FNTA_HUMAN - dbPTM
FNTA_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FNTA_HUMAN
UniProt AC P49354
Protein Name Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha
Gene Name FNTA
Organism Homo sapiens (Human).
Sequence Length 379
Subcellular Localization
Protein Description Essential subunit of both the farnesyltransferase and the geranylgeranyltransferase complex. Contributes to the transfer of a farnesyl or geranylgeranyl moiety from farnesyl or geranylgeranyl diphosphate to a cysteine at the fourth position from the C-terminus of several proteins having the C-terminal sequence Cys-aliphatic-aliphatic-X. May positively regulate neuromuscular junction development downstream of MUSK via its function in RAC1 prenylation and activation..
Protein Sequence MAATEGVGEAAQGGEPGQPAQPPPQPHPPPPQQQHKEEMAAEAGEAVASPMDDGFVSLDSPSYVLYRDRAEWADIDPVPQNDGPNPVVQIIYSDKFRDVYDYFRAVLQRDERSERAFKLTRDAIELNAANYTVWHFRRVLLKSLQKDLHEEMNYITAIIEEQPKNYQVWHHRRVLVEWLRDPSQELEFIADILNQDAKNYHAWQHRQWVIQEFKLWDNELQYVDQLLKEDVRNNSVWNQRYFVISNTTGYNDRAVLEREVQYTLEMIKLVPHNESAWNYLKGILQDRGLSKYPNLLNQLLDLQPSHSSPYLIAFLVDIYEDMLENQCDNKEDILNKALELCEILAKEKDTIRKEYWRYIGRSLQSKHSTENDSPTNVQQ
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------MAATEGVGE
------CCCCCCCCH		24.0819413330
49PhosphorylationEAGEAVASPMDDGFV
HHHHHCCCCCCCCCC		17.7326074081
57PhosphorylationPMDDGFVSLDSPSYV
CCCCCCCCCCCCCEE		24.9728985074
60PhosphorylationDGFVSLDSPSYVLYR
CCCCCCCCCCEEEEC		22.4926074081
62 (in isoform 2)Phosphorylation-31.6529116813
62PhosphorylationFVSLDSPSYVLYRDR
CCCCCCCCEEEECCC		31.6526074081
63PhosphorylationVSLDSPSYVLYRDRA
CCCCCCCEEEECCCC		9.6226074081
66PhosphorylationDSPSYVLYRDRAEWA
CCCCEEEECCCCCCC		10.6326074081
92PhosphorylationNPVVQIIYSDKFRDV
CCCEEEEECCCCHHH		16.67-
93PhosphorylationPVVQIIYSDKFRDVY
CCEEEEECCCCHHHH		24.74-
95UbiquitinationVQIIYSDKFRDVYDY
EEEEECCCCHHHHHH		36.04-
142UbiquitinationHFRRVLLKSLQKDLH
HHHHHHHHHHHHHHH		44.9833845483
152SulfoxidationQKDLHEEMNYITAII
HHHHHHHHCHHHHHH		4.1430846556
161 (in isoform 2)Ubiquitination-62.8721906983
183PhosphorylationVEWLRDPSQELEFIA
HHHHHCHHHHHHHHH		40.3428348404
198UbiquitinationDILNQDAKNYHAWQH
HHHCCCCCHHHHHHH		67.35-
228 (in isoform 1)Ubiquitination-61.5321906983
228UbiquitinationQYVDQLLKEDVRNNS
HHHHHHHHHHHHCCC		61.5322817900
247PhosphorylationRYFVISNTTGYNDRA
EEEEEECCCCCCHHH		18.14-
248PhosphorylationYFVISNTTGYNDRAV
EEEEECCCCCCHHHH		41.75-
250PhosphorylationVISNTTGYNDRAVLE
EEECCCCCCHHHHHH		16.29-
253MethylationNTTGYNDRAVLEREV
CCCCCCHHHHHHHHH		23.98-
287MethylationLKGILQDRGLSKYPN
HHHHHHHCCHHHCCH		34.68-
336UbiquitinationNKEDILNKALELCEI
CHHHHHHHHHHHHHH		51.4029967540
346UbiquitinationELCEILAKEKDTIRK
HHHHHHHHCCHHHHH		62.9529967540
350PhosphorylationILAKEKDTIRKEYWR
HHHHCCHHHHHHHHH		33.48-
355PhosphorylationKDTIRKEYWRYIGRS
CHHHHHHHHHHHHHH		9.7520068231
358PhosphorylationIRKEYWRYIGRSLQS
HHHHHHHHHHHHHHH		8.1220068231
362PhosphorylationYWRYIGRSLQSKHST
HHHHHHHHHHHCCCC		26.0820068231
365PhosphorylationYIGRSLQSKHSTEND
HHHHHHHHCCCCCCC		37.3120068231
366UbiquitinationIGRSLQSKHSTENDS
HHHHHHHCCCCCCCC		28.7229967540
368PhosphorylationRSLQSKHSTENDSPT
HHHHHCCCCCCCCCC		40.9530206219
369PhosphorylationSLQSKHSTENDSPTN
HHHHCCCCCCCCCCC		38.2322167270
373PhosphorylationKHSTENDSPTNVQQ-
CCCCCCCCCCCCCC-		45.2522167270
375PhosphorylationSTENDSPTNVQQ---
CCCCCCCCCCCC---		52.5622167270
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 FNTA_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of FNTA_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 FNTA_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TGFR1_HUMANTGFBR1physical
8530343
TGM2_HUMANTGM2physical
21988832
INHBB_HUMANINHBBphysical
21988832
STAT2_HUMANSTAT2physical
21988832
SAFB2_HUMANSAFB2physical
21988832
RL13A_HUMANRPL13Aphysical
21988832
HXK2_HUMANHK2physical
22863883
TOP1_HUMANTOP1genetic
28319113
KDM6A_HUMANKDM6Agenetic
28319113
XRCC3_HUMANXRCC3genetic
27453043
ATAD5_HUMANATAD5genetic
27453043
BLM_HUMANBLMgenetic
27453043
MTOR_HUMANMTORgenetic
27453043
RS19_HUMANRPS19genetic
27453043
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 FNTA_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, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-373, AND MASS SPECTROMETRY.
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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-373, AND MASS SPECTROMETRY.
"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-373, AND MASSSPECTROMETRY.

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