CC50A_HUMAN - dbPTM
CC50A_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CC50A_HUMAN
UniProt AC Q9NV96
Protein Name Cell cycle control protein 50A
Gene Name TMEM30A
Organism Homo sapiens (Human).
Sequence Length 361
Subcellular Localization Membrane
Multi-pass membrane protein. Cell membrane. Golgi apparatus. Cytoplasmic vesicle, secretory vesicle membrane. Apical cell membrane.
Protein Description Accessory 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. The beta subunit may assist in binding of the phospholipid substrate. Required for the proper folding, assembly and ER to Golgi exit of the ATP8A2:TMEM30A flippase complex. ATP8A2:TMEM30A may be involved in regulation of neurite outgrowth, and, reconstituted to liposomes, predomiminantly transports phosphatidylserine (PS) and to a lesser extent phosphatidylethanolamine (PE). The ATP8A1:TMEM30A flippase complex seems to play a role in regulation of cell migration probably involving flippase-mediated translocation of phosphatidylethanolamine (PE) at the plasma membrane. Required for the formation of the ATP8A2, ATP8B1 and ATP8B2 P-type ATPAse intermediate phosphoenzymes. Involved in uptake of platelet-activating factor (PAF), synthetic drug alkylphospholipid edelfosine, and, probably in association with ATP8B1, of perifosine. Also mediate the export of alpha subunits ATP8A1, ATP8B1, ATP8B2, ATP8B4, ATP10A, ATP10B, ATP10D, ATP11A, ATP11B and ATP11C from the ER to other membrane localizations..
Protein Sequence MAMNYNAKDEVDGGPPCAPGGTAKTRRPDNTAFKQQRLPAWQPILTAGTVLPIFFIIGLIFIPIGIGIFVTSNNIREIEIDYTGTEPSSPCNKCLSPDVTPCFCTINFTLEKSFEGNVFMYYGLSNFYQNHRRYVKSRDDSQLNGDSSALLNPSKECEPYRRNEDKPIAPCGAIANSMFNDTLELFLIGNDSYPIPIALKKKGIAWWTDKNVKFRNPPGGDNLEERFKGTTKPVNWLKPVYMLDSDPDNNGFINEDFIVWMRTAALPTFRKLYRLIERKSDLHPTLPAGRYSLNVTYNYPVHYFDGRKRMILSTISWMGGKNPFLGIAYIAVGSISFLLGVVLLVINHKYRNSSNTADITI
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------MAMNYNAKD
------CCCCCCCCC		8.5719413330
5Phosphorylation---MAMNYNAKDEVD
---CCCCCCCCCCCC		11.9226552605
8UbiquitinationMAMNYNAKDEVDGGP
CCCCCCCCCCCCCCC		51.2733845483
22PhosphorylationPPCAPGGTAKTRRPD
CCCCCCCCCCCCCCC		30.7826552605
24UbiquitinationCAPGGTAKTRRPDNT
CCCCCCCCCCCCCCC		42.2623000965
24 (in isoform 2)Ubiquitination-42.2621890473
24 (in isoform 1)Ubiquitination-42.2621890473
34UbiquitinationRPDNTAFKQQRLPAW
CCCCCCHHHCCCCCC		42.9521906983
34 (in isoform 1)Ubiquitination-42.9521890473
34 (in isoform 2)Ubiquitination-42.9521890473
85O-linked_GlycosylationIEIDYTGTEPSSPCN
EEEECCCCCCCCCCC		36.60OGP
89PhosphorylationYTGTEPSSPCNKCLS
CCCCCCCCCCCCCCC		44.16-
91 (in isoform 3)Ubiquitination-9.0921890473
94 (in isoform 3)Ubiquitination-2.5721890473
107N-linked_GlycosylationTPCFCTINFTLEKSF
CCEEEEEEEEEEECC		13.0031416931
119UbiquitinationKSFEGNVFMYYGLSN
ECCCCCEEEEEECCH		2.7821963094
128PhosphorylationYYGLSNFYQNHRRYV
EEECCHHHHHCHHHH		16.80-
141PhosphorylationYVKSRDDSQLNGDSS
HHHCCCCHHCCCCCC		40.6425307156
