SMAP_HUMAN - dbPTM
SMAP_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SMAP_HUMAN
UniProt AC O00193
Protein Name Small acidic protein
Gene Name SMAP
Organism Homo sapiens (Human).
Sequence Length 183
Subcellular Localization
Protein Description
Protein Sequence MSAARESHPHGVKRSASPDDDLGSSNWEAADLGNEERKQKFLRLMGAGKKEHTGRLVIGDHKSTSHFRTGEEDKKINEELESQYQQSMDSKLSGRYRRHCGLGFSEVEDHDGEGDVAGDDDDDDDDSPDPESPDDSESDSESEKEESAEELQAAEHPDEVEDPKNKKDAKSNYKMMFVKSSGS
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
2Phosphorylation------MSAARESHP
------CCCCHHCCC		30.5425159151
7Phosphorylation-MSAARESHPHGVKR
-CCCCHHCCCCCCCC		36.4430576142
132-HydroxyisobutyrylationESHPHGVKRSASPDD
HCCCCCCCCCCCCCC		45.27-
13SumoylationESHPHGVKRSASPDD
HCCCCCCCCCCCCCC		45.2728112733
14MethylationSHPHGVKRSASPDDD
CCCCCCCCCCCCCCC		34.74115917157
15PhosphorylationHPHGVKRSASPDDDL
CCCCCCCCCCCCCCC		27.6422167270
17PhosphorylationHGVKRSASPDDDLGS
CCCCCCCCCCCCCCC		30.0622167270
18UbiquitinationGVKRSASPDDDLGSS
CCCCCCCCCCCCCCC		49.0921890473
24PhosphorylationSPDDDLGSSNWEAAD
CCCCCCCCCCCHHHH		28.0026846344
25PhosphorylationPDDDLGSSNWEAADL
CCCCCCCCCCHHHHC		44.1326846344
30UbiquitinationGSSNWEAADLGNEER
CCCCCHHHHCCCHHH		10.8822817900
31UbiquitinationSSNWEAADLGNEERK
CCCCHHHHCCCHHHH		63.2621890473
38AcetylationDLGNEERKQKFLRLM
HCCCHHHHHHHHHHH		62.2130592385
47UbiquitinationKFLRLMGAGKKEHTG
HHHHHHCCCCCCCCC		16.8023000965
49UbiquitinationLRLMGAGKKEHTGRL
HHHHCCCCCCCCCCE		55.2224816145
492-HydroxyisobutyrylationLRLMGAGKKEHTGRL
HHHHCCCCCCCCCCE		55.22-
49AcetylationLRLMGAGKKEHTGRL
HHHHCCCCCCCCCCE		55.2225953088
50AcetylationRLMGAGKKEHTGRLV
HHHCCCCCCCCCCEE		54.5318527647
50UbiquitinationRLMGAGKKEHTGRLV
HHHCCCCCCCCCCEE		54.5323503661
53PhosphorylationGAGKKEHTGRLVIGD
CCCCCCCCCCEEECC		25.7028555341
55MethylationGKKEHTGRLVIGDHK
CCCCCCCCEEECCCC		27.26115917161
62SumoylationRLVIGDHKSTSHFRT
CEEECCCCCCCCCCC		61.2328112733
622-HydroxyisobutyrylationRLVIGDHKSTSHFRT
CEEECCCCCCCCCCC		61.23-
62UbiquitinationRLVIGDHKSTSHFRT
CEEECCCCCCCCCCC		61.2323000965
63PhosphorylationLVIGDHKSTSHFRTG
EEECCCCCCCCCCCC		31.5523403867
64PhosphorylationVIGDHKSTSHFRTGE
EECCCCCCCCCCCCH		30.9023186163
65PhosphorylationIGDHKSTSHFRTGEE
ECCCCCCCCCCCCHH		27.9323186163
74AcetylationFRTGEEDKKINEELE
CCCCHHHHHHHHHHH		59.8523749302
74UbiquitinationFRTGEEDKKINEELE
CCCCHHHHHHHHHHH		59.8522817900
75AcetylationRTGEEDKKINEELES
CCCHHHHHHHHHHHH		64.1925953088
75SumoylationRTGEEDKKINEELES
CCCHHHHHHHHHHHH		64.1928112733
75UbiquitinationRTGEEDKKINEELES
CCCHHHHHHHHHHHH		64.1921906983
82PhosphorylationKINEELESQYQQSMD
HHHHHHHHHHHHHHH		46.9721945579
84PhosphorylationNEELESQYQQSMDSK
HHHHHHHHHHHHHHH		20.1421945579
87PhosphorylationLESQYQQSMDSKLSG
HHHHHHHHHHHHHHH		14.7221945579
88SulfoxidationESQYQQSMDSKLSGR
HHHHHHHHHHHHHHH		6.1521406390
90PhosphorylationQYQQSMDSKLSGRYR
HHHHHHHHHHHHHHH		27.1921945579
91UbiquitinationYQQSMDSKLSGRYRR
HHHHHHHHHHHHHHH		42.2723000965
91AcetylationYQQSMDSKLSGRYRR
HHHHHHHHHHHHHHH		42.2723954790
91MalonylationYQQSMDSKLSGRYRR
HHHHHHHHHHHHHHH		42.2726320211
93PhosphorylationQSMDSKLSGRYRRHC
HHHHHHHHHHHHHHC		25.5926074081
96PhosphorylationDSKLSGRYRRHCGLG
HHHHHHHHHHHCCCC		18.6126074081
105PhosphorylationRHCGLGFSEVEDHDG
HHCCCCCEECCCCCC		38.6526074081
126UbiquitinationDDDDDDDDSPDPESP
CCCCCCCCCCCCCCC		69.8923000965
127PhosphorylationDDDDDDDSPDPESPD
CCCCCCCCCCCCCCC		37.8920363803
130UbiquitinationDDDDSPDPESPDDSE
CCCCCCCCCCCCCCC		47.5523000965
132PhosphorylationDDSPDPESPDDSESD
CCCCCCCCCCCCCCC		38.7325137130
135UbiquitinationPDPESPDDSESDSES
CCCCCCCCCCCCCHH		58.6623000965
136PhosphorylationDPESPDDSESDSESE
CCCCCCCCCCCCHHH		46.5125137130
138PhosphorylationESPDDSESDSESEKE
CCCCCCCCCCHHHHH		50.8425137130
140PhosphorylationPDDSESDSESEKEES
CCCCCCCCHHHHHHH		52.9125137130
142PhosphorylationDSESDSESEKEESAE
CCCCCCHHHHHHHHH		58.9025137130
147PhosphorylationSESEKEESAEELQAA
CHHHHHHHHHHHHHC		41.9129255136
170UbiquitinationPKNKKDAKSNYKMMF
CCCHHCCHHCCEEEE		49.7423000965
