ACD_HUMAN - dbPTM
ACD_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ACD_HUMAN
UniProt AC Q96AP0
Protein Name Adrenocortical dysplasia protein homolog
Gene Name ACD
Organism Homo sapiens (Human).
Sequence Length 544
Subcellular Localization Nucleus . Chromosome, telomere .
Protein Description Component of the shelterin complex (telosome) that is involved in the regulation of telomere length and protection. Shelterin associates with arrays of double-stranded TTAGGG repeats added by telomerase and protects chromosome ends. Without its protective activity, telomeres are no longer hidden from the DNA damage surveillance and chromosome ends are inappropriately processed by DNA repair pathways. Promotes binding of POT1 to single-stranded telomeric DNA. Modulates the inhibitory effects of POT1 on telomere elongation. The ACD-POT1 heterodimer enhances telomere elongation by recruiting telomerase to telomeres and increasing its processivity. May play a role in organogenesis..
Protein Sequence MPGRCQSDAAMRVNGPASRAPAGWTSGSLHTGPRAGRPRAQARGVRGRGLLLRPRPAKELPLPRKGGAWAPAGNPGPLHPLGVAVGMAGSGRLVLRPWIRELILGSETPSSPRAGQLLEVLQDAEAAVAGPSHAPDTSDVGATLLVSDGTHSVRCLVTREALDTSDWEEKEFGFRGTEGRLLLLQDCGVHVQVAEGGAPAEFYLQVDRFSLLPTEQPRLRVPGCNQDLDVQKKLYDCLEEHLSESTSSNAGLSLSQLLDEMREDQEHQGALVCLAESCLTLEGPCTAPPVTHWAASRCKATGEAVYTVPSSMLCISENDQLILSSLGPCQRTQGPELPPPDPALQDLSLTLIASPPSSPSSSGTPALPGHMSSEESGTSISLLPALSLAAPDPGQRSSSQPSPAICSAPATLTPRSPHASRTPSSPLQSCTPSLSPRSHVPSPHQALVTRPQKPSLEFKEFVGLPCKNRPPFPRTGATRGAQEPCSVWEPPKRHRDGSAFQYEYEPPCTSLCARVQAVRLPPQLMAWALHFLMDAQPGSEPTPM
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
25PhosphorylationSRAPAGWTSGSLHTG
HHCCCCCCCCCCCCC		23.4624275569
106PhosphorylationIRELILGSETPSSPR
HHHHHHCCCCCCCCC		34.5523401153
108PhosphorylationELILGSETPSSPRAG
HHHHCCCCCCCCCHH		30.1229255136
110 (in isoform 2)Phosphorylation-61.4725849741
110PhosphorylationILGSETPSSPRAGQL
HHCCCCCCCCCHHHH		61.4729255136
111 (in isoform 2)Phosphorylation-21.4329507054
111PhosphorylationLGSETPSSPRAGQLL
HCCCCCCCCCHHHHH		21.4329255136
167 (in isoform 2)Ubiquitination-18.5321906983
170 (in isoform 1)Ubiquitination-46.9921906983
170UbiquitinationDTSDWEEKEFGFRGT
CCCCCCCHHHCCCCC		46.9921906983
232UbiquitinationNQDLDVQKKLYDCLE
CCCHHHHHHHHHHHH		44.59-
233UbiquitinationQDLDVQKKLYDCLEE
CCHHHHHHHHHHHHH		34.882210193
248PhosphorylationHLSESTSSNAGLSLS
HHCCCCCCCCCCCHH		30.6850563075
255PhosphorylationSNAGLSLSQLLDEMR
CCCCCCHHHHHHHHH		18.5330814581
349PhosphorylationPALQDLSLTLIASPP
HHHHHCEEEEEECCC		6.1723186163
397PhosphorylationAPDPGQRSSSQPSPA
CCCCCCCCCCCCCCC		26.8423663014
398PhosphorylationPDPGQRSSSQPSPAI
CCCCCCCCCCCCCCC		34.8723663014
399PhosphorylationDPGQRSSSQPSPAIC
CCCCCCCCCCCCCCC		47.5623663014
402PhosphorylationQRSSSQPSPAICSAP
CCCCCCCCCCCCCCC		21.2330266825
407PhosphorylationQPSPAICSAPATLTP
CCCCCCCCCCCCCCC		31.0430266825
411PhosphorylationAICSAPATLTPRSPH
CCCCCCCCCCCCCCC		30.0623898821
413PhosphorylationCSAPATLTPRSPHAS
CCCCCCCCCCCCCCC		16.5821712546
416PhosphorylationPATLTPRSPHASRTP
CCCCCCCCCCCCCCC		23.4223401153
420PhosphorylationTPRSPHASRTPSSPL
CCCCCCCCCCCCCCC		33.3828450419
422PhosphorylationRSPHASRTPSSPLQS
CCCCCCCCCCCCCCC		25.6530266825
424PhosphorylationPHASRTPSSPLQSCT
CCCCCCCCCCCCCCC		43.9330266825
425PhosphorylationHASRTPSSPLQSCTP
CCCCCCCCCCCCCCC		30.7325159151
429PhosphorylationTPSSPLQSCTPSLSP
CCCCCCCCCCCCCCC		27.8630266825
431PhosphorylationSSPLQSCTPSLSPRS
CCCCCCCCCCCCCCC		22.5930266825
433PhosphorylationPLQSCTPSLSPRSHV
CCCCCCCCCCCCCCC		24.2730266825
435PhosphorylationQSCTPSLSPRSHVPS
CCCCCCCCCCCCCCC		23.7025159151
437MethylationCTPSLSPRSHVPSPH
CCCCCCCCCCCCCHH		35.70-
438PhosphorylationTPSLSPRSHVPSPHQ
CCCCCCCCCCCCHHH		32.0228122231
442PhosphorylationSPRSHVPSPHQALVT
