CISY_HUMAN - dbPTM
CISY_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CISY_HUMAN
UniProt AC O75390
Protein Name Citrate synthase, mitochondrial
Gene Name CS
Organism Homo sapiens (Human).
Sequence Length 466
Subcellular Localization Mitochondrion matrix.
Protein Description
Protein Sequence MALLTAAARLLGTKNASCLVLAARHASASSTNLKDILADLIPKEQARIKTFRQQHGKTVVGQITVDMMYGGMRGMKGLVYETSVLDPDEGIRFRGFSIPECQKLLPKAKGGEEPLPEGLFWLLVTGHIPTEEQVSWLSKEWAKRAALPSHVVTMLDNFPTNLHPMSQLSAAVTALNSESNFARAYAQGISRTKYWELIYEDSMDLIAKLPCVAAKIYRNLYREGSGIGAIDSNLDWSHNFTNMLGYTDHQFTELTRLYLTIHSDHEGGNVSAHTSHLVGSALSDPYLSFAAAMNGLAGPLHGLANQEVLVWLTQLQKEVGKDVSDEKLRDYIWNTLNSGRVVPGYGHAVLRKTDPRYTCQREFALKHLPNDPMFKLVAQLYKIVPNVLLEQGKAKNPWPNVDAHSGVLLQYYGMTEMNYYTVLFGVSRALGVLAQLIWSRALGFPLERPKSMSTEGLMKFVDSKSG
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
5Phosphorylation---MALLTAAARLLG
---CHHHHHHHHHHC		18.3320068231
13PhosphorylationAAARLLGTKNASCLV
HHHHHHCCCCHHHHH		22.5420068231
34UbiquitinationSASSTNLKDILADLI
CCCCCCHHHHHHHHC		44.80-
432-HydroxyisobutyrylationILADLIPKEQARIKT
HHHHHCCHHHHHHHH		56.30-
43AcetylationILADLIPKEQARIKT
HHHHHCCHHHHHHHH		56.3023954790
43MalonylationILADLIPKEQARIKT
HHHHHCCHHHHHHHH		56.3026320211
43UbiquitinationILADLIPKEQARIKT
HHHHHCCHHHHHHHH		56.3021890473
57SuccinylationTFRQQHGKTVVGQIT
HHHHHHCCEEEEEEE		35.70-
57SuccinylationTFRQQHGKTVVGQIT
HHHHHHCCEEEEEEE		35.70-
58PhosphorylationFRQQHGKTVVGQITV
HHHHHCCEEEEEEEH		25.6424043423
64PhosphorylationKTVVGQITVDMMYGG
CEEEEEEEHHHHCCC		11.5424043423
69PhosphorylationQITVDMMYGGMRGMK
EEEHHHHCCCCCCCC		12.1420068231
76SuccinylationYGGMRGMKGLVYETS
CCCCCCCCCEEEEEE		52.49-
76MalonylationYGGMRGMKGLVYETS
CCCCCCCCCEEEEEE		52.4926320211
76SuccinylationYGGMRGMKGLVYETS
CCCCCCCCCEEEEEE		52.4927452117
76UbiquitinationYGGMRGMKGLVYETS
CCCCCCCCCEEEEEE		52.49-
76AcetylationYGGMRGMKGLVYETS
CCCCCCCCCEEEEEE		52.4923954790
80PhosphorylationRGMKGLVYETSVLDP
CCCCCEEEEEEEECC		20.6622817900
82PhosphorylationMKGLVYETSVLDPDE
CCCEEEEEEEECCCC		13.37-
83PhosphorylationKGLVYETSVLDPDEG
CCEEEEEEEECCCCC		14.56-
97PhosphorylationGIRFRGFSIPECQKL
CCCCCCCCCHHHHHH		39.8025159151
101GlutathionylationRGFSIPECQKLLPKA
CCCCCHHHHHHCCCC		3.4722555962
101S-nitrosylationRGFSIPECQKLLPKA
CCCCCHHHHHHCCCC		3.472212679
103UbiquitinationFSIPECQKLLPKAKG
CCCHHHHHHCCCCCC		64.7521890473
103SuccinylationFSIPECQKLLPKAKG
CCCHHHHHHCCCCCC		64.75-
103MalonylationFSIPECQKLLPKAKG
CCCHHHHHHCCCCCC		64.7526320211
103AcetylationFSIPECQKLLPKAKG
