV PRNSCITCPQ CHRSLILDDR GLRGFPKNRV
160 170 180 190 200
LEGVIDRYQQ SKAAALKCQL CEKAPKEATV MCEQCDVFYC DPCRLRCHPP
210 220 230 240 250
RGPLAKHRLV PPAQGRVSRR LSPRKVSTCT DHELENHSMY CVQCKMPVCY
260 270 280 290 300
QCLEEGKHSS HEVKALGAMW KLHKSQLSQA LNGLSDRAKE AKEFLVQLRN
310 320 330 340 350
MVQQIQENSV EFEACLVAQC DALIDALNRR KAQLLARVNK EHEHKLKVVR
360 370 380 390 400
DQISHCTVKL RQTTGLMEYC LEVIKENDPS GFLQISDALI RRVHLTEDQW
410 420 430 440 450
GKGTLTPRMT TDFDLSLDNS PLLQSIHQLD FVQVKASSPV PATPILQLEE
460 470 480 490 500
CCTHNNSATL SWKQPPLSTV PADGYILELD DGNGGQFREV YVGKETMCTV
510 520 530 540 550
DGLHFNSTYN ARVKAFNKTG VSPYSKTLVL QTSEVAWFAF DPGSAHSDII
560 570 580 590 600
LSNDNLTVTC SSYDDRVVLG KTGFSKGIHY WELTVDRYDN HPDPAFGVAR
610 620 630 640 650
MDVMKDVMLG KDDKAWAMYV DNNRSWFMHN NSHTNRTEGG ITKGATIGVL
660 670 680 690 700
LDLNRKNLTF FINDEQQGPI AFDNVEGLFF PAVSLNRNVQ VTLHTGLPVP
710
DFYSSRASIA
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 163-266, 436-534.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 125280. 25 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.
GeneTreei ENSGT00760000118878.
HOVERGENi HBG062305.
InParanoidi Q9C026.
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.
IPR013320. ConA-like_dom.
IPR017903. COS_domain.
IPR003961. Fibronectin_type3.
IPR013783. Ig-like_fold.
IPR003877. SPRY_dom.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 139 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