CPLM-023188

CPLM 1.0 - Compendium of Protein Lysine Modification

Tag

Content

CPLM ID

CPLM-023188

UniProt Accession

PKCB1_HUMAN; Q9ULU4; B7Z680; E1P5U5; Q13517; Q2HXV2; Q2HXV7; Q2HXV8; Q2HXW0; Q2HXW1; Q2HXW2; Q4JJ94; Q4JJ95; Q5TH09; Q6MZM1; Q8WXC5; Q9H1F3; Q9H1F4; Q9H1F5; Q9H1L8; Q9H1L9; Q9H2G5; Q9NYN3; Q9UIX6

Genbank Protein ID

AF233453; U48251; AF454056; AF273045; DQ082998; DQ082999; DQ368673; DQ368674; DQ368679; DQ368669; DQ368670; DQ368671; AB032951; AK299899; BX641005; AL031666; AL049540; AL022342; AL049540; AL031666; AL022342; CH471077; CH471077; CH471077; CH471077; CH471077; BC030721

Genbank Nucleotide ID

AAF71262.1; AAC72244.1; AAL50790.1; AAG34905.1; AAY85630.1; AAY85631.1; ABC86684.1; ABC86685.1; ABC86690.1; ABC86680.1; ABC86681.1; ABC86682.1; BAA86439.1; BAH13166.1; CAE46008.1; CAI21842.1; CAI21842.1; CAI21842.1; CAI23169.1; CAI23169.1; CAI23169.1; EAW75703.1; EAW75706.1; EAW75709.1; EAW75712.1; EAW75715.1; AAH30721.2

Protein Name

Protein kinase C-binding protein 1

Protein Synonyms/Alias

Cutaneous T-cell lymphoma-associated antigen se14-3; CTCL-associated antigen se14-3; Rack7; Zinc finger MYND domain-containing protein 8

Gene Name

ZMYND8

Gene Synonyms/Alias

KIAA1125; PRKCBP1; RACK7

Created Date

July 27, 2013

Organism

Homo sapiens (Human)

NCBI Taxa ID

9606

Lysine Modification

Position	Peptide	Type	References
356	YVENIRRKFGVFNYS	ubiquitination	[1]
413	SPKILMSKPVLSGGT	acetylation	[2]
645	PTNPVEIKEELKSTS	sumoylation	[3]

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]
[2] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
[3] 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]

Functional Description

Sequence Annotation

DOMAIN 165 235 Bromo.
DOMAIN 277 327 PWWP.
ZN_FING 88 133 PHD-type.
ZN_FING 1028 1062 MYND-type.
REGION 1147 1186 Interacts with PRKCB1.
MOD_RES 404 404 Phosphothreonine.
MOD_RES 406 406 Phosphoserine.
MOD_RES 413 413 N6-acetyllysine.
MOD_RES 425 425 Phosphoserine.
MOD_RES 432 432 Phosphoserine.
MOD_RES 444 444 Phosphoserine.
MOD_RES 462 462 Phosphoserine.
MOD_RES 465 465 Phosphoserine.
MOD_RES 486 486 Phosphoserine.
MOD_RES 490 490 Phosphoserine.
MOD_RES 495 495 Phosphoserine.
MOD_RES 541 541 Phosphothreonine.
MOD_RES 547 547 Phosphoserine.
MOD_RES 668 668 Phosphoserine.
MOD_RES 682 682 Phosphoserine.
MOD_RES 746 746 Phosphothreonine.
MOD_RES 754 754 Phosphoserine.
MOD_RES 756 756 Phosphoserine.

Keyword

Acetylation; Alternative splicing; Bromodomain; Complete proteome; Metal-binding; Phosphoprotein; Polymorphism; Reference proteome; Zinc; Zinc-finger.

