ID A0A2K6C898_MACNE Unreviewed; 963 AA.
AC A0A2K6C898;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE SubName: Full=Tripartite motif containing 37 {ECO:0000313|Ensembl:ENSMNEP00000019867.1};
GN Name=TRIM37 {ECO:0000313|Ensembl:ENSMNEP00000019867.1};
OS Macaca nemestrina (Pig-tailed macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9545 {ECO:0000313|Ensembl:ENSMNEP00000019867.1, ECO:0000313|Proteomes:UP000233120};
RN [1] {ECO:0000313|Ensembl:ENSMNEP00000019867.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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DR RefSeq; XP_011731393.1; XM_011733091.1.
DR AlphaFoldDB; A0A2K6C898; -.
DR STRING; 9545.ENSMNEP00000019867; -.
DR Ensembl; ENSMNET00000044109.1; ENSMNEP00000019867.1; ENSMNEG00000033651.1.
DR GeneID; 105476833; -.
DR CTD; 4591; -.
DR GeneTree; ENSGT00410000025800; -.
DR OMA; XYEYRVE; -.
DR OrthoDB; 5487127at2759; -.
DR Proteomes; UP000233120; Unplaced.
DR Bgee; ENSMNEG00000033651; Expressed in temporal lobe and 12 other cell types or tissues.
DR GO; GO:0016235; C:aggresome; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0035098; C:ESC/E(Z) complex; IEA:Ensembl.
DR GO; GO:0005778; C:peroxisomal membrane; IEA:Ensembl.
DR GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
DR GO; GO:0140862; F:histone H2AK119 ubiquitin ligase activity; IEA:Ensembl.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR GO; GO:0003713; F:transcription coactivator activity; IEA:Ensembl.
DR GO; GO:0005164; F:tumor necrosis factor receptor binding; IEA:Ensembl.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:Ensembl.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0070842; P:aggresome assembly; IEA:Ensembl.
DR GO; GO:0046600; P:negative regulation of centriole replication; IEA:Ensembl.
DR GO; GO:0045814; P:negative regulation of gene expression, epigenetic; IEA:Ensembl.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0051865; P:protein autoubiquitination; IEA:Ensembl.
DR GO; GO:0016558; P:protein import into peroxisome matrix; IEA:Ensembl.
DR GO; GO:0006513; P:protein monoubiquitination; IEA:Ensembl.
DR GO; GO:0050821; P:protein stabilization; IEA:Ensembl.
DR CDD; cd19779; Bbox2_TRIM37_C-VIII; 1.
DR CDD; cd03773; MATH_TRIM37; 1.
DR CDD; cd16619; mRING-HC-C4C4_TRIM37_C-VIII; 1.
DR Gene3D; 3.30.160.60; Classic Zinc Finger; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR003649; Bbox_C.
DR InterPro; IPR002083; MATH/TRAF_dom.
DR InterPro; IPR008974; TRAF-like.
DR InterPro; IPR037299; TRIM37_MATH.
DR InterPro; IPR000315; Znf_B-box.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR36754; E3 UBIQUITIN-PROTEIN LIGASE TRIM37; 1.
DR PANTHER; PTHR36754:SF2; E3 UBIQUITIN-PROTEIN LIGASE TRIM37; 1.
DR Pfam; PF00917; MATH; 1.
DR Pfam; PF00643; zf-B_box; 1.
DR SMART; SM00502; BBC; 1.
DR SMART; SM00336; BBOX; 1.
DR SMART; SM00061; MATH; 1.
DR SUPFAM; SSF57845; B-box zinc-binding domain; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR SUPFAM; SSF49599; TRAF domain-like; 1.
DR PROSITE; PS50144; MATH; 1.
DR PROSITE; PS50119; ZF_BBOX; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000233120};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00024}.
FT DOMAIN 15..55
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 90..132
FT /note="B box-type"
FT /evidence="ECO:0000259|PROSITE:PS50119"
FT DOMAIN 276..403
FT /note="MATH"
FT /evidence="ECO:0000259|PROSITE:PS50144"
FT REGION 447..513
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 530..554
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 639..662
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 752..811
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 890..963
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 133..181
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 490..513
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 530..546
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 752..766
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 784..809
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 963 AA; 107960 MW; 1114BE67B17A69DE CRC64;
MDEQSVESIA EVFRCFICME KLRDARLCPH CSKLCCFSCI RRWLTEQRAQ CPHCRAPLQL
RELVNCRWAE EVTQQLDTLQ LCSLTKHEEN EKDKCENHHE KLSVFCWTCK KCICHQCALW
GGMHGGHTFK PLAEIYEQHV TKVNEEVAKL RRRLMELISL VQEVERNVEA VRNAKDERVR
EIRNAVEMMI ARLDTQLKNK LITLMGQKTS LTQETELLES LLQEVEHQLR SCSKSELISK
SSEILMMFQQ VHRKPMASFV TTPVPPDFTS ELVPSYDSAT FVLENFSTLR QRADPVYSPP
LQVSGLCWRL KVYPDGNGVV RGYYLSVFLE LSAGLPETSK YEYRVEMVHQ SCNDPTKNII
REFASDFEVG ECWGYNRFFR LDLLANEGYL NPQNDTVILR FQVRSPTFFQ KSRDQHWYIT
QLEAAQTSYI QQINNLKERL TIELSRTQKS RDLSPPDNHL SPQNDDVPET RAKKSACSDM
LLEGGPTTAS IREAKEDEEE EEKIQNEDYH HELSDGDLDL DLVYEDEVNQ LDGSSSSASS
TATSNTEEND IDEETMSGEN DVEYNNMELE EGELMEDAAA GPAGSNHDYV GSSSRISRRT
HLCSAATSSL LDIDPLILIH LLDLKDRSSI ENLWGLQPRP PASLLQPTAS YSRKDKDQRK
QQAMWRVPSD LKMLKRLKTQ MAEVRCMKTD VKNTLSEIKS SIAASGDMQT SLFSADQAAL
AACGTENSGR LQDLGMELLA KSSVASCYIR NSTNKKSNSP KPARSSVAGS LSLRRAVDPG
ESSRSKGDCQ TLSEGSPGSF QSGSRHSSPR ALIHGSIGDI LPKTEDRQCK ALDSDAVVVA
VFSGLPAVEK RRKMVTLGAN AKGGHLEGLQ MTDLENNSET GELQPVLPEG ASAAPEEGMS
SDSDIECDTE NEEQEEHTSV GGFHDSFMAM TQPPDEDTHS SFPDGEQIGP EDLSFNPDEN
SGR
//
