AT11C_HUMAN - dbPTM
AT11C_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID AT11C_HUMAN
UniProt AC Q8NB49
Protein Name Phospholipid-transporting ATPase IG
Gene Name ATP11C
Organism Homo sapiens (Human).
Sequence Length 1132
Subcellular Localization Cell membrane
Multi-pass membrane protein . Endoplasmic reticulum membrane . Efficient exit from the endoplasmic reticulum requires the presence of TMEM30A. Some cell membrane localization observed in the presence of TMEM30B.
Protein Description Catalytic component of a P4-ATPase flippase complex which catalyzes the hydrolysis of ATP coupled to the transport of aminophospholipids from the outer to the inner leaflet of various membranes and ensures the maintenance of asymmetric distribution of phospholipids. Phospholipid translocation seems also to be implicated in vesicle formation and in uptake of lipid signaling molecules. Required for B cell differentiation past the pro-B cell stage. Seems to mediate phosphatidylserine (PS) flipping in pro-B cells. May be involved in the transport of cholestatic bile acids (By similarity)..
Protein Sequence MQMVPSLPPASECAGEEKRVGTRTVFVGNHPVSETEAYIAQRFCDNRIVSSKYTLWNFLPKNLFEQFRRIANFYFLIIFLVQVTVDTPTSPVTSGLPLFFVITVTAIKQGYEDCLRHRADNEVNKSTVYIIENAKRVRKESEKIKVGDVVEVQADETFPCDLILLSSCTTDGTCYVTTASLDGESNCKTHYAVRDTIALCTAESIDTLRAAIECEQPQPDLYKFVGRINIYSNSLEAVARSLGPENLLLKGATLKNTEKIYGVAVYTGMETKMALNYQGKSQKRSAVEKSINAFLIVYLFILLTKAAVCTTLKYVWQSTPYNDEPWYNQKTQKERETLKVLKMFTDFLSFMVLFNFIIPVSMYVTVEMQKFLGSFFISWDKDFYDEEINEGALVNTSDLNEELGQVDYVFTDKTGTLTENSMEFIECCIDGHKYKGVTQEVDGLSQTDGTLTYFDKVDKNREELFLRALCLCHTVEIKTNDAVDGATESAELTYISSSPDEIALVKGAKRYGFTFLGNRNGYMRVENQRKEIEEYELLHTLNFDAVRRRMSVIVKTQEGDILLFCKGADSAVFPRVQNHEIELTKVHVERNAMDGYRTLCVAFKEIAPDDYERINRQLIEAKMALQDREEKMEKVFDDIETNMNLIGATAVEDKLQDQAAETIEALHAAGLKVWVLTGDKMETAKSTCYACRLFQTNTELLELTTKTIEESERKEDRLHELLIEYRKKLLHEFPKSTRSFKKAWTEHQEYGLIIDGSTLSLILNSSQDSSSNNYKSIFLQICMKCTAVLCCRMAPLQKAQIVRMVKNLKGSPITLSIGDGANDVSMILESHVGIGIKGKEGRQAARNSDYSVPKFKHLKKLLLAHGHLYYVRIAHLVQYFFYKNLCFILPQFLYQFFCGFSQQPLYDAAYLTMYNICFTSLPILAYSLLEQHINIDTLTSDPRLYMKISGNAMLQLGPFLYWTFLAAFEGTVFFFGTYFLFQTASLEENGKVYGNWTFGTIVFTVLVFTVTLKLALDTRFWTWINHFVIWGSLAFYVFFSFFWGGIIWPFLKQQRMYFVFAQMLSSVSTWLAIILLIFISLFPEILLIVLKNVRRRSARRNLSCRRASDSLSARPSVRPLLLRTFSDESNVL
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
38PhosphorylationPVSETEAYIAQRFCD
CCCHHHHHHHHHHCC		7.20-
129PhosphorylationEVNKSTVYIIENAKR
CCCHHHEEEECCHHH		9.03-
135UbiquitinationVYIIENAKRVRKESE
EEEECCHHHHHHHCC		64.11-
188UbiquitinationLDGESNCKTHYAVRD
CCCCCCCCCCHHHHH		42.4622817900
191UbiquitinationESNCKTHYAVRDTIA
CCCCCCCHHHHHHHH		16.4222817900
231PhosphorylationFVGRINIYSNSLEAV
HHHHEECCCCCHHHH		9.4130108239
232PhosphorylationVGRINIYSNSLEAVA
