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Q9C026 (TRIM9_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 133. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
E3 ubiquitin-protein ligase TRIM9

EC=6.3.2.-
Alternative name(s):
RING finger protein 91
Tripartite motif-containing protein 9
Gene names
Name:TRIM9
Synonyms:KIAA0282, RNF91
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length710 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.7

Pathway

Protein modification; protein ubiquitination.

Subunit structure

Interacts with SNAP25 By similarity.

Subcellular location

Cytoplasm. Cell projectiondendrite. 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. Ref.7

Tissue specificity

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. Ref.7

Domain

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

Post-translational modification

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

Sequence similarities

Belongs to the TRIM/RBCC family.

Contains 2 B box-type zinc fingers.

Contains 1 B30.2/SPRY domain.

Contains 1 COS domain.

Contains 1 fibronectin type-III domain.

Contains 1 RING-type zinc finger.

Sequence caution

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: Erroneous initiation. Translation N-terminally shortened.

The sequence BAA13398.2 differs from that shown. Reason: Frameshift at position 660.

Ontologies

Keywords
   Biological processUbl conjugation pathway
   Cellular componentCell junction
Cell projection
Cytoplasm
Cytoplasmic vesicle
Cytoskeleton
Synapse
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainCoiled coil
Repeat
Zinc-finger
   LigandMetal-binding
Zinc
   Molecular functionLigase
   PTMUbl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processnegative regulation of SNARE complex assembly

Inferred from electronic annotation. Source: Ensembl

negative regulation of calcium ion-dependent exocytosis

Inferred from electronic annotation. Source: Ensembl

proteasome-mediated ubiquitin-dependent protein catabolic process

Inferred from direct assay Ref.7. Source: UniProtKB

synaptic vesicle exocytosis

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcell junction

Inferred from electronic annotation. Source: UniProtKB-KW

cytoplasm

Inferred from direct assay Ref.1Ref.7. Source: UniProtKB

cytoskeleton

Inferred from electronic annotation. Source: UniProtKB-SubCell

dendrite

Inferred from direct assay Ref.7. Source: UniProtKB

synaptic vesicle

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionprotein homodimerization activity

Inferred from physical interaction Ref.1. Source: UniProtKB

ubiquitin-protein ligase activity

Inferred from direct assay Ref.7. Source: UniProtKB

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9C026-1)

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.
Isoform 4 (identifier: Q9C026-4)

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.
Isoform 5 (identifier: Q9C026-5)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 710710E3 ubiquitin-protein ligase TRIM9
PRO_0000056208

Regions

Domain374 – 43259COS
Domain440 – 53596Fibronectin type-III
Domain533 – 702170B30.2/SPRY
Zinc finger10 – 5041RING-type
Zinc finger163 – 21250B box-type 1
Zinc finger224 – 26643B box-type 2
Coiled coil273 – 34068 Potential

Natural variations

Alternative sequence436 – 4394Missing in isoform 4.
VSP_007922
Alternative sequence5341E → EDTDSEEQTLPFPVPSERLP LRRMSPFSSTLNLQPSFPGR SYFDFRSSPHQLSLHSSLQS LNAPGCNFETQSAPYSQLVD IKKLLA in isoform 4.
VSP_007923
Alternative sequence535 – 55016VAWFA…HSDII → GKALQQYPSERELRGI in isoform 5.
VSP_007925
Alternative sequence551 – 710160Missing in isoform 5.
VSP_007926
Alternative sequence692 – 71019TLHTG…RASIA → STLPLRLNSCCWLPVQRLPR AVQSNRREGS in isoform 4.
VSP_007924
Natural variant6531L → F. Ref.1 Ref.2 Ref.6
Corresponds to variant rs2275462 [ dbSNP | Ensembl ].
VAR_016202

Experimental info

Sequence conflict3141A → V in BAB70913. Ref.2
Sequence conflict3841Q → R in BAB70913. Ref.2

Secondary structure

............... 710
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (Beta) [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: AEAB24807C89D0E2

FASTA71079,177
        10         20         30         40         50         60 
MEEMEEELKC PVCGSFYREP IILPCSHNLC QACARNILVQ TPESESPQSH RAAGSGVSDY 

        70         80         90        100        110        120 
DYLDLDKMSL YSEADSGYGS YGGFASAPTT PCQKSPNGVR VFPPAMPPPA THLSPALAPV 

       130        140        150        160        170        180 
PRNSCITCPQ CHRSLILDDR GLRGFPKNRV LEGVIDRYQQ SKAAALKCQL CEKAPKEATV 

       190        200        210        220        230        240 
MCEQCDVFYC DPCRLRCHPP RGPLAKHRLV PPAQGRVSRR LSPRKVSTCT DHELENHSMY 

       250        260        270        280        290        300 
CVQCKMPVCY QCLEEGKHSS HEVKALGAMW KLHKSQLSQA LNGLSDRAKE AKEFLVQLRN 

       310        320        330        340        350        360 
MVQQIQENSV EFEACLVAQC DALIDALNRR KAQLLARVNK EHEHKLKVVR DQISHCTVKL 