Sequence Source

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

Protein Length

1186 AA

Protein Sequence

MDISTRSKDP GSAERTAQKR KFPSPPHSSN GHSPQDTSTS PIKKKKKPGL LNSNNKEQSE 60
LRHGPFYYMK QPLTTDPVDV VPQDGRNDFY CWVCHREGQV LCCELCPRVY HAKCLRLTSE 120
PEGDWFCPEC EKITVAECIE TQSKAMTMLT IEQLSYLLKF AIQKMKQPGT DAFQKPVPLE 180
QHPDYAEYIF HPMDLCTLEK NAKKKMYGCT EAFLADAKWI LHNCIIYNGG NHKLTQIAKV 240
VIKICEHEMN EIEVCPECYL AACQKRDNWF CEPCSNPHPL VWAKLKGFPF WPAKALRDKD 300
GQVDARFFGQ HDRAWVPINN CYLMSKEIPF SVKKTKSIFN SAMQEMEVYV ENIRRKFGVF 360
NYSPFRTPYT PNSQYQMLLD PTNPSAGTAK IDKQEKVKLN FDMTASPKIL MSKPVLSGGT 420
GRRISLSDMP RSPMSTNSSV HTGSDVEQDA EKKATSSHFS ASEESMDFLD KSTASPASTK 480
TGQAGSLSGS PKPFSPQLSA PITTKTDKTS TTGSILNLNL DRSKAEMDLK ELSESVQQQS 540
TPVPLISPKR QIRSRFQLNL DKTIESCKAQ LGINEISEDV YTAVEHSDSE DSEKSDSSDS 600
EYISDDEQKS KNEPEDTEDK EGCQMDKEPS AVKKKPKPTN PVEIKEELKS TSPASEKADP 660
GAVKDKASPE PEKDFSEKAK PSPHPIKDKL KGKDETDSPT VHLGLDSDSE SELVIDLGED 720
HSGREGRKNK KEPKEPSPKQ DVVGKTPPST TVGSHSPPET PVLTRSSAQT SAAGATATTS 780
TSSTVTVTAP APAATGSPVK KQRPLLPKET APAVQRVVWN SSSKFQTSSQ KWHMQKMQRQ 840
QQQQQQQNQQ QQPQSSQGTR YQTRQAVKAV QQKEITQSPS TSTITLVTST QSSPLVTSSG 900
SMSTLVSSVN ADLPIATASA DVAADIAKYT SKMMDAIKGT MTEIYNDLSK NTTGSTIAEI 960
RRLRIEIEKL QWLHQQELSE MKHNLELTMA EMRQSLEQER DRLIAEVKKQ LELEKQQAVD 1020
ETKKKQWCAN CKKEAIFYCC WNTSYCDYPC QQAHWPEHMK SCTQSATAPQ QEADAEVNTE 1080
TLNKSSQGSS SSTQSAPSET ASASKEKETS AEKSKESGST LDLSGSRETP SSILLGSNQG 1140
SDHSRSNKSS WSSSDEKRGS TRSDHNTSTS TKSLLPKESR LDTFWD 1186

Gene Ontology

GO:0005634; C:nucleus; ISS:BHF-UCL.
GO:0070491; F:repressing transcription factor binding; ISS:BHF-UCL.
GO:0001106; F:RNA polymerase II transcription corepressor activity; ISS:BHF-UCL.
GO:0008270; F:zinc ion binding; IEA:InterPro.

Interpro

IPR001487; Bromodomain.
IPR021931; DUF3544.
IPR000313; PWWP.
IPR019786; Zinc_finger_PHD-type_CS.
IPR011011; Znf_FYVE_PHD.
IPR002893; Znf_MYND.
IPR001965; Znf_PHD.
IPR019787; Znf_PHD-finger.
IPR013083; Znf_RING/FYVE/PHD.

Pfam

PF00439; Bromodomain
PF12064; DUF3544
PF00628; PHD
PF00855; PWWP
PF01753; zf-MYND

SMART

SM00297; BROMO
SM00249; PHD

PROSITE

PS50014; BROMODOMAIN_2
PS50812; PWWP
PS01360; ZF_MYND_1
PS50865; ZF_MYND_2
PS01359; ZF_PHD_1
PS50016; ZF_PHD_2

PRINTS