BAHD1_HUMAN - dbPTM
BAHD1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID BAHD1_HUMAN
UniProt AC Q8TBE0
Protein Name Bromo adjacent homology domain-containing 1 protein
Gene Name BAHD1
Organism Homo sapiens (Human).
Sequence Length 780
Subcellular Localization Nucleus . Chromosome . Localizes to heterochromatin and inactive X chromosome. Colocalizes with histone H3 trimethylated at 'Lys-27' (H3K27me3).
Protein Description Heterochromatin protein that acts as a transcription repressor and has the ability to promote the formation of large heterochromatic domains. May act by recruiting heterochromatin proteins such as CBX5 (HP1 alpha), HDAC5 and MBD1. Represses IGF2 expression by binding to its CpG-rich P3 promoter and recruiting heterochromatin proteins. At specific stages of Listeria infection, in complex with TRIM28, corepresses interferon-stimulated genes, including IFNL1, IFNL2 and IFNL3..
Protein Sequence MTHTRRKSLPMLSSGLTGRREPLQMEDSNMEQGVEGVEPGMPESPGHLTGRRKNYPLRKRPLVPEKPKACKVLLTRLENVAGPRSADEADELPPDLPKPPSPAPSSEDPGLAQPRKRRLASLNAEALNNLLLEREDTSSLAGTRRSRAGDPHRSRDRDRATGGWSSSKKRPRLGDLGGGSRDLSPEPAPDEGPRRDGDPAPKRLASLNAAAFLKLSQERELPLRLPRAHAEVDGRSTEPPAPKAPRPKWPKVNGKNYPKAWQGASSGEAAGPPGWQGCPDEPWPSATPCGPSVQPSHQPLSKALESPLGLRPHLPLLMGGQAALKPEPGRPGEESPAPKQELHQPSFPTPQLSPLPMPGNPADYNGLCVGPELTALGSFYLYCGQEGLQCGGYSPCPMLPEGKLSPVAAPHEEGLLLAPSSVPSGTPFQHPPWGSSRYCSSEDTGVNGYSICGVLPLSVTHAGTTCGGCPYKMPFAAEGCRSLGQLEFPLPEAGHPASPAHPLLGCPVPSVPPAAEPVPHLQTPTSEPQTVARACPQSAKPPSGSKSGLRTGSSCRHTARSKAARRPSHPKQPRVQRPRPRRRRRRRTNGWVPVGAACEKAVYVLDEPEPAIRKSYQAVERHGETIRVRDTVLLKSGPRKTSTPYVAKISALWENPESGELMMSLLWYYRPEHLQGGRSPSMHEPLQNEVFASRHQDQNSVACIEEKCYVLTFAEYCRFCAMAKRRGEGLPSRKTALVPPSADYSTPPHRTVPEDTDPELVFLCRHVYDFRHGRILKNPQ
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
7Ubiquitination-MTHTRRKSLPMLSS
-CCCCCHHCCCCCCC		53.72-
8PhosphorylationMTHTRRKSLPMLSSG
CCCCCHHCCCCCCCC		35.5725159151
13PhosphorylationRKSLPMLSSGLTGRR
HHCCCCCCCCCCCCC		18.9929978859
14PhosphorylationKSLPMLSSGLTGRRE
HCCCCCCCCCCCCCC		33.5826074081
28PhosphorylationEPLQMEDSNMEQGVE
CCCCCCCCCHHHCCC		25.4427251275
44PhosphorylationVEPGMPESPGHLTGR
CCCCCCCCCCCCCCC		30.2523401153
49PhosphorylationPESPGHLTGRRKNYP
CCCCCCCCCCCCCCC		23.9828450419
85PhosphorylationENVAGPRSADEADEL
HHCCCCCCHHHHHCC		43.1128464451
101PhosphorylationPDLPKPPSPAPSSED
CCCCCCCCCCCCCCC		42.0730266825
105PhosphorylationKPPSPAPSSEDPGLA
CCCCCCCCCCCCCCC		48.7630266825
106PhosphorylationPPSPAPSSEDPGLAQ
CCCCCCCCCCCCCCC		44.9830266825
121PhosphorylationPRKRRLASLNAEALN
HHHHHHHHCCHHHHH		27.0928674151
161PhosphorylationSRDRDRATGGWSSSK
CCCCCCCCCCCCCCC		36.80-
165PhosphorylationDRATGGWSSSKKRPR
CCCCCCCCCCCCCCC		28.1926425664
166PhosphorylationRATGGWSSSKKRPRL
CCCCCCCCCCCCCCC		39.4026425664
180PhosphorylationLGDLGGGSRDLSPEP
CCCCCCCCCCCCCCC		26.3730278072
184PhosphorylationGGGSRDLSPEPAPDE
CCCCCCCCCCCCCCC		31.3519664994
206PhosphorylationPAPKRLASLNAAAFL
CHHHHHHHCCHHHHH		27.0925159151
236PhosphorylationHAEVDGRSTEPPAPK
EEECCCCCCCCCCCC		42.5228555341
306PhosphorylationPLSKALESPLGLRPH
CHHHHHHCCCCCCCC		26.6925159151
335PhosphorylationPGRPGEESPAPKQEL
CCCCCCCCCCCCHHC		23.2725159151
346PhosphorylationKQELHQPSFPTPQLS
CHHCCCCCCCCCCCC		36.9726074081
349PhosphorylationLHQPSFPTPQLSPLP
CCCCCCCCCCCCCCC		22.9626074081
353PhosphorylationSFPTPQLSPLPMPGN
CCCCCCCCCCCCCCC		21.1026074081
364PhosphorylationMPGNPADYNGLCVGP
CCCCCCCCCCEECCH		17.1526074081
405PhosphorylationMLPEGKLSPVAAPHE
CCCCCCCCCCCCCCC		22.3330108239
420PhosphorylationEGLLLAPSSVPSGTP
CCEEECCCCCCCCCC		38.0625850435
421PhosphorylationGLLLAPSSVPSGTPF
CEEECCCCCCCCCCC		36.6725850435
498PhosphorylationPEAGHPASPAHPLLG
CCCCCCCCCCCCCCC		27.3726074081
523PhosphorylationEPVPHLQTPTSEPQT
CCCCCCCCCCCCCHH		34.5926714015
525PhosphorylationVPHLQTPTSEPQTVA
CCCCCCCCCCCHHHH		49.4626714015
526PhosphorylationPHLQTPTSEPQTVAR
CCCCCCCCCCHHHHH		48.7826714015
530PhosphorylationTPTSEPQTVARACPQ
CCCCCCHHHHHHCCC		27.1826714015
538PhosphorylationVARACPQSAKPPSGS
HHHHCCCCCCCCCCC		24.3329396449
543PhosphorylationPQSAKPPSGSKSGLR
CCCCCCCCCCCCCCC		65.3125159151
545PhosphorylationSAKPPSGSKSGLRTG
CCCCCCCCCCCCCCC		28.1728985074
588PhosphorylationRRRRRRRTNGWVPVG
CHHHHHCCCCCCCCC		35.9523401153
603PhosphorylationAACEKAVYVLDEPEP
HHCCEEEEECCCCCH		10.5120068231
679PhosphorylationEHLQGGRSPSMHEPL
HHCCCCCCCCCCHHH		25.3030108239
679 (in isoform 3)Phosphorylation-25.3020068231
681PhosphorylationLQGGRSPSMHEPLQN
CCCCCCCCCCHHHHC		33.7427080861
681 (in isoform 3)Phosphorylation-33.7426657352
690 (in isoform 3)Phosphorylation-6.7820068231
732PhosphorylationRRGEGLPSRKTALVP
HCCCCCCCCCCEECC		51.9920860994
741PhosphorylationKTALVPPSADYSTPP
CCEECCCCCCCCCCC		27.92-
744PhosphorylationLVPPSADYSTPPHRT
ECCCCCCCCCCCCCC		17.73-
745PhosphorylationVPPSADYSTPPHRTV
CCCCCCCCCCCCCCC		34.68-
746PhosphorylationPPSADYSTPPHRTVP
CCCCCCCCCCCCCCC		34.3128555341
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 BAHD1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of BAHD1_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 BAHD1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
BEGIN_HUMANBEGAINphysical
16189514
KR412_HUMANKRTAP4-12physical
16189514
TIF1B_HUMANTRIM28physical
21252314
HDAC1_HUMANHDAC1physical
21252314
HDAC2_HUMANHDAC2physical
21252314
CBX3_HUMANCBX3physical
21252314
KDM1A_HUMANKDM1Aphysical
23455924
SUV91_HUMANSUV39H1physical
23455924
LZTS2_HUMANLZTS2physical
25416956
K1C40_HUMANKRT40physical
25416956
KR107_HUMANKRTAP10-7physical
25416956
KR101_HUMANKRTAP10-1physical
25416956
KR103_HUMANKRTAP10-3physical
25416956
LZTS2_HUMANLZTS2physical
21516116
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of BAHD1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-101; SER-121 ANDSER-184, AND MASS SPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-101 AND SER-121, ANDMASS SPECTROMETRY.
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis.";
Wang B., Malik R., Nigg E.A., Korner R.;
Anal. Chem. 80:9526-9533(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-184, AND MASSSPECTROMETRY.

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