MA7D1_HUMAN - dbPTM
MA7D1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MA7D1_HUMAN
UniProt AC Q3KQU3
Protein Name MAP7 domain-containing protein 1
Gene Name MAP7D1
Organism Homo sapiens (Human).
Sequence Length 841
Subcellular Localization Cytoplasm, cytoskeleton, spindle .
Protein Description
Protein Sequence MESGPRAELGAGAPPAVVARTPPEPRPSPEGDPSPPPPPMSALVPDTPPDTPPAMKNATSSKQLPLEPESPSGQVGPRPAPPQEESPSSEAKSRGPTPPAMGPRDARPPRRSSQPSPTAVPASDSPPTKQEVKKAGERHKLAKERREERAKYLAAKKAVWLEKEEKAKALREKQLQERRRRLEEQRLKAEQRRAALEERQRQKLEKNKERYEAAIQRSVKKTWAEIRQQRWSWAGALHHSSPGHKTSGSRCSVSAVNLPKHVDSIINKRLSKSSATLWNSPSRNRSLQLSAWESSIVDRLMTPTLSFLARSRSAVTLPRNGRDQGRGCDPGRGPTWGRAGASLARGPQPDRTHPSAAVPVCPRSASASPLTPCSVTRSVHRCAPAGERGERRKPNAGGSPAPVRRRPEASPVQKKEKKDKERENEKEKSALARERSLKKRQSLPASPRARLSASTASELSPKSKARPSSPSTSWHRPASPCPSPGPGHTLPPKPPSPRGTTASPKGRVRRKEEAKESPSAAGPEDKSQSKRRASNEKESAAPASPAPSPAPSPTPAPPQKEQPPAETPTDAAVLTSPPAPAPPVTPSKPMAGTTDREEATRLLAEKRRQAREQREREEQERRLQAERDKRMREEQLAREAEARAEREAEARRREEQEAREKAQAEQEEQERLQKQKEEAEARSREEAERQRLEREKHFQQQEQERQERRKRLEEIMKRTRKSEVSETKQKQDSKEANANGSSPEPVKAVEARSPGLQKEAVQKEEPIPQEPQWSLPSKELPASLVNGLQPLPAHQENGFSTNGPSGDKSLSRTPETLLPFAEAEAFLKKAVVQSPQVTEVL
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
8 (in isoform 3)Ubiquitination-49.36-
14 (in isoform 3)Phosphorylation-19.2325159151
15 (in isoform 3)Phosphorylation-36.8325159151
21PhosphorylationPPAVVARTPPEPRPS
CCEEEECCCCCCCCC		33.2023927012
28PhosphorylationTPPEPRPSPEGDPSP
CCCCCCCCCCCCCCC		36.5423927012
34PhosphorylationPSPEGDPSPPPPPMS
CCCCCCCCCCCCCCH		55.5725159151
41PhosphorylationSPPPPPMSALVPDTP
CCCCCCCHHCCCCCC		24.9929255136
47PhosphorylationMSALVPDTPPDTPPA
CHHCCCCCCCCCCCH		30.5629255136
51PhosphorylationVPDTPPDTPPAMKNA
CCCCCCCCCCHHCCC		36.6229255136
59PhosphorylationPPAMKNATSSKQLPL
CCHHCCCCCCCCCCC		42.8223312004
60PhosphorylationPAMKNATSSKQLPLE
CHHCCCCCCCCCCCC		32.8823312004
61PhosphorylationAMKNATSSKQLPLEP
HHCCCCCCCCCCCCC		21.7723312004
70PhosphorylationQLPLEPESPSGQVGP
CCCCCCCCCCCCCCC		34.7729255136
72PhosphorylationPLEPESPSGQVGPRP
CCCCCCCCCCCCCCC		51.6529255136
86PhosphorylationPAPPQEESPSSEAKS
CCCCCCCCCCHHHHH		29.3629255136
88PhosphorylationPPQEESPSSEAKSRG
CCCCCCCCHHHHHCC		50.5229255136
89PhosphorylationPQEESPSSEAKSRGP
CCCCCCCHHHHHCCC		44.9829255136
93PhosphorylationSPSSEAKSRGPTPPA
CCCHHHHHCCCCCCC		49.9023927012
97PhosphorylationEAKSRGPTPPAMGPR
HHHHCCCCCCCCCCC		44.7423927012
112PhosphorylationDARPPRRSSQPSPTA
CCCCCCCCCCCCCCC		34.3129255136
113PhosphorylationARPPRRSSQPSPTAV
CCCCCCCCCCCCCCC		44.2829255136
113 (in isoform 3)Phosphorylation-44.2822199227