CCCHHHHHHCCCCCC		64.7523749302
103SuccinylationFSIPECQKLLPKAKG
CCCHHHHHHCCCCCC		64.75-
185PhosphorylationESNFARAYAQGISRT
CCHHHHHHHHCCCHH		8.2328152594
185NitrationESNFARAYAQGISRT
CCHHHHHHHHCCCHH		8.23-
190PhosphorylationRAYAQGISRTKYWEL
HHHHHCCCHHHHHHH		40.5028060719
193SuccinylationAQGISRTKYWELIYE
HHCCCHHHHHHHHCC		47.45-
193AcetylationAQGISRTKYWELIYE
HHCCCHHHHHHHHCC		47.4525038526
193SuccinylationAQGISRTKYWELIYE
HHCCCHHHHHHHHCC		47.45-
199PhosphorylationTKYWELIYEDSMDLI
HHHHHHHCCCCHHHH		26.7230576142
211S-nitrosylationDLIAKLPCVAAKIYR
HHHHHCHHHHHHHHH		4.7522178444
211S-nitrosocysteineDLIAKLPCVAAKIYR
HHHHHCHHHHHHHHH		4.75-
215AcetylationKLPCVAAKIYRNLYR
HCHHHHHHHHHHHHH		30.4525953088
215UbiquitinationKLPCVAAKIYRNLYR
HCHHHHHHHHHHHHH		30.45-
217PhosphorylationPCVAAKIYRNLYREG
HHHHHHHHHHHHHCC		7.8530576142
221PhosphorylationAKIYRNLYREGSGIG
HHHHHHHHHCCCCCC		15.3524043423
237PhosphorylationIDSNLDWSHNFTNML
CCCCCCCCCCCCCCC		14.2830576142
252PhosphorylationGYTDHQFTELTRLYL
CCCCHHHHHHHEEEE		24.4230576142
255PhosphorylationDHQFTELTRLYLTIH
CHHHHHHHEEEEEEE		16.6430576142
321UbiquitinationQLQKEVGKDVSDEKL
HHHHHHCCCCCHHHH		61.20-
321SuccinylationQLQKEVGKDVSDEKL
HHHHHHCCCCCHHHH		61.20-
321SuccinylationQLQKEVGKDVSDEKL
HHHHHHCCCCCHHHH		61.2023954790
321AcetylationQLQKEVGKDVSDEKL
HHHHHHCCCCCHHHH		61.2021339330
321MalonylationQLQKEVGKDVSDEKL
HHHHHHCCCCCHHHH		61.2026320211
3272-HydroxyisobutyrylationGKDVSDEKLRDYIWN
CCCCCHHHHHHHHHH		54.54-
327UbiquitinationGKDVSDEKLRDYIWN
CCCCCHHHHHHHHHH		54.5421890473
327AcetylationGKDVSDEKLRDYIWN
CCCCCHHHHHHHHHH		54.5419608861
327SuccinylationGKDVSDEKLRDYIWN
CCCCCHHHHHHHHHH		54.5421890473
327SuccinylationGKDVSDEKLRDYIWN
CCCCCHHHHHHHHHH		54.54-
331PhosphorylationSDEKLRDYIWNTLNS
CHHHHHHHHHHHHCC		11.0328152594
338PhosphorylationYIWNTLNSGRVVPGY
HHHHHHCCCCCCCCC		30.9621712546
345NitrationSGRVVPGYGHAVLRK
CCCCCCCCCCEEECC		10.32-
345PhosphorylationSGRVVPGYGHAVLRK
CCCCCCCCCCEEECC		10.3228152594
3662-HydroxyisobutyrylationCQREFALKHLPNDPM
CCHHHHHHCCCCCHH		39.40-
366UbiquitinationCQREFALKHLPNDPM
CCHHHHHHCCCCCHH		39.4019608861
366AcetylationCQREFALKHLPNDPM
CCHHHHHHCCCCCHH		39.4025825284
375AcetylationLPNDPMFKLVAQLYK
CCCCHHHHHHHHHHH		35.4819608861
375SuccinylationLPNDPMFKLVAQLYK
CCCCHHHHHHHHHHH		35.48-
375SuccinylationLPNDPMFKLVAQLYK
CCCCHHHHHHHHHHH		35.48-
381PhosphorylationFKLVAQLYKIVPNVL
HHHHHHHHHHHHHHH		6.13-
382AcetylationKLVAQLYKIVPNVLL
HHHHHHHHHHHHHHH		45.9119608861
382UbiquitinationKLVAQLYKIVPNVLL
HHHHHHHHHHHHHHH		45.9121890473
