CPLM-021675

CPLM 1.0 - Compendium of Protein Lysine Modification

Tag

Content

CPLM ID

CPLM-021675

UniProt Accession

TRI39_HUMAN; Q9HCM9; Q5STG3; Q5STG4; Q76BL3; Q8IYT9; Q96IB6

Genbank Protein ID

AB046381; BT007370; AB110937; AK292512; AB110938; AB202089; AL662832; AL662795; AL773535; AL773535; BX248580; BX248580; CR759928; CR759928; BX927214; BX927214; CR759281; CR759281; CH471081; CH471081; BC007661; BC034985

Genbank Nucleotide ID

BAB16374.1; AAP36034.1; BAD13703.1; BAF85201.1; BAD13704.1; BAE78608.1; CAI17501.1; CAI18251.1; CAI41818.1; CAI41819.1; CAM25899.1; CAM25900.1; CAQ08313.1; CAQ08314.1; CAQ08383.1; CAQ08384.1; CAQ09020.1; CAQ09021.1; EAX03283.1; EAX03284.1; AAH07661.1; AAH34985.1

Protein Name

E3 ubiquitin-protein ligase TRIM39

Protein Synonyms/Alias

RING finger protein 23; Testis-abundant finger protein; Tripartite motif-containing protein 39

Gene Name

TRIM39

Gene Synonyms/Alias

RNF23; TFP

Created Date

July 27, 2013

Organism

Homo sapiens (Human)

NCBI Taxa ID

9606

Lysine Modification

Position	Peptide	Type	References
92	GSMVEIAKQLQAVKR	ubiquitination	[1]
452	PFTPLHIKVKPKRVG	ubiquitination	[1]

Reference

[1] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]

Functional Description

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.

Sequence Annotation

DOMAIN 319 514 B30.2/SPRY.
ZN_FING 29 70 RING-type.
ZN_FING 102 143 B box-type.

Keyword

3D-structure; Alternative splicing; Apoptosis; Coiled coil; Complete proteome; Cytoplasm; Ligase; Metal-binding; Mitochondrion; Reference proteome; Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger.

Sequence Source

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

Protein Length

518 AA

Protein Sequence

MAETSLLEAG ASAASTAAAL ENLQVEASCS VCLEYLKEPV IIECGHNFCK ACITRWWEDL 60
ERDFPCPVCR KTSRYRSLRP NRQLGSMVEI AKQLQAVKRK IRDESLCPQH HEALSLFCYE 120
DQEAVCLICA ISHTHRAHTV VPLDDATQEY KEKLQKCLEP LEQKLQEITR CKSSEEKKPG 180
ELKRLVESRR QQILREFEEL HRRLDEEQQV LLSRLEEEEQ DILQRLRENA AHLGDKRRDL 240
AHLAAEVEGK CLQSGFEMLK DVKSTLEKNI PRKFGGSLST ICPRDHKALL GLVKEINRCE 300
KVKTMEVTSV SIELEKNFSN FPRQYFALRK ILKQLIADVT LDPETAHPNL VLSEDRKSVK 360
FVETRLRDLP DTPRRFTFYP CVLATEGFTS GRHYWEVEVG DKTHWAVGVC RDSVSRKGEL 420
TPLPETGYWR VRLWNGDKYA ATTTPFTPLH IKVKPKRVGI FLDYEAGTLS FYNVTDRSHI 480
YTFTDTFTEK LWPLFYPGIR AGRKNAAPLT IRPPTDWE 518

Gene Ontology

GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
GO:0008270; F:zinc ion binding; IEA:InterPro.
GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.

Interpro

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.
IPR018957; Znf_C3HC4_RING-type.
IPR001841; Znf_RING.
IPR013083; Znf_RING/FYVE/PHD.
IPR017907; Znf_RING_CS.

Pfam

PF00622; SPRY
PF00643; zf-B_box
PF00097; zf-C3HC4

SMART

SM00336; BBOX
SM00589; PRY
SM00184; RING
SM00449; SPRY

PROSITE

PS50188; B302_SPRY
PS50119; ZF_BBOX
PS00518; ZF_RING_1
PS50089; ZF_RING_2

PRINTS

PR01407; BUTYPHLNCDUF.