CPLM-013324

CPLM 1.0 - Compendium of Protein Lysine Modification

Tag

Content

CPLM ID

CPLM-013324

UniProt Accession

ARI4B_HUMAN; Q4LE39; A1L465; Q3MHV4; Q5HY99; Q5T2C2; Q5T2C3; Q5T2C4; Q5T2C5; Q5T2C6; Q6P600; Q86UX1; Q86WR4; Q9H915; Q9NYU3; Q9NZB6; Q9NZG4; Q9P2W4; Q9UF62; Q9Y6E1

Genbank Protein ID

AF214114; AY220790; AF208045; AB030181; AB210032; AL391994; AL133418; AL391994; AL391994; AL133418; AL133418; AL391994; AL133418; AL391994; BC048959; BC062536; BC104632; BC130418; BX648820; AL133594; AF227899; AF083249; AK023144

Genbank Nucleotide ID

AAF28341.2; AAO63590.1; AAF23433.3; BAA89794.1; BAE06114.1; CAI13747.2; CAI13747.2; CAI13749.1; CAI13751.1; CAI13751.1; CAI22961.2; CAI22961.2; CAI22962.1; CAI22962.1; AAH48959.1; AAH62536.1; AAI04633.1; AAI30419.1; CAI46047.1; CAB63731.1; AAF36964.1; AAD41239.1; BAB14428.1

Protein Name

AT-rich interactive domain-containing protein 4B

Protein Synonyms/Alias

ARID domain-containing protein 4B; 180 kDa Sin3-associated polypeptide; Sin3-associated polypeptide p180; Breast cancer-associated antigen BRCAA1; Histone deacetylase complex subunit SAP180; Retinoblastoma-binding protein 1-like 1

Gene Name

ARID4B

Gene Synonyms/Alias

BRCAA1; RBBP1L1; RBP1L1; SAP180

Created Date

July 27, 2013

Organism

Homo sapiens (Human)

NCBI Taxa ID

9606

Lysine Modification

Position	Peptide	Type	References
429	NVKEIKVKEENETEI	sumoylation	[1, 2]
440	ETEIKEIKMEEERNI	sumoylation	[1]
878	AKMTPTKKYNGLEEK	acetylation	[3]

Reference

[1] RBP1 family proteins exhibit SUMOylation-dependent transcriptional repression and induce cell growth inhibition reminiscent of senescence.
Binda O, Roy JS, Branton PE.
Mol Cell Biol. 2006 Mar;26(5):1917-31. [PMID: 16479010]
[2] Site-specific identification of SUMO-2 targets in cells reveals an inverted SUMOylation motif and a hydrophobic cluster SUMOylation motif.
Matic I, Schimmel J, Hendriks IA, van Santen MA, van de Rijke F, van Dam H, Gnad F, Mann M, Vertegaal AC.
Mol Cell. 2010 Aug 27;39(4):641-52. [PMID: 20797634]
[3] Regulation of cellular metabolism by protein lysine acetylation.
Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786]

Functional Description

Acts as a transcriptional repressor. May function in the assembly and/or enzymatic activity of the Sin3A corepressor complex or in mediating interactions between the complex and other regulatory complexes.

Sequence Annotation

DOMAIN 306 398 ARID.
REGION 465 473 Antigenic epitope.
REGION 1130 1137 Antigenic epitope.
MOD_RES 276 276 Phosphoserine.
MOD_RES 666 666 Phosphoserine.
MOD_RES 675 675 Phosphoserine.
MOD_RES 717 717 Phosphoserine.
MOD_RES 778 778 Phosphoserine.
MOD_RES 790 790 Phosphoserine.
MOD_RES 793 793 Phosphothreonine.
MOD_RES 1014 1014 Phosphoserine.
MOD_RES 1026 1026 Phosphothreonine.
MOD_RES 1150 1150 Phosphothreonine.
MOD_RES 1152 1152 Phosphoserine.
MOD_RES 1153 1153 Phosphoserine.
MOD_RES 1155 1155 Phosphoserine.
MOD_RES 1159 1159 Phosphoserine.

