ANC2_HUMAN - dbPTM
ANC2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ANC2_HUMAN
UniProt AC Q9UJX6
Protein Name Anaphase-promoting complex subunit 2
Gene Name ANAPC2
Organism Homo sapiens (Human).
Sequence Length 822
Subcellular Localization
Protein Description Together with the RING-H2 protein ANAPC11, constitutes the catalytic component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C complex acts by mediating ubiquitination and subsequent degradation of target proteins: it mainly mediates the formation of 'Lys-11'-linked polyubiquitin chains and, to a lower extent, the formation of 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains. The CDC20-APC/C complex positively regulates the formation of synaptic vesicle clustering at active zone to the presynaptic membrane in postmitotic neurons. CDC20-APC/C-induced degradation of NEUROD2 drives presynaptic differentiation..
Protein Sequence MAAAVVVAEGDSDSRPGQELLVAWNTVSTGLVPPAALGLVSSRTSGAVPPKEEELRAAVEVLRGHGLHSVLEEWFVEVLQNDLQANISPEFWNAISQCENSADEPQCLLLLLDAFGLLESRLDPYLRSLELLEKWTRLGLLMGTGAQGLREEVHTMLRGVLFFSTPRTFQEMIQRLYGCFLRVYMQSKRKGEGGTDPELEGELDSRYARRRYYRLLQSPLCAGCSSDKQQCWCRQALEQFHQLSQVLHRLSLLERVSAEAVTTTLHQVTRERMEDRCRGEYERSFLREFHKWIERVVGWLGKVFLQDGPARPASPEAGNTLRRWRCHVQRFFYRIYASLRIEELFSIVRDFPDSRPAIEDLKYCLERTDQRQQLLVSLKAALETRLLHPGVNTCDIITLYISAIKALRVLDPSMVILEVACEPIRRYLRTREDTVRQIVAGLTGDSDGTGDLAVELSKTDPASLETGQDSEDDSGEPEDWVPDPVDADPGKSSSKRRSSDIISLLVSIYGSKDLFINEYRSLLADRLLHQFSFSPEREIRNVELLKLRFGEAPMHFCEVMLKDMADSRRINANIREEDEKRPAEEQPPFGVYAVILSSEFWPPFKDEKLEVPEDIRAALEAYCKKYEQLKAMRTLSWKHTLGLVTMDVELADRTLSVAVTPVQAVILLYFQDQASWTLEELSKAVKMPVALLRRRMSVWLQQGVLREEPPGTFSVIEEERPQDRDNMVLIDSDDESDSGMASQADQKEEELLLFWTYIQAMLTNLESLSLDRIYNMLRMFVVTGPALAEIDLQELQGYLQKKVRDQQLVYSAGVYRLPKNCS
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
41PhosphorylationPAALGLVSSRTSGAV
HHHHCHHCCCCCCCC		21.1024719451
134 (in isoform 2)Ubiquitination-54.5621890473
134 (in isoform 1)Ubiquitination-54.5621890473
134UbiquitinationRSLELLEKWTRLGLL
HHHHHHHHHHHHHHH		54.5621890473
188UbiquitinationLRVYMQSKRKGEGGT
HHHHHHHHCCCCCCC		41.0322817900
190 (in isoform 2)Ubiquitination-66.1221890473
190 (in isoform 1)Ubiquitination-66.1221890473
190UbiquitinationVYMQSKRKGEGGTDP
HHHHHHCCCCCCCCH		66.1221963094
195PhosphorylationKRKGEGGTDPELEGE
HCCCCCCCCHHHCCH		60.2721815630
205PhosphorylationELEGELDSRYARRRY
HHCCHHCHHHHHHHH		39.5521815630
218PhosphorylationRYYRLLQSPLCAGCS
HHHHHHCCCCCCCCC		21.5819664994
225PhosphorylationSPLCAGCSSDKQQCW
CCCCCCCCCCHHHHH		40.4230266825
226PhosphorylationPLCAGCSSDKQQCWC
CCCCCCCCCHHHHHH		53.5630266825
228UbiquitinationCAGCSSDKQQCWCRQ