HHHEECCCCCHHHHH		19.0230108239
234PhosphorylationRINIYSNSLEAVARS
HEECCCCCHHHHHHH		22.9630108239
241PhosphorylationSLEAVARSLGPENLL
CHHHHHHHHCHHHEE		28.1322210691
247UbiquitinationRSLGPENLLLKGATL
HHHCHHHEEEECCCC		5.8932015554
250UbiquitinationGPENLLLKGATLKNT
CHHHEEEECCCCCCC		46.6032015554
252UbiquitinationENLLLKGATLKNTEK
HHEEEECCCCCCCCC		14.2622817900
253PhosphorylationNLLLKGATLKNTEKI
HEEEECCCCCCCCCE		47.1122210691
2552-HydroxyisobutyrylationLLKGATLKNTEKIYG
EEECCCCCCCCCEEE		58.42-
255UbiquitinationLLKGATLKNTEKIYG
EEECCCCCCCCCEEE		58.4222817900
257PhosphorylationKGATLKNTEKIYGVA
ECCCCCCCCCEEEEE		36.7522210691
261PhosphorylationLKNTEKIYGVAVYTG
CCCCCCEEEEEEEEC		19.3322817900
267PhosphorylationIYGVAVYTGMETKMA
EEEEEEEECCHHHHH		24.3722210691
277PhosphorylationETKMALNYQGKSQKR
HHHHHHCCCCCCHHH		21.3530387612
280UbiquitinationMALNYQGKSQKRSAV
HHHCCCCCCHHHHHH		33.90-
317UbiquitinationTTLKYVWQSTPYNDE
HHHHHHHHCCCCCCC		27.6421963094
330UbiquitinationDEPWYNQKTQKERET
CCCCCCCCCHHHHHH		49.65-
345PhosphorylationLKVLKMFTDFLSFMV
HHHHHHHHHHHHHHH		23.4920068231
349PhosphorylationKMFTDFLSFMVLFNF
HHHHHHHHHHHHHHH		15.9920068231
361PhosphorylationFNFIIPVSMYVTVEM
HHHHCCHHHHHHHHH		10.0720068231
363PhosphorylationFIIPVSMYVTVEMQK
HHCCHHHHHHHHHHH		5.8620068231
365PhosphorylationIPVSMYVTVEMQKFL
CCHHHHHHHHHHHHH		8.0220068231
381UbiquitinationSFFISWDKDFYDEEI
HHCCCCCCCCCCCHH		43.4021963094
430UbiquitinationEFIECCIDGHKYKGV
HHHHHHCCCCCCCCC		38.9532015554
433UbiquitinationECCIDGHKYKGVTQE
HHHCCCCCCCCCEEE		54.9432015554
434PhosphorylationCCIDGHKYKGVTQEV
HHCCCCCCCCCEEEE		13.80-
435UbiquitinationCIDGHKYKGVTQEVD
HCCCCCCCCCEEEEC		52.27-
438PhosphorylationGHKYKGVTQEVDGLS
CCCCCCCEEEECCCC		27.9028176443
442PhosphorylationKGVTQEVDGLSQTDG
CCCEEEECCCCCCCC		52.1132142685
445PhosphorylationTQEVDGLSQTDGTLT
EEEECCCCCCCCCEE		36.2419664994
447PhosphorylationEVDGLSQTDGTLTYF
EECCCCCCCCCEEEE		32.7830278072
450PhosphorylationGLSQTDGTLTYFDKV
CCCCCCCCEEEECCC		20.8028176443
452PhosphorylationSQTDGTLTYFDKVDK
CCCCCCEEEECCCCC		23.2128176443
453PhosphorylationQTDGTLTYFDKVDKN
CCCCCEEEECCCCCC		16.9428176443
453UbiquitinationQTDGTLTYFDKVDKN
CCCCCEEEECCCCCC		16.9422817900
456 (in isoform 3)Ubiquitination-42.2921906983
456 (in isoform 2)Ubiquitination-42.2921906983
456 (in isoform 1)Ubiquitination-42.2921906983
456 (in isoform 4)Ubiquitination-42.2921906983
456UbiquitinationGTLTYFDKVDKNREE
CCEEEECCCCCCHHH		42.2922817900
459UbiquitinationTYFDKVDKNREELFL
EEECCCCCCHHHHHH		61.9722817900
467UbiquitinationNREELFLRALCLCHT
CHHHHHHHHHHHHHE		20.4122817900
470UbiquitinationELFLRALCLCHTVEI
HHHHHHHHHHHEEEE		3.5822817900
473UbiquitinationLRALCLCHTVEIKTN
HHHHHHHHEEEEECC		21.7222817900
476UbiquitinationLCLCHTVEIKTNDAV