Keyword

Alternative splicing; Coiled coil; Complete proteome; Cytoplasm; DNA-binding; Nucleus; Phosphoprotein; Reference proteome; Transcription; Transcription regulation.

Sequence Source

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

Protein Length

1312 AA

Protein Sequence

MKALDEPPYL TVGTDVSAKY RGAFCEAKIK TAKRLVKVKV TFRHDSSTVE VQDDHIKGPL 60
KVGAIVEVKN LDGAYQEAVI NKLTDASWYT VVFDDGDEKT LRRSSLCLKG ERHFAESETL 120
DQLPLTNPEH FGTPVIGKKT NRGRRSNHIP EEESSSSSSD EDEDDRKQID ELLGKVVCVD 180
YISLDKKKAL WFPALVVCPD CSDEIAVKKD NILVRSFKDG KFTSVPRKDV HEITSDTAPK 240
PDAVLKQAFE QALEFHKSRT IPANWKTELK EDSSSSEAEE EEEEEDDEKE KEDNSSEEEE 300
EIEPFPEERE NFLQQLYKFM EDRGTPINKR PVLGYRNLNL FKLFRLVHKL GGFDNIESGA 360
VWKQVYQDLG IPVLNSAAGY NVKCAYKKYL YGFEEYCRSA NIEFQMALPE KVVNKQCKEC 420
ENVKEIKVKE ENETEIKEIK MEEERNIIPR EEKPIEDEIE RKENIKPSLG SKKNLLESIP 480
THSDQEKEVN IKKPEDNENL DDKDDDTTRV DESLNIKVEA EEEKAKSGDE TNKEEDEDDE 540
EAEEEEEEEE EEEDEDDDDN NEEEEFECYP PGMKVQVRYG RGKNQKMYEA SIKDSDVEGG 600
EVLYLVHYCG WNVRYDEWIK ADKIVRPADK NVPKIKHRKK IKNKLDKEKD KDEKYSPKNC 660
KLRRLSKPPF QTNPSPEMVS KLDLTDAKNS DTAHIKSIEI TSILNGLQAS ESSAEDSEQE 720
DERGAQDMDN NGKEESKIDH LTNNRNDLIS KEEQNSSSLL EENKVHADLV ISKPVSKSPE 780
RLRKDIEVLS EDTDYEEDEV TKKRKDVKKD TTDKSSKPQI KRGKRRYCNT EECLKTGSPG 840
KKEEKAKNKE SLCMENSSNS SSDEDEEETK AKMTPTKKYN GLEEKRKSLR TTGFYSGFSE 900
VAEKRIKLLN NSDERLQNSR AKDRKDVWSS IQGQWPKKTL KELFSDSDTE AAASPPHPAP 960
EEGVAEESLQ TVAEEESCSP SVELEKPPPV NVDSKPIEEK TVEVNDRKAE FPSSGSNSVL 1020
NTPPTTPESP SSVTVTEGSR QQSSVTVSEP LAPNQEEVRS IKSETDSTIE VDSVAGELQD 1080
LQSEGNSSPA GFDASVSSSS SNQPEPEHPE KACTGQKRVK DAQGGGSSSK KQKRSHKATV 1140
VNNKKKGKGT NSSDSEELSA GESITKSQPV KSVSTGMKSH STKSPARTQS PGKCGKNGDK 1200
DPDLKEPSNR LPKVYKWSFQ MSDLENMTSA ERITILQEKL QEIRKHYLSL KSEVASIDRR 1260
RKRLKKKERE SAATSSSSSS PSSSSITAAV MLTLAEPSMS SASQNGMSVE CR 1312

Gene Ontology

GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO:0006355; P:regulation of transcription, DNA-dependent; IEA:UniProtKB-KW.
GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW.

Interpro

IPR001606; ARID/BRIGHT_DNA-bd.
IPR000953; Chromo_domain/shadow.
IPR016197; Chromodomain-like.
IPR012603; RBB1NT.
IPR002999; Tudor.
IPR025995; Tudor-knot.

Pfam

PF01388; ARID
PF08169; RBB1NT
PF11717; Tudor-knot

SMART

SM00501; BRIGHT
SM00298; CHROMO
SM00333; TUDOR

PROSITE

PS51011; ARID

PRINTS