173PhosphorylationKKDAKSNYKMMFVKS
HHCCHHCCEEEEEEC		13.8327642862
174AcetylationKDAKSNYKMMFVKSS
HCCHHCCEEEEEECC		28.3019608861
174UbiquitinationKDAKSNYKMMFVKSS
HCCHHCCEEEEEECC		28.3023000965
179MethylationNYKMMFVKSSGS---
CCEEEEEECCCC---		27.8619608861
179UbiquitinationNYKMMFVKSSGS---
CCEEEEEECCCC---		27.8623000965
179AcetylationNYKMMFVKSSGS---
CCEEEEEECCCC---		27.8619608861
180PhosphorylationYKMMFVKSSGS----
CEEEEEECCCC----		34.3329214152
181PhosphorylationKMMFVKSSGS-----
EEEEEECCCC-----		37.0229214152
183PhosphorylationMFVKSSGS-------
EEEECCCC-------		38.7124719451
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 SMAP_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SMAP_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 SMAP_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TZAP_HUMANZBTB48physical
21900206
TRA2A_HUMANTRA2Aphysical
21900206
SF3B1_HUMANSF3B1physical
21900206
A2MG_HUMANA2Mphysical
21900206
CE126_HUMANKIAA1377physical
21900206
EF1G_HUMANEEF1Gphysical
21900206
FBN3_HUMANFBN3physical
21900206
RPB3_HUMANPOLR2Cphysical
21900206
SHC1_HUMANSHC1physical
21900206
CTL1_HUMANSLC44A1physical
21900206
RLA1_HUMANRPLP1physical
21900206
SEM5B_HUMANSEMA5Bphysical
21900206
RN19A_HUMANRNF19Aphysical
21900206
SNCAP_HUMANSNCAIPphysical
21900206
MBTP1_HUMANMBTPS1physical
21900206
PTN_HUMANPTNphysical
21900206
BZW2_HUMANBZW2physical
22863883
CHRD1_HUMANCHORDC1physical
22863883
CH60_HUMANHSPD1physical
22863883
KYNU_HUMANKYNUphysical
22863883
LDHA_HUMANLDHAphysical
22863883
SCRN1_HUMANSCRN1physical
22863883
SGT1_HUMANSUGT1physical
22863883
WDR1_HUMANWDR1physical
22863883
HMGN5_HUMANHMGN5physical
26344197
HYPK_HUMANHYPKphysical
26344197
NP1L1_HUMANNAP1L1physical
26344197
PTMA_HUMANPTMAphysical
26344197
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 SMAP_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-174 AND LYS-179, AND MASSSPECTROMETRY.
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-15 AND SER-17, AND MASSSPECTROMETRY.
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15, 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 SER-15; SER-17 AND SER-25,AND MASS SPECTROMETRY.
"Large-scale phosphoproteome analysis of human liver tissue byenrichment and fractionation of phosphopeptides with strong anionexchange chromatography.";
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,Zou H., Gu J.;
Proteomics 8:1346-1361(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15, 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-15 AND SER-17, AND MASSSPECTROMETRY.
"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-17 AND SER-147, 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-15, AND MASSSPECTROMETRY.
"Quantitative phosphoproteome profiling of Wnt3a-mediated signalingnetwork: indicating the involvement of ribonucleoside-diphosphatereductase M2 subunit phosphorylation at residue serine 20 in canonicalWnt signal transduction.";
Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S.,Li S.-J., Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R.;
Mol. Cell. Proteomics 6:1952-1967(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17, AND MASSSPECTROMETRY.
"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-15; SER-17; SER-105;SER-132; SER-136; SER-138; SER-140; SER-142 AND SER-147, AND MASSSPECTROMETRY.
"Quantitative phosphoproteome analysis using a dendrimer conjugationchemistry and tandem mass spectrometry.";
Tao W.A., Wollscheid B., O'Brien R., Eng J.K., Li X.-J.,Bodenmiller B., Watts J.D., Hood L., Aebersold R.;
Nat. Methods 2:591-598(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17, AND MASSSPECTROMETRY.
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells.";
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.;
Nat. Biotechnol. 23:94-101(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-84, AND MASSSPECTROMETRY.

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