115 (in isoform 3)Phosphorylation-44.2022199227
116PhosphorylationPRRSSQPSPTAVPAS
CCCCCCCCCCCCCCC		27.5229255136
118PhosphorylationRSSQPSPTAVPASDS
CCCCCCCCCCCCCCC		44.6229255136
122 (in isoform 3)Phosphorylation-21.2622199227
123PhosphorylationSPTAVPASDSPPTKQ
CCCCCCCCCCCCCHH		32.3323927012
124 (in isoform 3)Phosphorylation-68.2325850435
125PhosphorylationTAVPASDSPPTKQEV
CCCCCCCCCCCHHHH		30.2219664994
128PhosphorylationPASDSPPTKQEVKKA
CCCCCCCCHHHHHHH		49.0630266825
130 (in isoform 3)Phosphorylation-64.2925850435
131 (in isoform 3)Phosphorylation-58.8425850435
151AcetylationERREERAKYLAAKKA
HHHHHHHHHHHHHHH		47.2025953088
156AcetylationRAKYLAAKKAVWLEK
HHHHHHHHHHHHHCH		35.3419816235
157AcetylationAKYLAAKKAVWLEKE
HHHHHHHHHHHHCHH		43.3719816243
157UbiquitinationAKYLAAKKAVWLEKE
HHHHHHHHHHHHCHH		43.37-
166AcetylationVWLEKEEKAKALREK
HHHCHHHHHHHHHHH		57.1719816251
211PhosphorylationLEKNKERYEAAIQRS
HHHHHHHHHHHHHHH		15.83-
232PhosphorylationEIRQQRWSWAGALHH
HHHHHHHCHHHHHCC		14.8328176443
240PhosphorylationWAGALHHSSPGHKTS
HHHHHCCCCCCCCCC		27.7228176443
241PhosphorylationAGALHHSSPGHKTSG
HHHHCCCCCCCCCCC		30.4628176443
246PhosphorylationHSSPGHKTSGSRCSV
CCCCCCCCCCCCCEE		32.4223312004
247PhosphorylationSSPGHKTSGSRCSVS
CCCCCCCCCCCCEEE		39.3026434776
249PhosphorylationPGHKTSGSRCSVSAV
CCCCCCCCCCEEEEC		29.8526434776
252PhosphorylationKTSGSRCSVSAVNLP
CCCCCCCEEEECCCC		20.2825159151
254PhosphorylationSGSRCSVSAVNLPKH
CCCCCEEEECCCCHH		15.3725159151
256 (in isoform 3)Phosphorylation-6.1922210691
259 (in isoform 3)Phosphorylation-21.3622210691
260UbiquitinationVSAVNLPKHVDSIIN
EEECCCCHHHHHHHH		60.47-
264PhosphorylationNLPKHVDSIINKRLS
CCCHHHHHHHHHHCC		25.0328857561
268UbiquitinationHVDSIINKRLSKSSA
HHHHHHHHHCCCCCC		44.29-
271PhosphorylationSIINKRLSKSSATLW
HHHHHHCCCCCCCCC		34.2323401153
272UbiquitinationIINKRLSKSSATLWN
HHHHHCCCCCCCCCC		53.6921890473
272 (in isoform 1)Ubiquitination-53.6921890473
272 (in isoform 4)Ubiquitination-53.6921890473
273PhosphorylationINKRLSKSSATLWNS
HHHHCCCCCCCCCCC		23.1023401153
274PhosphorylationNKRLSKSSATLWNSP
HHHCCCCCCCCCCCC		29.0728176443
276PhosphorylationRLSKSSATLWNSPSR
HCCCCCCCCCCCCCC		33.9628176443
277 (in isoform 3)Phosphorylation-4.0025159151
278 (in isoform 3)Phosphorylation-10.0125849741
280PhosphorylationSSATLWNSPSRNRSL
CCCCCCCCCCCCCCC		16.8122167270
282PhosphorylationATLWNSPSRNRSLQL
CCCCCCCCCCCCCCH		41.8422167270
286PhosphorylationNSPSRNRSLQLSAWE
CCCCCCCCCCHHHHH		24.8228464451
290PhosphorylationRNRSLQLSAWESSIV
CCCCCCHHHHHHHHH		20.5528450419
294PhosphorylationLQLSAWESSIVDRLM
CCHHHHHHHHHHHHH		18.0530619164
295PhosphorylationQLSAWESSIVDRLMT