CCCCCCCCHHHHCCC		33.6546157515
449PhosphorylationSPHQALVTRPQKPSL
CHHHHCCCCCCCCCC		37.1730576142
450MethylationPHQALVTRPQKPSLE
HHHHCCCCCCCCCCC		24.95-
453MethylationALVTRPQKPSLEFKE
HCCCCCCCCCCCHHH		38.98-
455PhosphorylationVTRPQKPSLEFKEFV
CCCCCCCCCCHHHCC		47.7929214152
467SumoylationEFVGLPCKNRPPFPR
HCCCCCCCCCCCCCC		54.7928112733
467UbiquitinationEFVGLPCKNRPPFPR
HCCCCCCCCCCCCCC		54.79-
469MethylationVGLPCKNRPPFPRTG
CCCCCCCCCCCCCCC		26.26-
492UbiquitinationCSVWEPPKRHRDGSA
CCCCCCCCCCCCCCC		72.11-
498PhosphorylationPKRHRDGSAFQYEYE
CCCCCCCCCCCCEEC		30.1430834977
504PhosphorylationGSAFQYEYEPPCTSL
CCCCCCEECCCHHHH		28.8930834971
510PhosphorylationEYEPPCTSLCARVQA
EECCCHHHHHHHHHH		28.3324719451
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
169SPhosphorylationKinaseNEK6Q9HC98
PSP
255SPhosphorylationKinaseNEK6Q9HC98
GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ACD_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 ACD_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TINF2_HUMANTINF2physical
15231715
TERF1_HUMANTERF1physical
15231715
TINF2_HUMANTINF2physical
15181449
POTE1_HUMANPOT1physical
15181449
XRCC6_HUMANXRCC6physical
16169070
POTE1_HUMANPOT1physical
15383534
TERF2_HUMANTERF2physical
15383534
TINF2_HUMANTINF2physical
15383534
RGS3_HUMANRGS3physical
21044950
LRC25_HUMANLRRC25physical
21044950
ADPRH_HUMANADPRHphysical
21044950
CHIP_HUMANSTUB1physical
21044950
ABC3F_HUMANAPOBEC3Fphysical
21044950
FKBP6_HUMANFKBP6physical
21044950
POTE1_HUMANPOT1physical
21044950
TRI15_HUMANTRIM15physical
21044950
SRC8_HUMANCTTNphysical
21044950
STIP1_HUMANSTIP1physical
21044950
INVO_HUMANIVLphysical
21044950
RBSK_HUMANRBKSphysical
21044950
ENSA_HUMANENSAphysical
21044950
EIF3G_HUMANEIF3Gphysical
21044950
1433E_HUMANYWHAEphysical
21044950
PDLI2_HUMANPDLIM2physical
21044950
TINF2_HUMANTINF2physical
21044950
TBB2A_HUMANTUBB2Aphysical
21044950
IPO5_HUMANIPO5physical
21044950
DPYL3_HUMANDPYSL3physical
21044950
TBCD_HUMANTBCDphysical
21044950
TB10A_HUMANTBC1D10Aphysical
21044950
LEGL_HUMANLGALSLphysical
21044950
ANKY2_HUMANANKMY2physical
21044950
NCDN_HUMANNCDNphysical
21044950
PEX5_HUMANPEX5physical
21044950
RSSA_HUMANRPSAphysical
21044950
F131B_HUMANFAM131Bphysical
21044950
NUDC_HUMANNUDCphysical
21044950
AIPL1_HUMANAIPL1physical
21044950
TAGL_HUMANTAGLNphysical
21044950
BAG3_HUMANBAG3physical
21044950
ACTB_HUMANACTBphysical
21044950
HS90B_HUMANHSP90AB1physical
21044950
RECQ4_HUMANRECQL4physical
21044950
ZN790_HUMANZNF790physical
21044950
IF4B_HUMANEIF4Bphysical
21044950
DREB_HUMANDBN1physical
21044950
TBB4B_HUMANTUBB4Bphysical
21044950
DCX_HUMANDCXphysical
21044950
DBNL_HUMANDBNLphysical
21044950
ST1C2_HUMANSULT1C2physical
21044950
ENOG_HUMANENO2physical
21044950
AXA81_HUMANANXA8L1physical
21044950
LDHA_HUMANLDHAphysical
21044950
TRI16_HUMANTRIM16physical
21044950
TOM34_HUMANTOMM34physical
21044950
PGM2_HUMANPGM2physical
21044950
LASP1_HUMANLASP1physical
21044950
PFKAP_HUMANPFKPphysical
21044950
KCRB_HUMANCKBphysical
21044950
TISB_HUMANZFP36L1physical
21044950
NUDC2_HUMANNUDCD2physical
21044950
PAGE2_HUMANPAGE2physical
21044950
SBDS_HUMANSBDSphysical
21044950
G3P_HUMANGAPDHphysical
21044950
AF1L2_HUMANAFAP1L2physical
21044950
POTE1_HUMANPOT1physical
26365187
POTE1_HUMANPOT1physical
28514442
TE2IP_HUMANTERF2IPphysical
28514442
POF1B_HUMANPOF1Bphysical
28514442
UBP7_HUMANUSP7physical
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 ACD_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-111, AND MASSSPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-422; SER-424; SER-425AND SER-435, AND MASS SPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-422 AND SER-425, ANDMASS SPECTROMETRY.

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