HHHHHEEEEECCCCC		39.6722817900
479UbiquitinationCHTVEIKTNDAVDGA
HHEEEEECCCCCCCC		43.9522817900
506UbiquitinationPDEIALVKGAKRYGF
CCEEEEEECCHHCCC		54.74-
540PhosphorylationEEYELLHTLNFDAVR
HHHHHHHHCCHHHHH		24.3024719451
566UbiquitinationGDILLFCKGADSAVF
CCEEEEECCCCCCCC		50.20-
570PhosphorylationLFCKGADSAVFPRVQ
EEECCCCCCCCCCHH		26.2927067055
581UbiquitinationPRVQNHEIELTKVHV
CCHHCCEEEEEEEEE		4.0121963094
582UbiquitinationRVQNHEIELTKVHVE
CHHCCEEEEEEEEEE		47.6121963094
585UbiquitinationNHEIELTKVHVERNA
CCEEEEEEEEEECCC		42.8621963094
596UbiquitinationERNAMDGYRTLCVAF
ECCCCCCHHHHHHHH		9.0021963094
602UbiquitinationGYRTLCVAFKEIAPD
CHHHHHHHHHHHCCC		14.5921963094
604UbiquitinationRTLCVAFKEIAPDDY
HHHHHHHHHHCCCCH		38.17-
605UbiquitinationTLCVAFKEIAPDDYE
HHHHHHHHHCCCCHH		37.6221963094
622UbiquitinationNRQLIEAKMALQDRE
HHHHHHHHHHHCCHH		16.35-
654UbiquitinationGATAVEDKLQDQAAE
CHHHHHHHHHHHHHH		34.24-
6802-HydroxyisobutyrylationVWVLTGDKMETAKST
EEEEECCCHHHHHHH		39.72-
706UbiquitinationELLELTTKTIEESER
HHHHHHHHCHHHHHH		42.12-
736PhosphorylationLLHEFPKSTRSFKKA
HHHHCCCCCCHHHHH		29.3223312004
737PhosphorylationLHEFPKSTRSFKKAW
HHHCCCCCCHHHHHH		36.1426546556
739PhosphorylationEFPKSTRSFKKAWTE
HCCCCCCHHHHHHHH		41.32-
854UbiquitinationNSDYSVPKFKHLKKL
CCCCCCCCHHHHHHH		65.96-
977PhosphorylationGTVFFFGTYFLFQTA
CCEEEECEEEEEEEE		13.1225332170
1097PhosphorylationLKNVRRRSARRNLSC
HHHHHHHHHHHCCCC		25.0627282143
1108PhosphorylationNLSCRRASDSLSARP
CCCCCCCCCCCCCCC		26.3930266825
1110PhosphorylationSCRRASDSLSARPSV
CCCCCCCCCCCCCCC		23.0230266825
1112PhosphorylationRRASDSLSARPSVRP
CCCCCCCCCCCCCHH		26.6130266825
1116PhosphorylationDSLSARPSVRPLLLR
CCCCCCCCCHHHHEE		25.7923898821
1124PhosphorylationVRPLLLRTFSDESNV
CHHHHEEECCCCCCC		27.7130266825
1126PhosphorylationPLLLRTFSDESNVL-
HHHEEECCCCCCCC-		39.6030266825
1129PhosphorylationLRTFSDESNVL----
EEECCCCCCCC----		36.9130266825
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

Oops, there are no upstream regulatory protein records of AT11C_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
1116SPhosphorylation

23186163
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 AT11C_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CC50A_HUMANTMEM30Aphysical
21914794
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 AT11C_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-445, 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-445, AND MASSSPECTROMETRY.
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-445, AND MASSSPECTROMETRY.
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
Anal. Sci. 24:161-166(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-261, AND MASSSPECTROMETRY.

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