147PhosphorylationDSQLNGDSSALLNPS
CHHCCCCCCCCCCCC		20.9325307156
148PhosphorylationSQLNGDSSALLNPSK
HHCCCCCCCCCCCCC		27.8925307156
155UbiquitinationSALLNPSKECEPYRR
CCCCCCCCCCCCCCC		68.5821963094
160 (in isoform 3)Ubiquitination-10.4221890473
164UbiquitinationCEPYRRNEDKPIAPC
CCCCCCCCCCCCCCC		66.6523503661
165UbiquitinationEPYRRNEDKPIAPCG
CCCCCCCCCCCCCCC		66.6323503661
166 (in isoform 2)Ubiquitination-31.95-
166UbiquitinationPYRRNEDKPIAPCGA
CCCCCCCCCCCCCCH		31.9523503661
174 (in isoform 2)Ubiquitination-1.9521890473
174UbiquitinationPIAPCGAIANSMFND
CCCCCCHHHHHHHCC		1.9521890473
177UbiquitinationPCGAIANSMFNDTLE
CCCHHHHHHHCCCEE		18.7421890473
177 (in isoform 2)Ubiquitination-18.7421890473
180N-linked_GlycosylationAIANSMFNDTLELFL
HHHHHHHCCCEEEEE		32.4931416931
190N-linked_GlycosylationLELFLIGNDSYPIPI
EEEEEECCCCCCCEE		28.2319349973
190N-linked_GlycosylationLELFLIGNDSYPIPI
EEEEEECCCCCCCEE		28.2319349973
192UbiquitinationLFLIGNDSYPIPIAL
EEEECCCCCCCEEEE		36.4929967540
196UbiquitinationGNDSYPIPIALKKKG
CCCCCCCEEEEEECC		10.9929967540
200UbiquitinationYPIPIALKKKGIAWW
CCCEEEEEECCEEEE		43.3423503661
201UbiquitinationPIPIALKKKGIAWWT
CCEEEEEECCEEEEE		58.0223503661
202UbiquitinationIPIALKKKGIAWWTD
CEEEEEECCEEEEEC		54.7023503661
210UbiquitinationGIAWWTDKNVKFRNP
CEEEEECCCCCCCCC		57.1522817900
210 (in isoform 1)Ubiquitination-57.1521890473
213 (in isoform 1)Ubiquitination-48.2621890473
213UbiquitinationWWTDKNVKFRNPPGG
EEECCCCCCCCCCCC		48.2622817900
228UbiquitinationDNLEERFKGTTKPVN
CCHHHHHCCCCCCCC		62.6629967540
232UbiquitinationERFKGTTKPVNWLKP
HHHCCCCCCCCCCEE		46.9729967540
243 (in isoform 2)Ubiquitination-2.9021890473
243UbiquitinationWLKPVYMLDSDPDNN
CCEEEEEECCCCCCC		2.9029967540
279UbiquitinationLYRLIERKSDLHPTL
HHHHHHHHCCCCCCC		35.2222817900
279 (in isoform 1)Ubiquitination-35.2221890473
280PhosphorylationYRLIERKSDLHPTLP
HHHHHHHCCCCCCCC		52.1828270605
285PhosphorylationRKSDLHPTLPAGRYS
HHCCCCCCCCCCCEE		34.3328270605
285O-linked_GlycosylationRKSDLHPTLPAGRYS
HHCCCCCCCCCCCEE		34.3355826101
294N-linked_GlycosylationPAGRYSLNVTYNYPV
CCCCEEEEEEEECCC		20.3919159218
294N-linked_GlycosylationPAGRYSLNVTYNYPV
CCCCEEEEEEEECCC		20.3919349973
298N-linked_GlycosylationYSLNVTYNYPVHYFD
EEEEEEEECCCEEEC		25.85-
298N-linked_GlycosylationYSLNVTYNYPVHYFD
EEEEEEEECCCEEEC		25.8519349973
313PhosphorylationGRKRMILSTISWMGG
CCEEEEEEEEHHHCC		16.87-
360PhosphorylationSSNTADITI------
CCCCCCCCC------		22.6025159151
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 CC50A_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CC50A_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 CC50A_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
AT8A1_HUMANATP8A1physical
23269685
LSR_HUMANLSRphysical
26186194
1C07_HUMANHLA-Cphysical
26186194
BACE2_HUMANBACE2physical
26186194
CLCC1_HUMANCLCC1physical
26186194
AGRL1_HUMANLPHN1physical
26186194
SARAF_HUMANSARAFphysical
26186194
NSDHL_HUMANNSDHLphysical
26186194
