FACE1_HUMAN - dbPTM
FACE1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FACE1_HUMAN
UniProt AC O75844
Protein Name CAAX prenyl protease 1 homolog
Gene Name ZMPSTE24
Organism Homo sapiens (Human).
Sequence Length 475
Subcellular Localization Endoplasmic reticulum membrane
Multi-pass membrane protein . Nucleus inner membrane
Multi-pass membrane protein .
Protein Description Proteolytically removes the C-terminal three residues of farnesylated proteins. Acts on lamin A/C..
Protein Sequence MGMWASLDALWEMPAEKRIFGAVLLFSWTVYLWETFLAQRQRRIYKTTTHVPPELGQIMDSETFEKSRLYQLDKSTFSFWSGLYSETEGTLILLFGGIPYLWRLSGRFCGYAGFGPEYEITQSLVFLLLATLFSALTGLPWSLYNTFVIEEKHGFNQQTLGFFMKDAIKKFVVTQCILLPVSSLLLYIIKIGGDYFFIYAWLFTLVVSLVLVTIYADYIAPLFDKFTPLPEGKLKEEIEVMAKSIDFPLTKVYVVEGSKRSSHSNAYFYGFFKNKRIVLFDTLLEEYSVLNKDIQEDSGMEPRNEEEGNSEEIKAKVKNKKQGCKNEEVLAVLGHELGHWKLGHTVKNIIISQMNSFLCFFLFAVLIGRKELFAAFGFYDSQPTLIGLLIIFQFIFSPYNEVLSFCLTVLSRRFEFQADAFAKKLGKAKDLYSALIKLNKDNLGFPVSDWLFSMWHYSHPPLLERLQALKTMKQH
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
6Phosphorylation--MGMWASLDALWEM
--CCCCCCHHHHHCC		15.98-
35PhosphorylationWTVYLWETFLAQRQR
HHHHHHHHHHHHHHH		16.62-
45PhosphorylationAQRQRRIYKTTTHVP
HHHHHHHHHCCCCCC		10.64-
46UbiquitinationQRQRRIYKTTTHVPP
HHHHHHHHCCCCCCC		36.7021906983
61PhosphorylationELGQIMDSETFEKSR
HHHCCCCCHHHCHHH		22.58-
66UbiquitinationMDSETFEKSRLYQLD
CCCHHHCHHHCEECC		36.3621906983
67PhosphorylationDSETFEKSRLYQLDK
CCHHHCHHHCEECCH		21.96-
233UbiquitinationFTPLPEGKLKEEIEV
CCCCCCCCCHHHHHH		55.5133845483
235UbiquitinationPLPEGKLKEEIEVMA
CCCCCCCHHHHHHHH		57.7122817900
243UbiquitinationEEIEVMAKSIDFPLT
HHHHHHHHHCCCCCC		29.8321963094
244PhosphorylationEIEVMAKSIDFPLTK
HHHHHHHHCCCCCCE		20.1821712546
250PhosphorylationKSIDFPLTKVYVVEG
HHCCCCCCEEEEEEC		20.7818452278
251UbiquitinationSIDFPLTKVYVVEGS
HCCCCCCEEEEEECC		38.9721906983
253PhosphorylationDFPLTKVYVVEGSKR
CCCCCEEEEEECCCC		10.5928152594
259UbiquitinationVYVVEGSKRSSHSNA
EEEEECCCCCCCCCC		68.1321906983
2592-HydroxyisobutyrylationVYVVEGSKRSSHSNA
EEEEECCCCCCCCCC		68.13-
261PhosphorylationVVEGSKRSSHSNAYF
EEECCCCCCCCCCEE		35.8229214152
262PhosphorylationVEGSKRSSHSNAYFY
EECCCCCCCCCCEEE		34.6629214152
264PhosphorylationGSKRSSHSNAYFYGF
CCCCCCCCCCEEEEE		25.7129214152
292UbiquitinationEEYSVLNKDIQEDSG
HHHHHHCCHHHCCCC		52.6429967540
298PhosphorylationNKDIQEDSGMEPRNE
CCHHHCCCCCCCCCC		39.0125159151
300SulfoxidationDIQEDSGMEPRNEEE
HHHCCCCCCCCCCCC		8.0921406390
310PhosphorylationRNEEEGNSEEIKAKV
CCCCCCCHHHHHHHH		47.6825159151
314UbiquitinationEGNSEEIKAKVKNKK