382MalonylationKLVAQLYKIVPNVLL
HHHHHHHHHHHHHHH		45.9126320211
393SuccinylationNVLLEQGKAKNPWPN
HHHHHCCCCCCCCCC		56.75-
393AcetylationNVLLEQGKAKNPWPN
HHHHHCCCCCCCCCC		56.7519608861
393SuccinylationNVLLEQGKAKNPWPN
HHHHHCCCCCCCCCC		56.75-
393UbiquitinationNVLLEQGKAKNPWPN
HHHHHCCCCCCCCCC		56.7519608861
393MalonylationNVLLEQGKAKNPWPN
HHHHHCCCCCCCCCC		56.7526320211
395"N6,N6,N6-trimethyllysine"LLEQGKAKNPWPNVD
HHHCCCCCCCCCCCC		68.01-
395UbiquitinationLLEQGKAKNPWPNVD
HHHCCCCCCCCCCCC		68.01-
395MethylationLLEQGKAKNPWPNVD
HHHCCCCCCCCCCCC		68.0128887308
450AcetylationGFPLERPKSMSTEGL
CCCCCCCCCCCCCHH		66.0823749302
450UbiquitinationGFPLERPKSMSTEGL
CCCCCCCCCCCCCHH		66.08-
450MalonylationGFPLERPKSMSTEGL
CCCCCCCCCCCCCHH		66.0826320211
450SuccinylationGFPLERPKSMSTEGL
CCCCCCCCCCCCCHH		66.0827452117
450SuccinylationGFPLERPKSMSTEGL
CCCCCCCCCCCCCHH		66.08-
451PhosphorylationFPLERPKSMSTEGLM
CCCCCCCCCCCCHHH		22.2030108239
453PhosphorylationLERPKSMSTEGLMKF
CCCCCCCCCCHHHHH		30.3330108239
454PhosphorylationERPKSMSTEGLMKFV
CCCCCCCCCHHHHHH		25.9830108239
4592-HydroxyisobutyrylationMSTEGLMKFVDSKSG
CCCCHHHHHHHCCCC		47.48-
459SuccinylationMSTEGLMKFVDSKSG
CCCCHHHHHHHCCCC		47.4821890473
459UbiquitinationMSTEGLMKFVDSKSG
CCCCHHHHHHHCCCC		47.4821890473
459AcetylationMSTEGLMKFVDSKSG
CCCCHHHHHHHCCCC		47.4823954790
459SuccinylationMSTEGLMKFVDSKSG
CCCCHHHHHHHCCCC		47.48-
463PhosphorylationGLMKFVDSKSG----
HHHHHHHCCCC----		24.3429083192
465PhosphorylationMKFVDSKSG------
HHHHHCCCC------		54.4024719451
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 CISY_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
395KMethylation

28391595
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 CISY_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CRYAB_HUMANCRYABphysical
16274233
PYRG1_HUMANCTPS1physical
22863883
IDH3A_HUMANIDH3Aphysical
26344197
ODPX_HUMANPDHXphysical
26344197
SDHA_HUMANSDHAphysical
26344197
SDHB_HUMANSDHBphysical
26344197
ZN207_HUMANZNF207physical
27173435
PA2G4_HUMANPA2G4physical
27173435
TRAP1_HUMANTRAP1physical
27173435
SND1_HUMANSND1physical
27173435
ANXA5_HUMANANXA5physical
27173435
IF2P_HUMANEIF5Bphysical
27173435
G6PI_HUMANGPIphysical
27173435
UBE2N_HUMANUBE2Nphysical
27173435
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 CISY_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-327; LYS-366; LYS-375;LYS-382 AND LYS-393, AND MASS SPECTROMETRY.

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