ACACB_HUMAN - dbPTM
ACACB_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ACACB_HUMAN
UniProt AC O00763
Protein Name Acetyl-CoA carboxylase 2
Gene Name ACACB
Organism Homo sapiens (Human).
Sequence Length 2458
Subcellular Localization Mitochondrion . Nucleus . Endomembrane system. May associate with membranes.
Protein Description Catalyzes the ATP-dependent carboxylation of acetyl-CoA to malonyl-CoA. Carries out three functions: biotin carboxyl carrier protein, biotin carboxylase and carboxyltransferase. Involved in inhibition of fatty acid and glucose oxidation and enhancement of fat storage (By similarity). May play a role in regulation of mitochondrial fatty acid oxidation through malonyl-CoA-dependent inhibition of carnitine palmitoyltransferase 1 (By similarity)..
Protein Sequence MVLLLCLSCLIFSCLTFSWLKIWGKMTDSKPITKSKSEANLIPSQEPFPASDNSGETPQRNGEGHTLPKTPSQAEPASHKGPKDAGRRRNSLPPSHQKPPRNPLSSSDAAPSPELQANGTGTQGLEATDTNGLSSSARPQGQQAGSPSKEDKKQANIKRQLMTNFILGSFDDYSSDEDSVAGSSRESTRKGSRASLGALSLEAYLTTGEAETRVPTMRPSMSGLHLVKRGREHKKLDLHRDFTVASPAEFVTRFGGDRVIEKVLIANNGIAAVKCMRSIRRWAYEMFRNERAIRFVVMVTPEDLKANAEYIKMADHYVPVPGGPNNNNYANVELIVDIAKRIPVQAVWAGWGHASENPKLPELLCKNGVAFLGPPSEAMWALGDKIASTVVAQTLQVPTLPWSGSGLTVEWTEDDLQQGKRISVPEDVYDKGCVKDVDEGLEAAERIGFPLMIKASEGGGGKGIRKAESAEDFPILFRQVQSEIPGSPIFLMKLAQHARHLEVQILADQYGNAVSLFGRDCSIQRRHQKIVEEAPATIAPLAIFEFMEQCAIRLAKTVGYVSAGTVEYLYSQDGSFHFLELNPRLQVEHPCTEMIADVNLPAAQLQIAMGVPLHRLKDIRLLYGESPWGVTPISFETPSNPPLARGHVIAARITSENPDEGFKPSSGTVQELNFRSSKNVWGYFSVAATGGLHEFADSQFGHCFSWGENREEAISNMVVALKELSIRGDFRTTVEYLINLLETESFQNNDIDTGWLDYLIAEKVQAEKPDIMLGVVCGALNVADAMFRTCMTDFLHSLERGQVLPADSLLNLVDVELIYGGVKYILKVARQSLTMFVLIMNGCHIEIDAHRLNDGGLLLSYNGNSYTTYMKEEVDSYRITIGNKTCVFEKENDPTVLRSPSAGKLTQYTVEDGGHVEAGSSYAEMEVMKMIMTLNVQERGRVKYIKRPGAVLEAGCVVARLELDDPSKVHPAEPFTGELPAQQTLPILGEKLHQVFHSVLENLTNVMSGFCLPEPVFSIKLKEWVQKLMMTLRHPSLPLLELQEIMTSVAGRIPAPVEKSVRRVMAQYASNITSVLCQFPSQQIATILDCHAATLQRKADREVFFINTQSIVQLVQRYRSGIRGYMKTVVLDLLRRYLRVEHHFQQAHYDKCVINLREQFKPDMSQVLDCIFSHAQVAKKNQLVIMLIDELCGPDPSLSDELISILNELTQLSKSEHCKVALRARQILIASHLPSYELRHNQVESIFLSAIDMYGHQFCPENLKKLILSETTIFDVLPTFFYHANKVVCMASLEVYVRRGYIAYELNSLQHRQLPDGTCVVEFQFMLPSSHPNRMTVPISITNPDLLRHSTELFMDSGFSPLCQRMGAMVAFRRFEDFTRNFDEVISCFANVPKDTPLFSEARTSLYSEDDCKSLREEPIHILNVSIQCADHLEDEALVPILRTFVQSKKNILVDYGLRRITFLIAQEKEFPKFFTFRARDEFAEDRIYRHLEPALAFQLELNRMRNFDLTAVPCANHKMHLYLGAAKVKEGVEVTDHRFFIRAIIRHSDLITKEASFEYLQNEGERLLLEAMDELEVAFNNTSVRTDCNHIFLNFVPTVIMDPFKIEESVRYMVMRYGSRLWKLRVLQAEVKINIRQTTTGSAVPIRLFITNESGYYLDISLYKEVTDSRSGNIMFHSFGNKQGPQHGMLINTPYVTKDLLQAKRFQAQTLGTTYIYDFPEMFRQALFKLWGSPDKYPKDILTYTELVLDSQGQLVEMNRLPGGNEVGMVAFKMRFKTQEYPEGRDVIVIGNDITFRIGSFGPGEDLLYLRASEMARAEGIPKIYVAANSGARIGMAEEIKHMFHVAWVDPEDPHKGFKYLYLTPQDYTRISSLNSVHCKHIEEGGESRYMITDIIGKDDGLGVENLRGSGMIAGESSLAYEEIVTISLVTCRAIGIGAYLVRLGQRVIQVENSHIILTGASALNKVLGREVYTSNNQLGGVQIMHYNGVSHITVPDDFEGVYTILEWLSYMPKDNHSPVPIITPTDPIDREIEFLPSRAPYDPRWMLAGRPHPTLKGTWQSGFFDHGSFKEIMAPWAQTVVTGRARLGGIPVGVIAVETRTVEVAVPADPANLDSEAKIIQQAGQVWFPDSAYKTAQAVKDFNREKLPLMIFANWRGFSGGMKDMYDQVLKFGAYIVDGLRQYKQPILIYIPPYAELRGGSWVVIDATINPLCIEMYADKESRGGVLEPEGTVEIKFRKKDLIKSMRRIDPAYKKLMEQLGEPDLSDKDRKDLEGRLKAREDLLLPIYHQVAVQFADFHDTPGRMLEKGVISDILEWKTARTFLYWRLRRLLLEDQVKQEILQASGELSHVHIQSMLRRWFVETEGAVKAYLWDNNQVVVQWLEQHWQAGDGPRSTIRENITYLKHDSVLKTIRGLVEENPEVAVDCVIYLSQHISPAERAQVVHLLSTMDSPAST
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
35PhosphorylationDSKPITKSKSEANLI
CCCCCCCCHHHCCCC
32.5324972180
37PhosphorylationKPITKSKSEANLIPS
CCCCCCHHHCCCCCC
49.3728258704
44PhosphorylationSEANLIPSQEPFPAS
HHCCCCCCCCCCCCC
39.9321902226
70PhosphorylationEGHTLPKTPSQAEPA
CCCCCCCCCCCCCCC
26.6623312004
72PhosphorylationHTLPKTPSQAEPASH
CCCCCCCCCCCCCCC
47.4528258704
91PhosphorylationDAGRRRNSLPPSHQK
CCCCCCCCCCHHHCC
40.2029116813
95PhosphorylationRRNSLPPSHQKPPRN
CCCCCCHHHCCCCCC
36.2923312004
106PhosphorylationPPRNPLSSSDAAPSP
CCCCCCCCCCCCCCH
39.6624275569
107PhosphorylationPRNPLSSSDAAPSPE
CCCCCCCCCCCCCHH
28.0824275569
169PhosphorylationMTNFILGSFDDYSSD
HHHHHHCCCCCCCCC
23.27113299501
175PhosphorylationGSFDDYSSDEDSVAG
CCCCCCCCCCCCCCC
38.50-
192PhosphorylationRESTRKGSRASLGAL
CCCCCCCCHHHHCCE
27.9228258704
195PhosphorylationTRKGSRASLGALSLE
CCCCCHHHHCCEEEE
26.6528258704
200PhosphorylationRASLGALSLEAYLTT
HHHHCCEEEEEEECC
24.5128258704
204PhosphorylationGALSLEAYLTTGEAE
CCEEEEEEECCCCCC
8.6625072903
206PhosphorylationLSLEAYLTTGEAETR
EEEEEEECCCCCCCC
21.7824043423
207PhosphorylationSLEAYLTTGEAETRV
EEEEEECCCCCCCCC
30.3524043423
212PhosphorylationLTTGEAETRVPTMRP
ECCCCCCCCCCCCCC
43.9724043423
216PhosphorylationEAETRVPTMRPSMSG
CCCCCCCCCCCCCCH
23.9724043423
220PhosphorylationRVPTMRPSMSGLHLV
CCCCCCCCCCHHCHH
18.4024972180
222PhosphorylationPTMRPSMSGLHLVKR
CCCCCCCCHHCHHCC
42.4125072903
243PhosphorylationLDLHRDFTVASPAEF
CCCCCCCCCCCHHHH
21.3223186163
246PhosphorylationHRDFTVASPAEFVTR
CCCCCCCCHHHHHHH
21.9525850435
262UbiquitinationGGDRVIEKVLIANNG
CCCHHEEEEEEECCC
31.0829967540
274UbiquitinationNNGIAAVKCMRSIRR
CCCCHHHHHHHHHHH
20.00-
454AcetylationIGFPLMIKASEGGGG
HCCCEEEEECCCCCC
31.7120167786
469PhosphorylationKGIRKAESAEDFPIL
CCCCCCCCCCCCCEE
41.6424275569
663UbiquitinationENPDEGFKPSSGTVQ
CCCCCCCCCCCCCEE
55.6421906983
663 (in isoform 2)Ubiquitination-55.6421906983
663 (in isoform 1)Ubiquitination-55.6421906983
