CC50B_HUMAN - dbPTM
CC50B_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CC50B_HUMAN
UniProt AC Q3MIR4
Protein Name Cell cycle control protein 50B
Gene Name TMEM30B
Organism Homo sapiens (Human).
Sequence Length 351
Subcellular Localization Cell membrane
Multi-pass membrane protein .
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 (Probable). Can mediate the export of alpha subunits ATP8A1, ATP8B1, ATP8B2 and ATP8B4 from the ER to the plasma membrane..
Protein Sequence MTWSATARGAHQPDNTAFTQQRLPAWQPLLSASIALPLFFCAGLAFIGLGLGLYYSSNGIKELEYDYTGDPGTGNCSVCAAAGQGRALPPPCSCAWYFSLPELFQGPVYLYYELTNFYQNNRRYGVSRDDAQLSGLPSALRHPVNECAPYQRSAAGLPIAPCGAIANSLFNDSFSLWHQRQPGGPYVEVPLDRSGIAWWTDYHVKFRNPPLVNGSLALAFQGTAPPPNWRRPVYELSPDPNNTGFINQDFVVWMRTAALPTFRKLYARIRQGNYSAGLPRGAYRVNITYNYPVRAFGGHKLLIFSSISWMGGKNPFLGIAYLVVGSLCILTGFVMLVVYIRYQDQDDDDEE
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------MTWSATARG
------CCCCCCCCC
28.29-
4Phosphorylation----MTWSATARGAH
----CCCCCCCCCCC
13.43-
6Phosphorylation--MTWSATARGAHQP
--CCCCCCCCCCCCC
16.04-
75N-linked_GlycosylationTGDPGTGNCSVCAAA
CCCCCCCCCCEEECC
18.09UniProtKB CARBOHYD
213N-linked_GlycosylationFRNPPLVNGSLALAF
ECCCCCCCCEEEEEE
41.86UniProtKB CARBOHYD
286N-linked_GlycosylationPRGAYRVNITYNYPV
CCCCEEEEEEEECCC
16.34UniProtKB CARBOHYD
291PhosphorylationRVNITYNYPVRAFGG
EEEEEEECCCEEECC
7.84-
305PhosphorylationGHKLLIFSSISWMGG
CEEEEEEEECCCCCC
21.5528348404
306PhosphorylationHKLLIFSSISWMGGK
EEEEEEEECCCCCCC
15.1928348404
308PhosphorylationLLIFSSISWMGGKNP
EEEEEECCCCCCCCC
16.9828348404
321PhosphorylationNPFLGIAYLVVGSLC
CCCHHHHHHHHHHHH
9.7125332170
339PhosphorylationGFVMLVVYIRYQDQD
HHEEEEEEEECCCCC
3.3824719451

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 CC50B_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CC50B_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 CC50B_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PCD17_HUMANPCDH17physical
28514442
PRTG_HUMANPRTGphysical
28514442
SGCE_HUMANSGCEphysical
28514442
IGDC4_HUMANIGDCC4physical
28514442
PCDGB_HUMANPCDHGA11physical
28514442
TYRO3_HUMANTYRO3physical
28514442
FGFR4_HUMANFGFR4physical
28514442
TM230_HUMANTMEM230physical
28514442
FGFR2_HUMANFGFR2physical
28514442
PDXL2_HUMANPODXL2physical
28514442
PCDGL_HUMANPCDHGC4physical
28514442
NECT2_HUMANPVRL2physical
28514442
FGFR3_HUMANFGFR3physical
28514442
MA1A1_HUMANMAN1A1physical
28514442
SDK2_HUMANSDK2physical
28514442
TTMP_HUMANC3orf52physical
28514442
PLXA2_HUMANPLXNA2physical
28514442
FUT8_HUMANFUT8physical
28514442
PCDGK_HUMANPCDHGC3physical
28514442
PCD10_HUMANPCDH10physical
28514442
TM143_HUMANTMEM143physical
28514442
NALD2_HUMANNAALAD2physical
28514442
JAG2_HUMANJAG2physical
28514442
KIRR1_HUMANKIRRELphysical
28514442
EPHA7_HUMANEPHA7physical
28514442
CELR2_HUMANCELSR2physical
28514442
OCLN_HUMANOCLNphysical
28514442
CDHR1_HUMANCDHR1physical
28514442
CC50A_HUMANTMEM30Aphysical
28514442
KLH15_HUMANKLHL15physical
28514442
I27RA_HUMANIL27RAphysical
28514442
TNFL9_HUMANTNFSF9physical
28514442
ULBP3_HUMANULBP3physical
28514442
AGRL1_HUMANLPHN1physical
28514442
C1QRF_HUMANC1QL1physical
28514442
ULBP2_HUMANULBP2physical
28514442
MPZL1_HUMANMPZL1physical
28514442
SCRB1_HUMANSCARB1physical
28514442
MFAP3_HUMANMFAP3physical
28514442
LRFN1_HUMANLRFN1physical
28514442
B4GT1_HUMANB4GALT1physical
28514442
F1712_HUMANFAM171A2physical
28514442
CAH12_HUMANCA12physical
28514442
APBB2_HUMANAPBB2physical
28514442
PCDH7_HUMANPCDH7physical
28514442
K319L_HUMANKIAA0319Lphysical
28514442
TSN3_HUMANTSPAN3physical
28514442
IGSF8_HUMANIGSF8physical
28514442
FCGRN_HUMANFCGRTphysical
28514442
STX4_HUMANSTX4physical
28514442
TSN6_HUMANTSPAN6physical
28514442
SIDT2_HUMANSIDT2physical
28514442
A4_HUMANAPPphysical
28514442
DSC2_HUMANDSC2physical
28514442
TIP_HUMANITFG1physical
28514442
FGFR1_HUMANFGFR1physical
28514442
GOT1B_HUMANGOLT1Bphysical
28514442
KLRG2_HUMANKLRG2physical
28514442
C1QL4_HUMANC1QL4physical
28514442
CELR3_HUMANCELSR3physical
28514442
LRC8A_HUMANLRRC8Aphysical
28514442
DSC3_HUMANDSC3physical
28514442
PTPRF_HUMANPTPRFphysical
28514442
MKS3_HUMANTMEM67physical
28514442
ACV1B_HUMANACVR1Bphysical
28514442
CD276_HUMANCD276physical
28514442
INGR1_HUMANIFNGR1physical
28514442
GPC5C_HUMANGPRC5Cphysical
28514442
SEM4F_HUMANSEMA4Fphysical
28514442
NETO2_HUMANNETO2physical
28514442
MA1A2_HUMANMAN1A2physical
28514442
MANEA_HUMANMANEAphysical
28514442
NGBR_HUMANNUS1physical
28514442
SEM4C_HUMANSEMA4Cphysical
28514442
PTPRS_HUMANPTPRSphysical
28514442
GP1BB_HUMANGP1BBphysical
28514442
STXB3_HUMANSTXBP3physical
28514442

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CC50B_HUMAN

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Related Literatures of Post-Translational Modification

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