CHHHHHHHHHHHHHC		18.3430619164
302PhosphorylationSIVDRLMTPTLSFLA
HHHHHHHCHHHHHHH		20.0821712546
304PhosphorylationVDRLMTPTLSFLARS
HHHHHCHHHHHHHHC		26.3526434776
306PhosphorylationRLMTPTLSFLARSRS
HHHCHHHHHHHHCCC		22.2328857561
310MethylationPTLSFLARSRSAVTL
HHHHHHHHCCCCEEC		34.45115386781
311PhosphorylationTLSFLARSRSAVTLP
HHHHHHHCCCCEECC		25.6123927012
313PhosphorylationSFLARSRSAVTLPRN
HHHHHCCCCEECCCC		28.4730266825
313 (in isoform 4)Phosphorylation-28.4729507054
316PhosphorylationARSRSAVTLPRNGRD
HHCCCCEECCCCCCC		30.6623927012
316 (in isoform 4)Phosphorylation-30.6629507054
326MethylationRNGRDQGRGCDPGRG
CCCCCCCCCCCCCCC		36.6182955203
332MethylationGRGCDPGRGPTWGRA
CCCCCCCCCCCCCCC		53.99115492383
342PhosphorylationTWGRAGASLARGPQP
CCCCCCHHHCCCCCC		22.9523312004
352PhosphorylationRGPQPDRTHPSAAVP
CCCCCCCCCCCCCCC		45.5828555341
355PhosphorylationQPDRTHPSAAVPVCP
CCCCCCCCCCCCCCC		22.66-
364PhosphorylationAVPVCPRSASASPLT
CCCCCCCCCCCCCCC		16.2422167270
366PhosphorylationPVCPRSASASPLTPC
CCCCCCCCCCCCCCC		30.4422167270
368PhosphorylationCPRSASASPLTPCSV
CCCCCCCCCCCCCCC		20.2522167270
371PhosphorylationSASASPLTPCSVTRS
CCCCCCCCCCCCCCC		26.1527273156
374PhosphorylationASPLTPCSVTRSVHR
CCCCCCCCCCCCHHC		27.9422167270
376PhosphorylationPLTPCSVTRSVHRCA
CCCCCCCCCCHHCCC		10.8423403867
399PhosphorylationRKPNAGGSPAPVRRR
CCCCCCCCCCCCCCC		19.5729255136
410PhosphorylationVRRRPEASPVQKKEK
CCCCCCCCCCCCHHH		24.7623401153
414AcetylationPEASPVQKKEKKDKE
CCCCCCCCHHHHHHH		64.2312656543
415AcetylationEASPVQKKEKKDKER
CCCCCCCHHHHHHHH		58.6412656553
436PhosphorylationSALARERSLKKRQSL
HHHHHHHHHHHHHCC		39.5326074081
439UbiquitinationARERSLKKRQSLPAS
HHHHHHHHHHCCCCC		62.0517370265
442PhosphorylationRSLKKRQSLPASPRA
HHHHHHHCCCCCHHH		40.1123927012
446PhosphorylationKRQSLPASPRARLSA
HHHCCCCCHHHHHCC		16.9929255136
452PhosphorylationASPRARLSASTASEL
CCHHHHHCCCCHHHC		18.0230266825
454PhosphorylationPRARLSASTASELSP
HHHHHCCCCHHHCCC		22.5630266825
455PhosphorylationRARLSASTASELSPK
HHHHCCCCHHHCCCC		33.6430266825
457PhosphorylationRLSASTASELSPKSK
HHCCCCHHHCCCCCC		38.8822167270
460O-linked_GlycosylationASTASELSPKSKARP
CCCHHHCCCCCCCCC		26.6530379171
460PhosphorylationASTASELSPKSKARP
CCCHHHCCCCCCCCC		26.6519664994
462SumoylationTASELSPKSKARPSS
CHHHCCCCCCCCCCC		62.3028112733
463PhosphorylationASELSPKSKARPSSP
HHHCCCCCCCCCCCC		34.6327174698
468PhosphorylationPKSKARPSSPSTSWH
CCCCCCCCCCCCCCC		49.6923927012
469PhosphorylationKSKARPSSPSTSWHR
CCCCCCCCCCCCCCC		26.0823927012
471PhosphorylationKARPSSPSTSWHRPA
CCCCCCCCCCCCCCC		36.7023927012
472PhosphorylationARPSSPSTSWHRPAS
CCCCCCCCCCCCCCC		38.9423927012
