SIN1_HUMAN - dbPTM
SIN1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SIN1_HUMAN
UniProt AC Q9BPZ7
Protein Name Target of rapamycin complex 2 subunit MAPKAP1
Gene Name MAPKAP1
Organism Homo sapiens (Human).
Sequence Length 522
Subcellular Localization Cell membrane
Peripheral membrane protein. Cytoplasmic vesicle. Nucleus.
Protein Description Subunit of mTORC2, which regulates cell growth and survival in response to hormonal signals. mTORC2 is activated by growth factors, but, in contrast to mTORC1, seems to be nutrient-insensitive. mTORC2 seems to function upstream of Rho GTPases to regulate the actin cytoskeleton, probably by activating one or more Rho-type guanine nucleotide exchange factors. mTORC2 promotes the serum-induced formation of stress-fibers or F-actin. mTORC2 plays a critical role in AKT1 'Ser-473' phosphorylation, which may facilitate the phosphorylation of the activation loop of AKT1 on 'Thr-308' by PDK1 which is a prerequisite for full activation. mTORC2 regulates the phosphorylation of SGK1 at 'Ser-422'. mTORC2 also modulates the phosphorylation of PRKCA on 'Ser-657'. Within mTORC2, MAPKAP1 is required for complex formation and mTORC2 kinase activity. MAPKAP1 inhibits MAP3K2 by preventing its dimerization and autophosphorylation. Inhibits HRAS and KRAS signaling. Enhances osmotic stress-induced phosphorylation of ATF2 and ATF2-mediated transcription. Involved in ciliogenesis, regulates cilia length through its interaction with CCDC28B independently of mTORC2 complex..
Protein Sequence MAFLDNPTIILAHIRQSHVTSDDTGMCEMVLIDHDVDLEKIHPPSMPGDSGSEIQGSNGETQGYVYAQSVDITSSWDFGIRRRSNTAQRLERLRKERQNQIKCKNIQWKERNSKQSAQELKSLFEKKSLKEKPPISGKQSILSVRLEQCPLQLNNPFNEYSKFDGKGHVGTTATKKIDVYLPLHSSQDRLLPMTVVTMASARVQDLIGLICWQYTSEGREPKLNDNVSAYCLHIAEDDGEVDTDFPPLDSNEPIHKFGFSTLALVEKYSSPGLTSKESLFVRINAAHGFSLIQVDNTKVTMKEILLKAVKRRKGSQKVSGPQYRLEKQSEPNVAVDLDSTLESQSAWEFCLVRENSSRADGVFEEDSQIDIATVQDMLSSHHYKSFKVSMIHRLRFTTDVQLGISGDKVEIDPVTNQKASTKFWIKQKPISIDSDLLCACDLAEEKSPSHAIFKLTYLSNHDYKHLYFESDAATVNEIVLKVNYILESRASTARADYFAQKQRKLNRRTSFSFQKEKKSGQQ
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
2Acetylation------MAFLDNPTI
------CCCCCCCEE		17.45-
84PhosphorylationDFGIRRRSNTAQRLE
HHCCCCCCCHHHHHH		36.4022817900
86PhosphorylationGIRRRSNTAQRLERL
CCCCCCCHHHHHHHH		25.9722817900
113O-linked_GlycosylationIQWKERNSKQSAQEL
CCHHHHCCHHHHHHH		37.9930379171
116O-linked_GlycosylationKERNSKQSAQELKSL
HHHCCHHHHHHHHHH		35.3430379171
121UbiquitinationKQSAQELKSLFEKKS
HHHHHHHHHHHHHHC		44.34-
128PhosphorylationKSLFEKKSLKEKPPI
HHHHHHHCCCCCCCC		56.60-
140PhosphorylationPPISGKQSILSVRLE
CCCCCCCEEEEEEEE		29.0520873877
143PhosphorylationSGKQSILSVRLEQCP
CCCCEEEEEEEECCC		11.9720873877
160PhosphorylationLNNPFNEYSKFDGKG
CCCCCCCCCCCCCCC		20.4723090842
161PhosphorylationNNPFNEYSKFDGKGH
CCCCCCCCCCCCCCC		22.2223090842
