SAMD1_HUMAN - dbPTM
SAMD1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SAMD1_HUMAN
UniProt AC Q6SPF0
Protein Name Atherin
Gene Name SAMD1
Organism Homo sapiens (Human).
Sequence Length 538
Subcellular Localization Cytoplasm . Secreted .
Protein Description May play a role in atherogenesis by immobilizing LDL in the atherial wall..
Protein Sequence MAGPPALPPPETAAAATTAAAASSSAASPHYQEWILDTIDSLRSRKARPDLERICRMVRRRHGPEPERTRAELEKLIQQRAVLRVSYKGSISYRNAARVQPPRRGATPPAPPRAPRGAPAAAAAAAPPPTPAPPPPPAPVAAAAPARAPRAAAAAATAPPSPGPAQPGPRAQRAAPLAAPPPAPAAPPAVAPPAGPRRAPPPAVAAREPPLPPPPQPPAPPQQQQPPPPQPQPPPEGGAVRAGGAARPVSLREVVRYLGGSGGAGGRLTRGRVQGLLEEEAAARGRLERTRLGALALPRGDRPGRAPPAASARPSRSKRGGEERVLEKEEEEDDDEDEDEEDDVSEGSEVPESDRPAGAQHHQLNGERGPQSAKERVKEWTPCGPHQGQDEGRGPAPGSGTRQVFSMAAMNKEGGTASVATGPDSPSPVPLPPGKPALPGADGTPFGCPPGRKEKPSDPVEWTVMDVVEYFTEAGFPEQATAFQEQEIDGKSLLLMQRTDVLTGLSIRLGPALKIYEHHIKVLQQGHFEDDDPDGFLG
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
12PhosphorylationPALPPPETAAAATTA
CCCCCHHHHHHHHHH		27.6322210691
17PhosphorylationPETAAAATTAAAASS
HHHHHHHHHHHHHHH		16.5522210691
18PhosphorylationETAAAATTAAAASSS
HHHHHHHHHHHHHHC		15.0122210691
23PhosphorylationATTAAAASSSAASPH
HHHHHHHHHCCCCHH		21.7928464451
24PhosphorylationTTAAAASSSAASPHY
HHHHHHHHCCCCHHH		21.1928348404
25PhosphorylationTAAAASSSAASPHYQ
HHHHHHHCCCCHHHH		25.9228348404
28PhosphorylationAASSSAASPHYQEWI
HHHHCCCCHHHHHHH		16.3625159151
31PhosphorylationSSAASPHYQEWILDT
HCCCCHHHHHHHHHH		16.12-
46SumoylationIDSLRSRKARPDLER
HHHHHHHCCCCCHHH		50.42-
46SumoylationIDSLRSRKARPDLER
HHHHHHHCCCCCHHH		50.42-
75UbiquitinationRTRAELEKLIQQRAV
HHHHHHHHHHHHHCC		64.61-
86PhosphorylationQRAVLRVSYKGSISY
HHCCCEEEECCCEEE		18.0723186163
87PhosphorylationRAVLRVSYKGSISYR
HCCCEEEECCCEEEE		19.26-
88AcetylationAVLRVSYKGSISYRN
CCCEEEECCCEEEEC		38.3825953088
88UbiquitinationAVLRVSYKGSISYRN
CCCEEEECCCEEEEC		38.38-
88MethylationAVLRVSYKGSISYRN
CCCEEEECCCEEEEC		38.38115977517
90PhosphorylationLRVSYKGSISYRNAA
CEEEECCCEEEECCC		12.28-
92PhosphorylationVSYKGSISYRNAARV
EEECCCEEEECCCCC		21.53-
93PhosphorylationSYKGSISYRNAARVQ
EECCCEEEECCCCCC		13.25-
104MethylationARVQPPRRGATPPAP
CCCCCCCCCCCCCCC		44.8954559047
107PhosphorylationQPPRRGATPPAPPRA
CCCCCCCCCCCCCCC		32.4023927012
116MethylationPAPPRAPRGAPAAAA
CCCCCCCCCCCCHHH		53.58115493235
130PhosphorylationAAAAPPPTPAPPPPP
HHCCCCCCCCCCCCC		37.5423312004
144PhosphorylationPAPVAAAAPARAPRA
CCCCHHCCCCCCHHH		8.11-
151PhosphorylationAPARAPRAAAAAATA
CCCCCHHHHHHHHCC		10.61-
155PhosphorylationAPRAAAAAATAPPSP
CHHHHHHHHCCCCCC		10.7120068231
157PhosphorylationRAAAAAATAPPSPGP
HHHHHHHCCCCCCCC		34.6630278072
161PhosphorylationAAATAPPSPGPAQPG
HHHCCCCCCCCCCCC		41.2429255136
166MethylationPPSPGPAQPGPRAQR
CCCCCCCCCCCHHCC		46.76-
170MethylationGPAQPGPRAQRAAPL
CCCCCCCHHCCCCCC		49.63115493229
178MethylationAQRAAPLAAPPPAPA
HCCCCCCCCCCCCCC		19.50-
180MethylationRAAPLAAPPPAPAAP
CCCCCCCCCCCCCCC		29.78-
185MethylationAAPPPAPAAPPAVAP
CCCCCCCCCCCCCCC		34.41-
197MethylationVAPPAGPRRAPPPAV
CCCCCCCCCCCCCCC		46.61115387211
209PhosphorylationPAVAAREPPLPPPPQ
CCCCCCCCCCCCCCC		30.1219007248
239PhosphorylationQPPPEGGAVRAGGAA
CCCCCCCCCCCCCCC		9.8519007248
242PhosphorylationPEGGAVRAGGAARPV
CCCCCCCCCCCCCCC		17.74-
250PhosphorylationGGAARPVSLREVVRY
CCCCCCCCHHHHHHH		25.1323186163
257PhosphorylationSLREVVRYLGGSGGA
CHHHHHHHHCCCCCC		9.7024732914
261PhosphorylationVVRYLGGSGGAGGRL
HHHHHCCCCCCCCCC		32.0526055452
272UbiquitinationGGRLTRGRVQGLLEE
CCCCCHHHHHHHHHH		17.81-
272MethylationGGRLTRGRVQGLLEE
CCCCCHHHHHHHHHH		17.81115493241
275PhosphorylationLTRGRVQGLLEEEAA
CCHHHHHHHHHHHHH		29.40-