473PhosphorylationRPSSPSTSWHRPASP
CCCCCCCCCCCCCCC		25.8123927012
479PhosphorylationTSWHRPASPCPSPGP
CCCCCCCCCCCCCCC		29.7129255136
483PhosphorylationRPASPCPSPGPGHTL
CCCCCCCCCCCCCCC		49.5629255136
489PhosphorylationPSPGPGHTLPPKPPS
CCCCCCCCCCCCCCC		47.0429255136
496PhosphorylationTLPPKPPSPRGTTAS
CCCCCCCCCCCCCCC		35.4429255136
500PhosphorylationKPPSPRGTTASPKGR
CCCCCCCCCCCCCCC		22.0728176443
501PhosphorylationPPSPRGTTASPKGRV
CCCCCCCCCCCCCCC		28.1426699800
503PhosphorylationSPRGTTASPKGRVRR
CCCCCCCCCCCCCCC		25.6726699800
517PhosphorylationRKEEAKESPSAAGPE
CHHHHHCCCCCCCCC		24.3729255136
519PhosphorylationEEAKESPSAAGPEDK
HHHHCCCCCCCCCCH		39.7819691289
529PhosphorylationGPEDKSQSKRRASNE
CCCCHHHHHHHHHCH		34.91-
534PhosphorylationSQSKRRASNEKESAA
HHHHHHHHCHHCCCC		43.6523401153
539PhosphorylationRASNEKESAAPASPA
HHHCHHCCCCCCCCC		40.5829255136
544PhosphorylationKESAAPASPAPSPAP
HCCCCCCCCCCCCCC		22.1229255136
548PhosphorylationAPASPAPSPAPSPTP
CCCCCCCCCCCCCCC		35.4829255136
552PhosphorylationPAPSPAPSPTPAPPQ
CCCCCCCCCCCCCCC		43.4429255136
554PhosphorylationPSPAPSPTPAPPQKE
CCCCCCCCCCCCCCC		36.1029255136
567PhosphorylationKEQPPAETPTDAAVL
CCCCCCCCCCCCCHH		33.3327174698
569PhosphorylationQPPAETPTDAAVLTS
CCCCCCCCCCCHHCC		45.7725159151
575PhosphorylationPTDAAVLTSPPAPAP
CCCCCHHCCCCCCCC		32.3729255136
576PhosphorylationTDAAVLTSPPAPAPP
CCCCHHCCCCCCCCC		25.4029255136
585PhosphorylationPAPAPPVTPSKPMAG
CCCCCCCCCCCCCCC		27.8429255136
587PhosphorylationPAPPVTPSKPMAGTT
CCCCCCCCCCCCCCC		39.7729255136
593PhosphorylationPSKPMAGTTDREEAT
CCCCCCCCCCHHHHH		18.9129255136
594PhosphorylationSKPMAGTTDREEATR
CCCCCCCCCHHHHHH		31.9429255136
600PhosphorylationTTDREEATRLLAEKR
CCCHHHHHHHHHHHH		25.7329978859
682 (in isoform 2)Phosphorylation-27.9622210691
685 (in isoform 2)Phosphorylation-63.9122210691
687 (in isoform 4)Phosphorylation-16.7222210691
690 (in isoform 4)Phosphorylation-45.9022210691
703 (in isoform 2)Phosphorylation-47.0025159151
704 (in isoform 2)Phosphorylation-56.4225849741
708 (in isoform 4)Phosphorylation-40.8725159151
709 (in isoform 4)Phosphorylation-27.9125849741
733PhosphorylationETKQKQDSKEANANG
HHHHHHHHHHHHCCC		29.8720068231
741PhosphorylationKEANANGSSPEPVKA
HHHHCCCCCCCCHHH		42.3923401153
742PhosphorylationEANANGSSPEPVKAV
HHHCCCCCCCCHHHH		34.3829255136
753PhosphorylationVKAVEARSPGLQKEA
HHHHHCCCCCCHHHH		30.3028355574
777PhosphorylationEPQWSLPSKELPASL
CCCCCCCCCCCCHHH		44.0224719451
800PhosphorylationAHQENGFSTNGPSGD
CHHCCCCCCCCCCCC		23.5126074081
801PhosphorylationHQENGFSTNGPSGDK
HHCCCCCCCCCCCCC		41.7726074081
805PhosphorylationGFSTNGPSGDKSLSR
CCCCCCCCCCCCCCC		62.1126074081