162UbiquitinationNPFNEYSKFDGKGHV
CCCCCCCCCCCCCCC		46.72-
166UbiquitinationEYSKFDGKGHVGTTA
CCCCCCCCCCCCCCC		47.92-
180PhosphorylationATKKIDVYLPLHSSQ
CCCEEEEEEECCCCC		10.0023403867
185PhosphorylationDVYLPLHSSQDRLLP
EEEEECCCCCCCCCC		37.0623911959
186PhosphorylationVYLPLHSSQDRLLPM
EEEECCCCCCCCCCC		25.9223911959
194PhosphorylationQDRLLPMTVVTMASA
CCCCCCCCHHHHHHH		15.1924043423
197PhosphorylationLLPMTVVTMASARVQ
CCCCCHHHHHHHHHH		11.5924043423
200PhosphorylationMTVVTMASARVQDLI
CCHHHHHHHHHHHHH		13.0424043423
214PhosphorylationIGLICWQYTSEGREP
HHHHHEEECCCCCCC		6.4224043423
215PhosphorylationGLICWQYTSEGREPK
HHHHEEECCCCCCCC		12.7624043423
216PhosphorylationLICWQYTSEGREPKL
HHHEEECCCCCCCCC		32.8724043423
260PhosphorylationPIHKFGFSTLALVEK
CHHHCCCCHHHHHHH		23.9228857561
261PhosphorylationIHKFGFSTLALVEKY
HHHCCCCHHHHHHHC		17.4928270605
268PhosphorylationTLALVEKYSSPGLTS
HHHHHHHCCCCCCCC		10.8128270605
269PhosphorylationLALVEKYSSPGLTSK
HHHHHHCCCCCCCCC		40.9226657352
270PhosphorylationALVEKYSSPGLTSKE
HHHHHCCCCCCCCCC		21.6425159151
274PhosphorylationKYSSPGLTSKESLFV
HCCCCCCCCCCEEEE		43.6028270605
275PhosphorylationYSSPGLTSKESLFVR
CCCCCCCCCCEEEEE		39.2028270605
276UbiquitinationSSPGLTSKESLFVRI
CCCCCCCCCEEEEEE		46.19-
302UbiquitinationDNTKVTMKEILLKAV
CCCEEEHHHHHHHHH		32.03-
315PhosphorylationAVKRRKGSQKVSGPQ
HHHHCCCCCCCCCCC		29.8423312004
319PhosphorylationRKGSQKVSGPQYRLE
CCCCCCCCCCCHHCC		52.3623401153
323PhosphorylationQKVSGPQYRLEKQSE
CCCCCCCHHCCCCCC		21.9423312004
367PhosphorylationDGVFEEDSQIDIATV
CCCCCCCCCCEEEHH		32.1128348404
428UbiquitinationTKFWIKQKPISIDSD
CEEEECCCCCCCCHH		39.04-
447PhosphorylationCDLAEEKSPSHAIFK
HHHCCCCCCCCCEEE		34.6125159151
449PhosphorylationLAEEKSPSHAIFKLT
HCCCCCCCCCEEEEE		32.4225159151
456PhosphorylationSHAIFKLTYLSNHDY
CCCEEEEEEECCCCC		24.0225954137
457PhosphorylationHAIFKLTYLSNHDYK
CCEEEEEEECCCCCC		20.6925954137
459PhosphorylationIFKLTYLSNHDYKHL
EEEEEEECCCCCCEE		23.0025159151
463PhosphorylationTYLSNHDYKHLYFES
EEECCCCCCEEEEEC		7.8625954137
467PhosphorylationNHDYKHLYFESDAAT
CCCCCEEEEECCCCC		12.6725954137
470PhosphorylationYKHLYFESDAATVNE
CCEEEEECCCCCHHH		23.7325954137
497PhosphorylationASTARADYFAQKQRK
HCHHHHHHHHHHHHH		10.38-
501UbiquitinationRADYFAQKQRKLNRR
HHHHHHHHHHHHHCC		48.95-
509PhosphorylationQRKLNRRTSFSFQKE
HHHHHCCCCCCCCHH		30.7730266825
510PhosphorylationRKLNRRTSFSFQKEK
HHHHCCCCCCCCHHH		19.6529255136
512PhosphorylationLNRRTSFSFQKEKKS
HHCCCCCCCCHHHHC		26.9130266825
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
86TPhosphorylationKinaseAKT1P31749
PSP
128SPhosphorylationKinasePKCAP17252
PSP
260SPhosphorylationKinaseMTORP42345
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SIN1_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 SIN1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
AKT1_HUMANAKT1physical
16962653
MTOR_HUMANMTORphysical