NSMA_HUMANSMPD2physical
26186194
A4_HUMANAPPphysical
26186194
DHRS7_HUMANDHRS7physical
26186194
ACHA5_HUMANCHRNA5physical
26186194
ACV1B_HUMANACVR1Bphysical
26186194
MARC1_HUMANMARC1physical
26186194
DJC16_HUMANDNAJC16physical
26186194
HMR1_HUMANMR1physical
26186194
HYEP_HUMANEPHX1physical
26186194
GRM1A_HUMANGRAMD1Aphysical
26186194
HMDH_HUMANHMGCRphysical
26186194
PON2_HUMANPON2physical
26186194
EPHA7_HUMANEPHA7physical
26186194
TX264_HUMANTEX264physical
26186194
UPK3L_HUMANUPK3BLphysical
26186194
NETO2_HUMANNETO2physical
26186194
RN149_HUMANRNF149physical
26186194
GPC6_HUMANGPC6physical
26186194
GLBL2_HUMANGLB1L2physical
26186194
CGRF1_HUMANCGRRF1physical
26186194
APOL2_HUMANAPOL2physical
26186194
BNIP3_HUMANBNIP3physical
26186194
TMM59_HUMANTMEM59physical
26186194
TMPPE_HUMANTMPPEphysical
26186194
TMED7_HUMANTMED7physical
26186194
LMF1_HUMANLMF1physical
26186194
SEM4C_HUMANSEMA4Cphysical
26186194
ST17B_HUMANSTK17Bphysical
26186194
EDEM2_HUMANEDEM2physical
26186194
NRP1_HUMANNRP1physical
26186194
DNJB9_HUMANDNAJB9physical
26186194
SC11C_HUMANSEC11Cphysical
26186194
TLCD2_HUMANTLCD2physical
26186194
AVR2B_HUMANACVR2Bphysical
26186194
SARAF_HUMANSARAFphysical
28514442
AVR2B_HUMANACVR2Bphysical
28514442
NSMA_HUMANSMPD2physical
28514442
CNNM1_HUMANCNNM1physical
28514442
A4_HUMANAPPphysical
28514442
DHRS7_HUMANDHRS7physical
28514442
1C07_HUMANHLA-Cphysical
28514442
GRM1A_HUMANGRAMD1Aphysical
28514442
MKS3_HUMANTMEM67physical
28514442
EDEM2_HUMANEDEM2physical
28514442
UPK3L_HUMANUPK3BLphysical
28514442
LSR_HUMANLSRphysical
28514442
BACE2_HUMANBACE2physical
28514442
CGRF1_HUMANCGRRF1physical
28514442
MARC1_HUMANMARC1physical
28514442
RN149_HUMANRNF149physical
28514442
NB5R1_HUMANCYB5R1physical
28514442
F213A_HUMANFAM213Aphysical
28514442
TMPPE_HUMANTMPPEphysical
28514442
TX264_HUMANTEX264physical
28514442
ST17B_HUMANSTK17Bphysical
28514442
PON2_HUMANPON2physical
28514442
TMX4_HUMANTMX4physical
28514442
1B07_HUMANHLA-Bphysical
28514442
1B18_HUMANHLA-Bphysical
28514442
ACHA5_HUMANCHRNA5physical
28514442
HYEP_HUMANEPHX1physical
28514442
ANTR1_HUMANANTXR1physical
28514442
HMR1_HUMANMR1physical
28514442
TMED7_HUMANTMED7physical
28514442
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 CC50A_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
N-linked Glycosylation
ReferencePubMed
"Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins.";
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,Schiess R., Aebersold R., Watts J.D.;
Nat. Biotechnol. 27:378-386(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-190, AND MASSSPECTROMETRY.
"Glycoproteomics analysis of human liver tissue by combination ofmultiple enzyme digestion and hydrazide chemistry.";
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
J. Proteome Res. 8:651-661(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-294, AND MASSSPECTROMETRY.

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