809PhosphorylationNGPSGDKSLSRTPET
CCCCCCCCCCCCHHH		36.0025159151
811PhosphorylationPSGDKSLSRTPETLL
CCCCCCCCCCHHHHH		40.9925159151
813PhosphorylationGDKSLSRTPETLLPF
CCCCCCCCHHHHHHH		23.3130278072
816PhosphorylationSLSRTPETLLPFAEA
CCCCCHHHHHHHHHH		34.4925159151
828UbiquitinationAEAEAFLKKAVVQSP
HHHHHHHHHHHHCCC		32.03-
834PhosphorylationLKKAVVQSPQVTEVL
HHHHHHCCCCCCCCC		12.9930266825
838O-linked_GlycosylationVVQSPQVTEVL----
HHCCCCCCCCC----		18.3530379171
838PhosphorylationVVQSPQVTEVL----
HHCCCCCCCCC----		18.3530266825
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 MA7D1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MA7D1_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 MA7D1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
APOA1_HUMANAPOA1physical
16169070
RBM48_HUMANRBM48physical
16169070
GASP1_HUMANGPRASP1physical
16169070
CSN6_HUMANCOPS6physical
16169070
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 MA7D1_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-125; SER-460; SER-544AND SER-548, AND MASS SPECTROMETRY.
"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 SER-72; SER-86; THR-118;SER-460; SER-544; SER-548; SER-552; THR-554 AND SER-834, AND MASSSPECTROMETRY.
"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-41; THR-47; THR-51;SER-86; SER-113; SER-116; SER-125; SER-442; SER-446; SER-460; SER-544;SER-548; SER-552 AND SER-834, AND MASS SPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-460 AND SER-834, ANDMASS 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-302; SER-313; SER-576AND THR-585, AND MASS 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-70; SER-86; SER-88;THR-97; SER-123; SER-125; SER-252; SER-460; SER-753 AND SER-834, ANDMASS SPECTROMETRY.
"Phosphoproteome analysis of the human mitotic spindle.";
Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R.;
Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-460; SER-544; SER-548;SER-552 AND SER-834, AND MASS SPECTROMETRY.
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-460 AND SER-834, ANDMASS SPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-399; SER-544; SER-548;SER-741 AND SER-834, AND MASS SPECTROMETRY.
Ubiquitylation
ReferencePubMed
"Tryptic digestion of ubiquitin standards reveals an improved strategyfor identifying ubiquitinated proteins by mass spectrometry.";
Denis N.J., Vasilescu J., Lambert J.-P., Smith J.C., Figeys D.;
Proteomics 7:868-874(2007).
Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-439, AND MASSSPECTROMETRY.

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