17043309
MTOR_HUMANMTORphysical
16962653
RICTR_HUMANRICTORphysical
17043309
RICTR_HUMANRICTORphysical
16962653
PRR5_HUMANPRR5physical
17461779
MTOR_HUMANMTORphysical
17461779
RICTR_HUMANRICTORphysical
17461779
RICTR_HUMANRICTORphysical
20832730
RL23_HUMANRPL23physical
21045808
RS6_HUMANRPS6physical
21045808
MTOR_HUMANMTORphysical
21045808
RICTR_HUMANRICTORphysical
21045808
KS6B1_HUMANRPS6KB1physical
17043309
KPCA_HUMANPRKCAphysical
18566587
AKT1_HUMANAKT1physical
21177249
MTOR_HUMANMTORphysical
21177249
RICTR_HUMANRICTORphysical
21177249
PINK1_HUMANPINK1physical
21177249
MTOR_HUMANMTORphysical
19875983
RICTR_HUMANRICTORphysical
19875983
STK38_HUMANSTK38physical
19875983
MK08_HUMANMAPK8physical
15722200
MTOR_HUMANMTORphysical
18566586
RICTR_HUMANRICTORphysical
18566586
AKT1_HUMANAKT1physical
18566586
NBN_HUMANNBNphysical
23762398
KCTD3_HUMANKCTD3physical
27173435
KI13B_HUMANKIF13Bphysical
27173435
ZBT21_HUMANZBTB21physical
27173435
GGYF1_HUMANGIGYF1physical
27173435
LRFN1_HUMANLRFN1physical
27173435
DEN1A_HUMANDENND1Aphysical
27173435
SRGP2_HUMANSRGAP2physical
27173435
SI1L1_HUMANSIPA1L1physical
27173435
LIMA1_HUMANLIMA1physical
27173435
MAGI1_HUMANMAGI1physical
27173435
TESK2_HUMANTESK2physical
27173435
DCLK1_HUMANDCLK1physical
27173435
MAST3_HUMANMAST3physical
27173435
ZN638_HUMANZNF638physical
27173435
CING_HUMANCGNphysical
27173435
SRS12_HUMANSRSF12physical
27173435
SYDE1_HUMANSYDE1physical
27173435
AGAP1_HUMANAGAP1physical
27173435
MPIP2_HUMANCDC25Bphysical
27173435
CDK16_HUMANCDK16physical
27173435
F110B_HUMANFAM110Bphysical
27173435
UBP21_HUMANUSP21physical
27173435
FA53C_HUMANFAM53Cphysical
27173435
AN34A_HUMANANKRD34Aphysical
27173435
HDAC4_HUMANHDAC4physical
27173435
F110A_HUMANFAM110Aphysical
27173435
NF1_HUMANNF1physical
27173435
CBY1_HUMANCBY1physical
27173435
NADK_HUMANNADKphysical
27173435
LPIN3_HUMANLPIN3physical
27173435
TIAM1_HUMANTIAM1physical
27173435
M3K21_HUMANKIAA1804physical
27173435
NGAP_HUMANRASAL2physical
27173435
TBC25_HUMANTBC1D25physical
27173435
MPIP3_HUMANCDC25Cphysical
27173435
CAMP2_HUMANCAMSAP2physical
27173435
GGYF2_HUMANGIGYF2physical
27173435
PKHA7_HUMANPLEKHA7physical
27173435
MELK_HUMANMELKphysical
27173435
KIF1C_HUMANKIF1Cphysical
27173435
NAV1_HUMANNAV1physical
27173435
INP5E_HUMANINPP5Ephysical
27173435
RAB3I_HUMANRAB3IPphysical
27173435
AKT1_HUMANAKT1physical
28264193
KPCA_HUMANPRKCAphysical
28264193
SGK1_HUMANSGK1physical
28264193
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 SIN1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-510, 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-510, 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-270 AND SER-510, 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-510, AND MASSSPECTROMETRY.

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