284MethylationLEEEAAARGRLERTR
HHHHHHHCCCCCHHH		26.4954559041
286MethylationEEAAARGRLERTRLG
HHHHHCCCCCHHHCC		28.02115493247
291MethylationRGRLERTRLGALALP
CCCCCHHHCCEEECC		37.0354559059
310PhosphorylationPGRAPPAASARPSRS
CCCCCCCHHCCCCCC		14.97-
315PhosphorylationPAASARPSRSKRGGE
CCHHCCCCCCCCCCC		43.5719007248
319PhosphorylationARPSRSKRGGEERVL
CCCCCCCCCCCCCCC		60.64-
321PhosphorylationPSRSKRGGEERVLEK
CCCCCCCCCCCCCCH		37.31-
329UbiquitinationEERVLEKEEEEDDDE
CCCCCCHHHHCCCCC		62.35-
338PhosphorylationEEDDDEDEDEEDDVS
HCCCCCCCCCCCCCC		66.3320068231
345PhosphorylationEDEEDDVSEGSEVPE
CCCCCCCCCCCCCCH		43.1429496963
348PhosphorylationEDDVSEGSEVPESDR
CCCCCCCCCCCHHCC		31.2230576142
353PhosphorylationEGSEVPESDRPAGAQ
CCCCCCHHCCCCCHH		32.6121406692
372PhosphorylationNGERGPQSAKERVKE
CCCCCCHHHHHHHHH		44.4321406692
378UbiquitinationQSAKERVKEWTPCGP
HHHHHHHHHCCCCCC		54.4729967540
381PhosphorylationKERVKEWTPCGPHQG
HHHHHHCCCCCCCCC		15.1424732914
385SumoylationKEWTPCGPHQGQDEG
HHCCCCCCCCCCCCC		24.28-
399PhosphorylationGRGPAPGSGTRQVFS
CCCCCCCCCHHHHEE		35.6124732914
401PhosphorylationGPAPGSGTRQVFSMA
CCCCCCCHHHHEEEE		21.4524732914
408UbiquitinationTRQVFSMAAMNKEGG
HHHHEEEEEECCCCC		11.45-
415UbiquitinationAAMNKEGGTASVATG
EEECCCCCEEEEECC		21.14-
416PhosphorylationAMNKEGGTASVATGP
EECCCCCEEEEECCC		26.9829255136
418PhosphorylationNKEGGTASVATGPDS
CCCCCEEEEECCCCC		16.4823401153
421PhosphorylationGGTASVATGPDSPSP
CCEEEEECCCCCCCC		47.2829255136
425PhosphorylationSVATGPDSPSPVPLP
EEECCCCCCCCCCCC		30.3423401153
427PhosphorylationATGPDSPSPVPLPPG
ECCCCCCCCCCCCCC		42.3423401153
435UbiquitinationPVPLPPGKPALPGAD
CCCCCCCCCCCCCCC		32.6529967540
444PhosphorylationALPGADGTPFGCPPG
CCCCCCCCCCCCCCC		18.9125159151
514UbiquitinationIRLGPALKIYEHHIK
CCCCHHHHHHHHHHH		45.40-
516PhosphorylationLGPALKIYEHHIKVL
CCHHHHHHHHHHHHH		13.9729496907
521UbiquitinationKIYEHHIKVLQQGHF
HHHHHHHHHHHCCCC		32.32-
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 SAMD1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SAMD1_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 SAMD1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
XIAP_HUMANXIAPphysical
26496610
CLCN7_HUMANCLCN7physical
26496610
DSG1_HUMANDSG1physical
26496610
ECT2_HUMANECT2physical
26496610
NDUB5_HUMANNDUFB5physical
26496610
RENT1_HUMANUPF1physical
26496610
SDCB1_HUMANSDCBPphysical
26496610
TLN1_HUMANTLN1physical
26496610
CIP4_HUMANTRIP10physical
26496610
TRI14_HUMANTRIM14physical
26496610
PDCD6_HUMANPDCD6physical
26496610
CDIPT_HUMANCDIPTphysical
26496610
PUM2_HUMANPUM2physical
26496610
HIG1A_HUMANHIGD1Aphysical
26496610
MYOF_HUMANMYOFphysical
26496610
PCF11_HUMANPCF11physical
26496610
IWS1_HUMANIWS1physical
26496610
KI18A_HUMANKIF18Aphysical
26496610
USMG5_HUMANUSMG5physical
26496610
PP4P1_HUMANTMEM55Bphysical
26496610
R3HC1_HUMANR3HCC1physical
26496610
REEP3_HUMANREEP3physical
26496610
NSE2_HUMANNSMCE2physical
26496610
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 SAMD1_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 THR-107 AND SER-161, ANDMASS 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-161, 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 THR-107; SER-161 ANDSER-261, 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-161, AND MASSSPECTROMETRY.
"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 SER-161, AND MASSSPECTROMETRY.
"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 THR-107; SER-161; SER-315AND SER-345, AND MASS 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-161, AND MASSSPECTROMETRY.

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