663AcetylationENPDEGFKPSSGTVQ
CCCCCCCCCCCCCEE
55.6425953088
722UbiquitinationSNMVVALKELSIRGD
HHHHHHHHHHCCCCC
47.04-
725PhosphorylationVVALKELSIRGDFRT
HHHHHHHCCCCCHHH
16.0124719451
753PhosphorylationFQNNDIDTGWLDYLI
HCCCCCCCCHHHHHH
30.50-
808PhosphorylationGQVLPADSLLNLVDV
CCCCCHHHHHHCCCH
36.5446157487
860PhosphorylationNDGGLLLSYNGNSYT
CCCCEEEEECCCCCE
19.2729083192
861PhosphorylationDGGLLLSYNGNSYTT
CCCEEEEECCCCCEE
27.3629083192
865PhosphorylationLLSYNGNSYTTYMKE
EEEECCCCCEEEEEC
25.8429083192
866PhosphorylationLSYNGNSYTTYMKEE
EEECCCCCEEEEECC
13.7030873031
867PhosphorylationSYNGNSYTTYMKEEV
EECCCCCEEEEECCC
15.9829083192
868PhosphorylationYNGNSYTTYMKEEVD
ECCCCCEEEEECCCC
17.2429083192
869PhosphorylationNGNSYTTYMKEEVDS
CCCCCEEEEECCCCE
9.8229083192
880PhosphorylationEVDSYRITIGNKTCV
CCCEEEEEECCEEEE
17.5228258704
895PhosphorylationFEKENDPTVLRSPSA
EEECCCCCEEECCCC
34.7369213021
929BiotinylationYAEMEVMKMIMTLNV
CHHHHHHHHHHHCCH
30.3718247344
929N6-biotinyllysineYAEMEVMKMIMTLNV
CHHHHHHHHHHHCCH
30.37-
933PhosphorylationEVMKMIMTLNVQERG
HHHHHHHHCCHHHCC
12.3124114839
1074PhosphorylationQYASNITSVLCQFPS
HHHHCHHHHHCCCCH
14.8622210691
1081PhosphorylationSVLCQFPSQQIATIL
HHHCCCCHHHHHHHH
35.6922210691
1094PhosphorylationILDCHAATLQRKADR
HHHHHHHHHHHHCCC
24.9822210691
1137PhosphorylationVLDLLRRYLRVEHHF
HHHHHHHHHHHHHHH
7.7629083192
1149PhosphorylationHHFQQAHYDKCVINL
HHHHHHHHHHHEEEH
21.8029083192
1292PhosphorylationNKVVCMASLEVYVRR
CEEEEEEEEEEEECC
9.7429759185
1340PhosphorylationNRMTVPISITNPDLL
CCEEEEEEECCHHHH
19.799474075
1342PhosphorylationMTVPISITNPDLLRH
EEEEEEECCHHHHHH
33.6320166139
1350PhosphorylationNPDLLRHSTELFMDS
CHHHHHHHHHHHHCC
19.6923312004
1351PhosphorylationPDLLRHSTELFMDSG
HHHHHHHHHHHHCCC
30.4923312004
1357PhosphorylationSTELFMDSGFSPLCQ
HHHHHHCCCCHHHHH
29.9225072903
1360PhosphorylationLFMDSGFSPLCQRMG
HHHCCCCHHHHHHHC
22.0823312004
1405PhosphorylationLFSEARTSLYSEDDC
CCCHHHHHCCCHHHH
21.5422798277
1413UbiquitinationLYSEDDCKSLREEPI
CCCHHHHHHHCCCCE
60.56-
1414PhosphorylationYSEDDCKSLREEPIH
CCHHHHHHHCCCCEE
38.7023312004
1450AcetylationRTFVQSKKNILVDYG
HHHHHCCCCEEHHCC
55.2419820785
1456PhosphorylationKKNILVDYGLRRITF
CCCEEHHCCHHHHHE
15.5821253578
1462PhosphorylationDYGLRRITFLIAQEK
HCCHHHHHEEEECCC
15.5820068231
1473UbiquitinationAQEKEFPKFFTFRAR
ECCCCCCCCEEEECC
59.43-
1489PhosphorylationEFAEDRIYRHLEPAL
HHHHHHHHHHHHHHH
7.907947665
1557PhosphorylationDLITKEASFEYLQNE
HCCCHHHHHHHHHHH
21.5020068231
1560PhosphorylationTKEASFEYLQNEGER
CHHHHHHHHHHHHHH
16.1620068231
1618PhosphorylationVRYMVMRYGSRLWKL
HHHHHHHCCCCCEEE
11.0123828894
1620PhosphorylationYMVMRYGSRLWKLRV
