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Q9HCM9

- TRI39_HUMAN

UniProt

Q9HCM9 - TRI39_HUMAN

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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

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. 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
Complete GO annotation...

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, UP000005640: Unplaced

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
Complete GO annotation...

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

BgeeiQ9HCM9.
CleanExiHS_TRIM39.
ExpressionAtlasiQ9HCM9. baseline and differential.
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. 42 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 – 323Combined sources
Helixi50 – 567Combined sources
Turni108 – 1103Combined sources
Beta strandi116 – 1216Combined sources
Beta strandi123 – 1253Combined sources
Helixi127 – 1304Combined sources
Turni134 – 1374Combined sources
Beta strandi140 – 1423Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2DIDNMR-A104-143[»]
2DIFNMR-A104-143[»]
2ECJNMR-A19-69[»]
ProteinModelPortaliQ9HCM9.
SMRiQ9HCM9. Positions 13-69, 106-250, 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.
GeneTreeiENSGT00760000118893.
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.
IPR013320. ConA-like_dom.
IPR006574. PRY.
IPR003877. SPRY_dom.
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

        10         20         30         40         50
MAETSLLEAG ASAASTAAAL ENLQVEASCS VCLEYLKEPV IIECGHNFCK
60 70 80 90 100
ACITRWWEDL ERDFPCPVCR KTSRYRSLRP NRQLGSMVEI AKQLQAVKRK
110 120 130 140 150
IRDESLCPQH HEALSLFCYE DQEAVCLICA ISHTHRAHTV VPLDDATQEY
160 170 180 190 200
KEKLQKCLEP LEQKLQEITR CKSSEEKKPG ELKRLVESRR QQILREFEEL
210 220 230 240 250
HRRLDEEQQV LLSRLEEEEQ DILQRLRENA AHLGDKRRDL AHLAAEVEGK
260 270 280 290 300
CLQSGFEMLK DVKSTLEKNI PRKFGGSLST ICPRDHKALL GLVKEINRCE
310 320 330 340 350
KVKTMEVTSV SIELEKNFSN FPRQYFALRK ILKQLIADVT LDPETAHPNL
360 370 380 390 400
VLSEDRKSVK FVETRLRDLP DTPRRFTFYP CVLATEGFTS GRHYWEVEVG
410 420 430 440 450
DKTHWAVGVC RDSVSRKGEL TPLPETGYWR VRLWNGDKYA ATTTPFTPLH
460 470 480 490 500
IKVKPKRVGI FLDYEAGTLS FYNVTDRSHI YTFTDTFTEK LWPLFYPGIR
510
AGRKNAAPLT IRPPTDWE
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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, 106-250, 338-513.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 121170. 42 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.
GeneTreei ENSGT00760000118893.
HOGENOMi HOG000234133.
HOVERGENi HBG001357.
InParanoidi Q9HCM9.
KOi K12015.
OMAi VECRRQQ.
PhylomeDBi Q9HCM9.
TreeFami TF342569.

Enzyme and pathway databases

UniPathwayi UPA00143 .

Miscellaneous databases

ChiTaRSi TRIM39. human.
EvolutionaryTracei Q9HCM9.
GenomeRNAii 56658.
NextBioi 62129.
PROi Q9HCM9.
SOURCEi Search...

Gene expression databases

Bgeei Q9HCM9.
CleanExi HS_TRIM39.
ExpressionAtlasi Q9HCM9. baseline and differential.
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.
IPR013320. ConA-like_dom.
IPR006574. PRY.
IPR003877. SPRY_dom.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 138 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

Dasty 3