PRDM5_HUMAN - dbPTM
PRDM5_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PRDM5_HUMAN
UniProt AC Q9NQX1
Protein Name PR domain zinc finger protein 5
Gene Name PRDM5
Organism Homo sapiens (Human).
Sequence Length 630
Subcellular Localization Nucleus .
Protein Description Sequence-specific DNA-binding transcription factor. Represses transcription at least in part by recruitment of the histone methyltransferase EHMT2/G9A and histone deacetylases such as HDAC1. Regulates hematopoiesis-associated protein-coding and microRNA (miRNA) genes. May regulate the expression of proteins involved in extracellular matrix development and maintenance, including fibrillar collagens, such as COL4A1 and COL11A1, connective tissue components, such as HAPLN1, and molecules regulating cell migration and adhesion, including EDIL3 and TGFB2. May caused G2/M arrest and apoptosis in cancer cells..
Protein Sequence MLGMYVPDRFSLKSSRVQDGMGLYTARRVRKGEKFGPFAGEKRMPEDLDENMDYRLMWEVRGSKGEVLYILDATNPRHSNWLRFVHEAPSQEQKNLAAIQEGENIFYLAVEDIETDTELLIGYLDSDMEAEEEEQQIMTVIKEGEVENSRRQSTAGRKDRLGCKEDYACPQCESSFTSEDILAEHLQTLHQKPTEEKEFKCKNCGKKFPVKQALQRHVLQCTAKSSLKESSRSFQCSVCNSSFSSASSFEQHQETCRGDARFVCKADSCGKRLKSKDALKRHQENVHTGDPKKKLICSVCNKKCSSASSLQEHRKIHEIFDCQECMKKFISANQLKRHMITHSEKRPYNCEICNKSFKRLDQVGAHKVIHSEDKPYKCKLCGKGFAHRNVYKNHKKTHSEERPFQCEECKALFRTPFSLQRHLLIHNSERTFKCHHCDATFKRKDTLNVHVQVVHERHKKYRCELCNKAFVTPSVLRSHKKTHTGEKEKICPYCGQKFASSGTLRVHIRSHTGERPYQCPYCEKGFSKNDGLKMHIRTHTREKPYKCSECSKAFSQKRGLDEHKRTHTGEKPFQCDVCDLAFSLKKMLIRHKMTHNPNRPLAECQFCHKKFTRNDYLKVHMDNIHGVADS
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
69PhosphorylationGSKGEVLYILDATNP
CCCCEEEEEEECCCC		12.4722817900
153PhosphorylationVENSRRQSTAGRKDR
CCCCCCCCCCCCCCC		20.57-
230PhosphorylationAKSSLKESSRSFQCS
HCCHHHHHCCCEECE		29.4830576142
231PhosphorylationKSSLKESSRSFQCSV
CCHHHHHCCCEECEE		32.79-
244PhosphorylationSVCNSSFSSASSFEQ
EECCCCCCCCCCHHH		27.2630576142
245PhosphorylationVCNSSFSSASSFEQH
ECCCCCCCCCCHHHH		30.1130576142
265AcetylationGDARFVCKADSCGKR
CCCEEEEECCCCCCC		50.347432163
331PhosphorylationECMKKFISANQLKRH
HHHHHHHCHHHHHHH		25.05-
336AcetylationFISANQLKRHMITHS
HHCHHHHHHHCCCCC		30.4111924551
463S-palmitoylationERHKKYRCELCNKAF
HHHHHHHEECCCCCC		4.2029575903
466S-palmitoylationKKYRCELCNKAFVTP
HHHHEECCCCCCCCH		1.9929575903
482PhosphorylationVLRSHKKTHTGEKEK
HHHHCCCCCCCCCHH		29.4924719451
500PhosphorylationYCGQKFASSGTLRVH
CCCCEECCCCEEEEE		32.22-
501PhosphorylationCGQKFASSGTLRVHI
CCCEECCCCEEEEEE		32.16-
503PhosphorylationQKFASSGTLRVHIRS
CEECCCCEEEEEEEC		17.22-
538PhosphorylationGLKMHIRTHTREKPY
CCEEEEEECCCCCCC		27.3124719451
540PhosphorylationKMHIRTHTREKPYKC
EEEEEECCCCCCCCC		39.6524719451
566PhosphorylationGLDEHKRTHTGEKPF
CCCHHCCCCCCCCCC		28.70-
568PhosphorylationDEHKRTHTGEKPFQC
CHHCCCCCCCCCCCC		46.56-
583PhosphorylationDVCDLAFSLKKMLIR
CHHHHHHHHHHHHHH		33.4024719451
612PhosphorylationQFCHKKFTRNDYLKV
CCCCCCCCCCCCEEE		37.13-
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of PRDM5_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PRDM5_HUMAN !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of PRDM5_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
EHMT2_HUMANEHMT2physical
17636019
HDAC1_HUMANHDAC1physical
17636019
CCD77_HUMANCCDC77physical
28514442
F102B_HUMANFAM102Bphysical
28514442
FBX11_HUMANFBXO11physical
28514442
ZN687_HUMANZNF687physical
28514442
THA11_HUMANTHAP11physical
28514442
TNC18_HUMANTNRC18physical
28514442
YBOX2_HUMANYBX2physical
28514442
ABT1_HUMANABT1physical
28514442
ZFP91_HUMANZFP91physical
28514442
ZBTB4_HUMANZBTB4physical
28514442
BAG1_HUMANBAG1physical
28514442
RL26L_HUMANRPL26L1physical
28514442
NSD2_HUMANWHSC1physical
28514442
RBM34_HUMANRBM34physical
28514442
RL10A_HUMANRPL10Aphysical
28514442
RENT1_HUMANUPF1physical
28514442
RBM28_HUMANRBM28physical
28514442
PRD10_HUMANPRDM10physical
28514442
BRX1_HUMANBRIX1physical
28514442
SPB1_HUMANFTSJ3physical
28514442
PGK2_HUMANPGK2physical
28514442
GLYR1_HUMANGLYR1physical
28514442
KIF1C_HUMANKIF1Cphysical
28514442
RL8_HUMANRPL8physical
28514442
NGRN_HUMANNGRNphysical
28514442
CASC3_HUMANCASC3physical
28514442
RL4_HUMANRPL4physical
28514442
H2A2B_HUMANHIST2H2ABphysical
28514442
SURF6_HUMANSURF6physical
28514442
PUM3_HUMANKIAA0020physical
28514442
GAR1_HUMANGAR1physical
28514442
RL18A_HUMANRPL18Aphysical
28514442
RPF2_HUMANRPF2physical
28514442
ZFP62_HUMANZFP62physical
28514442
SP130_HUMANSAP130physical
28514442
RL36_HUMANRPL36physical
28514442
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PRDM5_HUMAN

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Related Literatures of Post-Translational Modification

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