CCCHHHHHHHHHCCC		45.4921906983
316UbiquitinationNSEEIKAKVKNKKQG
CHHHHHHHHHCCCCC		49.0622817900
318UbiquitinationEEIKAKVKNKKQGCK
HHHHHHHHCCCCCCC		63.4422817900
320UbiquitinationIKAKVKNKKQGCKNE
HHHHHHCCCCCCCCH		40.5323503661
325UbiquitinationKNKKQGCKNEEVLAV
HCCCCCCCCHHHHHH		74.3729967540
325AcetylationKNKKQGCKNEEVLAV
HCCCCCCCCHHHHHH		74.3726051181
341UbiquitinationGHELGHWKLGHTVKN
CHHHCHHHHCHHHHH		38.6329967540
4232-HydroxyisobutyrylationFQADAFAKKLGKAKD
HCHHHHHHHHCCHHH		41.92-
427AcetylationAFAKKLGKAKDLYSA
HHHHHHCCHHHHHHH		63.8012435105
429MalonylationAKKLGKAKDLYSALI
HHHHCCHHHHHHHHH		52.3226320211
429UbiquitinationAKKLGKAKDLYSALI
HHHHCCHHHHHHHHH		52.3233845483
429AcetylationAKKLGKAKDLYSALI
HHHHCCHHHHHHHHH		52.3212435115
432PhosphorylationLGKAKDLYSALIKLN
HCCHHHHHHHHHHHC		11.3021406692
433PhosphorylationGKAKDLYSALIKLNK
CCHHHHHHHHHHHCC		24.7221406692
437UbiquitinationDLYSALIKLNKDNLG
HHHHHHHHHCCCCCC		47.0223000965
440UbiquitinationSALIKLNKDNLGFPV
HHHHHHCCCCCCCCH		59.4323000965
470MalonylationLERLQALKTMKQH--
HHHHHHHHHHHCC--		49.9826320211
470AcetylationLERLQALKTMKQH--
HHHHHHHHHHHCC--		49.9825953088
470UbiquitinationLERLQALKTMKQH--
HHHHHHHHHHHCC--		49.98-
473UbiquitinationLQALKTMKQH-----
HHHHHHHHCC-----		50.9124816145
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 FACE1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of FACE1_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 FACE1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
OST48_HUMANDDOSTphysical
22939629
S10AA_HUMANS100A10physical
22939629
MGST3_HUMANMGST3physical
22939629
VATH_HUMANATP6V1Hphysical
22939629
NDUB7_HUMANNDUFB7physical
22939629
TMM43_HUMANTMEM43physical
22939629
SYJ2B_HUMANSYNJ2BPphysical
22939629
RAB5C_HUMANRAB5Cphysical
22939629
GALT2_HUMANGALNT2physical
22939629
HNRPF_HUMANHNRNPFphysical
22939629
RT05_HUMANMRPS5physical
22939629
VDAC1_HUMANVDAC1physical
22939629
HNRL1_HUMANHNRNPUL1physical
22939629
K2013_HUMANKIAA2013physical
22939629
PTN1_HUMANPTPN1physical
22939629
RM40_HUMANMRPL40physical
22939629
RAB10_HUMANRAB10physical
22939629
CLH1_HUMANCLTCphysical
26344197
Drug and Disease Associations
Kegg Disease
H00663 Restrictive dermopathy
H00665 Mandibuloacral dysplasia
OMIM Disease
608612Mandibuloacral dysplasia with type B lipodystrophy (MADB)
275210Lethal tight skin contracture syndrome (LTSCS)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of FACE1_HUMAN

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-310, AND MASSSPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory