MACD1_HUMAN - dbPTM
MACD1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MACD1_HUMAN
UniProt AC Q9BQ69
Protein Name O-acetyl-ADP-ribose deacetylase MACROD1
Gene Name MACROD1
Organism Homo sapiens (Human).
Sequence Length 325
Subcellular Localization Nucleus . Recruited to DNA lesions, probably via mono-APD-ribosylated proteins.
Protein Description Removes ADP-ribose from glutamate residues in proteins bearing a single ADP-ribose moiety. Inactive towards proteins bearing poly-ADP-ribose. Deacetylates O-acetyl-ADP ribose, a signaling molecule generated by the deacetylation of acetylated lysine residues in histones and other proteins. Plays a role in estrogen signaling. Binds to androgen receptor (AR) and amplifies the transactivation function of AR in response to androgen. May play an important role in carcinogenesis and/or progression of hormone-dependent cancers by feed-forward mechanism that activates ESR1 transactivation. Could be an ESR1 coactivator, providing a positive feedback regulatory loop for ESR1 signal transduction. Could be involved in invasive growth by down-regulating CDH1 in endometrial cancer cells. Enhances ESR1-mediated transcription activity..
Protein Sequence MSLQSRLSGRLAQLRAAGQLLVPPRPRPGHLAGATRTRSSTCGPPAFLGVFGRRARTSAGVGAWGAAAVGRTAGVRTWAPLAMAAKVDLSTSTDWKEAKSFLKGLSDKQREEHYFCKDFVRLKKIPTWKEMAKGVAVKVEEPRYKKDKQLNEKISLLRSDITKLEVDAIVNAANSSLLGGGGVDGCIHRAAGPLLTDECRTLQSCKTGKAKITGGYRLPAKYVIHTVGPIAYGEPSASQAAELRSCYLSSLDLLLEHRLRSVAFPCISTGVFGYPCEAAAEIVLATLREWLEQHKDKVDRLIICVFLEKDEDIYRSRLPHYFPVA
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
90PhosphorylationMAAKVDLSTSTDWKE
HEECCCCCCCCCHHH		18.8220873877
91PhosphorylationAAKVDLSTSTDWKEA
EECCCCCCCCCHHHH		42.8320873877
92PhosphorylationAKVDLSTSTDWKEAK
ECCCCCCCCCHHHHH		22.4625627689
93PhosphorylationKVDLSTSTDWKEAKS
CCCCCCCCCHHHHHH		46.0620873877
96UbiquitinationLSTSTDWKEAKSFLK
CCCCCCHHHHHHHHH		51.08-
96SuccinylationLSTSTDWKEAKSFLK
CCCCCCHHHHHHHHH		51.0823954790
96AcetylationLSTSTDWKEAKSFLK
CCCCCCHHHHHHHHH		51.0825953088
96SuccinylationLSTSTDWKEAKSFLK
CCCCCCHHHHHHHHH		51.08-
100PhosphorylationTDWKEAKSFLKGLSD
CCHHHHHHHHHCCCH		42.7424719451
103MalonylationKEAKSFLKGLSDKQR
HHHHHHHHCCCHHHH		56.6526320211
103AcetylationKEAKSFLKGLSDKQR
HHHHHHHHCCCHHHH		56.6519608861
103SuccinylationKEAKSFLKGLSDKQR
HHHHHHHHCCCHHHH		56.65-
103SuccinylationKEAKSFLKGLSDKQR
HHHHHHHHCCCHHHH		56.65-
117MalonylationREEHYFCKDFVRLKK
HHHHHCCCHHHHHHC		44.2832601280
129SuccinylationLKKIPTWKEMAKGVA
HHCCCCHHHHHCCCE		39.84-
129MalonylationLKKIPTWKEMAKGVA
HHCCCCHHHHHCCCE		39.8426320211
129SuccinylationLKKIPTWKEMAKGVA
HHCCCCHHHHHCCCE		39.84-
129AcetylationLKKIPTWKEMAKGVA
HHCCCCHHHHHCCCE		39.8426822725
133SuccinylationPTWKEMAKGVAVKVE
CCHHHHHCCCEEEEC		53.2423954790
138SumoylationMAKGVAVKVEEPRYK
HHCCCEEEECCCCHH		33.9028112733
138SumoylationMAKGVAVKVEEPRYK
HHCCCEEEECCCCHH		33.90-
148AcetylationEPRYKKDKQLNEKIS
CCCHHHHHHHHHHHH		66.6125953088
153AcetylationKDKQLNEKISLLRSD
HHHHHHHHHHHHHHC		36.2025953088
163AcetylationLLRSDITKLEVDAIV
HHHHCCHHHHHHHHH		42.8823236377
2062-HydroxyisobutyrylationCRTLQSCKTGKAKIT
CCHHHHCCCCCCEEC		66.61-
222PhosphorylationGYRLPAKYVIHTVGP
CCCCCCEEEEEECCC		13.5226437602
226PhosphorylationPAKYVIHTVGPIAYG
CCEEEEEECCCHHCC		18.9422673903
232PhosphorylationHTVGPIAYGEPSASQ
EECCCHHCCCCCHHH		23.8127642862
236PhosphorylationPIAYGEPSASQAAEL
CHHCCCCCHHHHHHH		35.9328348404
238PhosphorylationAYGEPSASQAAELRS
HCCCCCHHHHHHHHH		25.3728348404
244MethylationASQAAELRSCYLSSL
HHHHHHHHHHHHHHH		19.04115482467
297AcetylationWLEQHKDKVDRLIIC
HHHHCCHHCCEEEEE		51.3325953088
309AcetylationIICVFLEKDEDIYRS
EEEEEECCCHHHHHH		69.4430590221
321PhosphorylationYRSRLPHYFPVA---
HHHCCCCCCCCC---		13.9827642862
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 MACD1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MACD1_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 MACD1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NEMO_HUMANIKBKGphysical
25735744
PARP1_HUMANPARP1physical
25735744
XRCC6_HUMANXRCC6physical
25735744
XRCC5_HUMANXRCC5physical
25735744
IKKB_HUMANIKBKBphysical
25735744
RB6I2_HUMANERC1physical
25735744
E2AK2_HUMANEIF2AK2physical
25735744
HNRPU_HUMANHNRNPUphysical
25735744
CSTF3_HUMANCSTF3physical
25735744
YBOX1_HUMANYBX1physical
25735744
DHX9_HUMANDHX9physical
25735744
DDX21_HUMANDDX21physical
25735744
2AAA_HUMANPPP2R1Aphysical
25735744
H2AX_HUMANH2AFXphysical
28514442
PARP1_HUMANPARP1physical
28514442
PARP2_HUMANPARP2physical
28514442
SP16H_HUMANSUPT16Hphysical
28514442
XPC_HUMANXPCphysical
28514442
SSRP1_HUMANSSRP1physical
28514442
CETN2_HUMANCETN2physical
28514442
DNLI3_HUMANLIG3physical
28514442
HBE_HUMANHBE1physical
28514442
RFA1_HUMANRPA1physical
28514442
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 MACD1_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-103, AND MASS SPECTROMETRY.

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