HHHHHCCCCCEEEEE
18.4423828894
1641PhosphorylationINIRQTTTGSAVPIR
EEEEECCCCCCCEEE
32.3115632253
1658PhosphorylationITNESGYYLDISLYK
EECCCCEEEEEEEEE
11.0421720203
1664PhosphorylationYYLDISLYKEVTDSR
EEEEEEEEEEECCCC
9.7912308941
1694PhosphorylationQHGMLINTPYVTKDL
CCCEEECCCCCCHHH
14.7022210691
1696PhosphorylationGMLINTPYVTKDLLQ
CEEECCCCCCHHHHH
20.7924043423
1698PhosphorylationLINTPYVTKDLLQAK
EECCCCCCHHHHHHH
17.0122210691
1826PhosphorylationAEGIPKIYVAANSGA
HCCCCEEEEEECCCC
7.0821406692
1831PhosphorylationKIYVAANSGARIGMA
EEEEEECCCCCCCCH
29.1530278072
1877PhosphorylationTRISSLNSVHCKHIE
CCCCCCCCEECEECC
20.6623403867
1891PhosphorylationEEGGESRYMITDIIG
CCCCCCCEEEEEEEC
11.3630174305
2081PhosphorylationIMAPWAQTVVTGRAR
HHHCCCCEEECCCHH
14.8120068231
2084PhosphorylationPWAQTVVTGRARLGG
CCCCEEECCCHHHCC
19.3320068231
2161PhosphorylationFANWRGFSGGMKDMY
EECCCCCCCCHHHHH
36.9428258704
2268PhosphorylationQLGEPDLSDKDRKDL
HHCCCCCCHHHHHCH
50.4226270265
2324PhosphorylationLEWKTARTFLYWRLR
HHHHHHHHHHHHHHH
18.6128258704
2327PhosphorylationKTARTFLYWRLRRLL
HHHHHHHHHHHHHHH
5.5828258704
2347PhosphorylationKQEILQASGELSHVH
HHHHHHHCCCCCHHH
21.6046157481
2404PhosphorylationSTIRENITYLKHDSV
CHHHHHHEEECHHHH
34.0923532336
2405PhosphorylationTIRENITYLKHDSVL
HHHHHHEEECHHHHH
15.2324719451
2410PhosphorylationITYLKHDSVLKTIRG
HEEECHHHHHHHHHH
29.1224719451
2432PhosphorylationVAVDCVIYLSQHISP
HHHHHEEEHHHCCCH
4.6626434552
2438PhosphorylationIYLSQHISPAERAQV
EEHHHCCCHHHHHHH
18.8826434552
2451PhosphorylationQVVHLLSTMDSPAST
HHHHHHHCCCCCCCC
25.6021815630
2454PhosphorylationHLLSTMDSPAST---
HHHHCCCCCCCC---
16.1427134283
2458PhosphorylationTMDSPAST-------
CCCCCCCC-------
44.7446157493

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
222SPhosphorylationKinaseAMPKQ9Y478
Uniprot
222SPhosphorylationKinasePRKAA1Q13131
GPS
222SPhosphorylationKinaseAMPK-FAMILY-GPS
222SPhosphorylationKinaseAMPK_GROUP-PhosphoELM
-KUbiquitinationE3 ubiquitin ligaseCOP1Q8NHY2
PMID:22199232
-KUbiquitinationE3 ubiquitin ligaseDET1Q7L5Y6
PMID:16794074
-KUbiquitinationE3 ubiquitin ligaseDET1#COP1Q7L5Y6#Q8NHY2
PMID:22199232

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
222SPhosphorylation

12488245

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 ACACB_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of ACACB_HUMAN !!

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
DB00173Adenine
DB00121Biotin
Regulatory Network of ACACB_HUMAN

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Related Literatures of Post-Translational Modification

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