       370        380        390        400        410        420 
RQTTGLMEYC LEVIKENDPS GFLQISDALI RRVHLTEDQW GKGTLTPRMT TDFDLSLDNS 

       430        440        450        460        470        480 
PLLQSIHQLD FVQVKASSPV PATPILQLEE CCTHNNSATL SWKQPPLSTV PADGYILELD 

       490        500        510        520        530        540 
DGNGGQFREV YVGKETMCTV DGLHFNSTYN ARVKAFNKTG VSPYSKTLVL QTSEVAWFAF 

       550        560        570        580        590        600 
DPGSAHSDII LSNDNLTVTC SSYDDRVVLG KTGFSKGIHY WELTVDRYDN HPDPAFGVAR 

       610        620        630        640        650        660 
MDVMKDVMLG KDDKAWAMYV DNNRSWFMHN NSHTNRTEGG ITKGATIGVL LDLNRKNLTF 

       670        680        690        700        710 
FINDEQQGPI AFDNVEGLFF PAVSLNRNVQ VTLHTGLPVP DFYSSRASIA 

« Hide

Isoform 4 [UniParc].

Checksum: 38ABF6696A12C84C
Show »

FASTA80289,762
Isoform 5 [UniParc].

Checksum: 47ACD9147C1BE651
Show »

FASTA55061,346

References

« Hide 'large scale' references
[1]"The tripartite motif family identifies cell compartments."
Reymond A., Meroni G., Fantozzi A., Merla G., Cairo S., Luzi L., Riganelli D., Zanaria E., Messali S., Cainarca S., Guffanti A., Minucci S., Pelicci P.G., Ballabio A.
EMBO J. 20:2140-2151(2001) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_055978.4. NM_015163.5.
NP_443210.1. NM_052978.4.
UniGeneHs.654750.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2DB8NMR-A439-534[»]
ProteinModelPortalQ9C026.
SMRQ9C026. Positions 6-39, 160-268, 436-694.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid125280. 23 interactions.
IntActQ9C026. 15 interactions.
MINTMINT-1478450.
STRING9606.ENSP00000298355.

PTM databases

PhosphoSiteQ9C026.

Polymorphism databases

DMDM33516964.

2D gel databases

REPRODUCTION-2DPAGEQ9C026.

Proteomic databases

PaxDbQ9C026.
PRIDEQ9C026.

Protocols and materials databases

DNASU114088.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000298355; ENSP00000298355; ENSG00000100505. [Q9C026-1]
ENST00000338969; ENSP00000342970; ENSG00000100505. [Q9C026-4]
ENST00000360392; ENSP00000353561; ENSG00000100505. [Q9C026-5]
GeneID114088.
KEGGhsa:114088.
UCSCuc001wyx.4. human. [Q9C026-1]
uc001wyy.2. human. [Q9C026-4]
uc001wyz.4. human. [Q9C026-5]

Organism-specific databases

CTD114088.
GeneCardsGC14M051441.
HGNCHGNC:16288. TRIM9.
MIM606555. gene.
neXtProtNX_Q9C026.
PharmGKBPA38116.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG260378.
HOVERGENHBG062305.
KOK10649.
OMAPCSHNIC.
OrthoDBEOG7SJD63.
PhylomeDBQ9C026.
TreeFamTF315216.

Enzyme and pathway databases

ReactomeREACT_6900. Immune System.
UniPathwayUPA00143.

Gene expression databases

BgeeQ9C026.
CleanExHS_TRIM9.
GenevestigatorQ9C026.

Family and domain databases

Gene3D2.60.40.10. 1 hit.
3.30.40.10. 2 hits.
4.10.45.10. 1 hit.
InterProIPR001870. 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]
PfamPF00041. fn3. 1 hit.
PF00622. SPRY. 1 hit.
PF00643. zf-B_box. 1 hit.
PF00097. zf-C3HC4. 1 hit.
[Graphical view]
SMARTSM00502. BBC. 1 hit.
SM00336. BBOX. 2 hits.
SM00060. FN3. 1 hit.
SM00184. RING. 1 hit.
[Graphical view]
SUPFAMSSF49265. SSF49265. 1 hit.
SSF49899. SSF49899. 1 hit.
PROSITEPS50188. 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]
ProtoNetSearch...

Other

EvolutionaryTraceQ9C026.
GeneWikiTRIM9.
GenomeRNAi114088.
NextBio78980.
PROQ9C026.
SOURCESearch...

Entry information

Entry nameTRIM9_HUMAN
AccessionPrimary (citable) accession number: Q9C026
Secondary accession number(s): D3DSB7 expand/collapse secondary AC list , D3DSB8, Q92557, Q96D24, Q96NI4, Q9C025, Q9C027
Entry history
Integrated into UniProtKB/Swiss-Prot: August 4, 2003
Last sequence update: June 1, 2001
Last modified: April 16, 2014
This is version 133 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 14

Human chromosome 14: entries, gene names and cross-references to MIM