CCCCCCCHHHHHHHH		44.1921963094
257PhosphorylationLSLLERVSAEAVTTT
HHHHHHHCHHHHHHH		26.9828851738
262PhosphorylationRVSAEAVTTTLHQVT
HHCHHHHHHHHHHHH		22.5528851738
263PhosphorylationVSAEAVTTTLHQVTR
HCHHHHHHHHHHHHH		22.2928851738
314PhosphorylationDGPARPASPEAGNTL
CCCCCCCCCCCCHHH		26.4229255136
320PhosphorylationASPEAGNTLRRWRCH
CCCCCCHHHHHHHHH		22.2629255136
346PhosphorylationLRIEELFSIVRDFPD
HCHHHHHHHHHCCCC		32.5721406692
351 (in isoform 2)Phosphorylation-5.1924275569
354PhosphorylationIVRDFPDSRPAIEDL
HHHCCCCCCHHHHHH		40.1622817900
377PhosphorylationQRQQLLVSLKAALET
HHHHHHHHHHHHHHH		24.91-
393PhosphorylationLLHPGVNTCDIITLY
HCCCCCCHHHHHHHH		14.7822817900
398PhosphorylationVNTCDIITLYISAIK
CCHHHHHHHHHHHHH		17.5330206219
400PhosphorylationTCDIITLYISAIKAL
HHHHHHHHHHHHHHH		5.5630206219
402PhosphorylationDIITLYISAIKALRV
HHHHHHHHHHHHHHC		15.4730206219
443PhosphorylationRQIVAGLTGDSDGTG
HHHHHHHHCCCCCCC		37.72-
459PhosphorylationLAVELSKTDPASLET
EEEEECCCCHHHCCC		43.7923403867
463PhosphorylationLSKTDPASLETGQDS
ECCCCHHHCCCCCCC		31.9323403867
466PhosphorylationTDPASLETGQDSEDD
CCHHHCCCCCCCCCC		45.4923927012
470PhosphorylationSLETGQDSEDDSGEP
HCCCCCCCCCCCCCC		34.7323927012
474PhosphorylationGQDSEDDSGEPEDWV
CCCCCCCCCCCCCCC		58.3326503892
492PhosphorylationVDADPGKSSSKRRSS
CCCCCCCCCCCCCHH		45.8423312004
493PhosphorylationDADPGKSSSKRRSSD
CCCCCCCCCCCCHHH		43.2823312004
494PhosphorylationADPGKSSSKRRSSDI
CCCCCCCCCCCHHHH		36.9523312004
498PhosphorylationKSSSKRRSSDIISLL
CCCCCCCHHHHHHHH		36.0726657352
499PhosphorylationSSSKRRSSDIISLLV
CCCCCCHHHHHHHHH		30.9030108239
503PhosphorylationRRSSDIISLLVSIYG
CCHHHHHHHHHHHHC		18.9121406692
507PhosphorylationDIISLLVSIYGSKDL
HHHHHHHHHHCCCCH		15.2921406692
509PhosphorylationISLLVSIYGSKDLFI
HHHHHHHHCCCCHHH		14.0821406692
511PhosphorylationLLVSIYGSKDLFINE
HHHHHHCCCCHHHHH		13.1622496350
532PhosphorylationDRLLHQFSFSPEREI
HHHHHHCCCCCHHHC		20.4623927012
534PhosphorylationLLHQFSFSPEREIRN
HHHHCCCCCHHHCCC		25.3422167270
546UbiquitinationIRNVELLKLRFGEAP
CCCEEEEEHHHCCCC		50.68-
562UbiquitinationHFCEVMLKDMADSRR
HHHHHHHHHHHHHHC		27.6221963094
608UbiquitinationWPPFKDEKLEVPEDI
CCCCCCCCCCCCHHH		61.1429967540
624UbiquitinationAALEAYCKKYEQLKA
HHHHHHHHHHHHHHH		45.7929967540
625UbiquitinationALEAYCKKYEQLKAM
HHHHHHHHHHHHHHH		50.92-
630UbiquitinationCKKYEQLKAMRTLSW
HHHHHHHHHHHHCCH		39.57-
645PhosphorylationKHTLGLVTMDVELAD
HHHCEEEEECHHHHC		16.8224505115
686UbiquitinationEELSKAVKMPVALLR
HHHHHHHHHHHHHHH		42.2027667366
697PhosphorylationALLRRRMSVWLQQGV
HHHHHHHHHHHHCCC		14.3428348404
712PhosphorylationLREEPPGTFSVIEEE
CCCCCCCCEEEEECC		20.6428111955
714PhosphorylationEEPPGTFSVIEEERP
CCCCCCEEEEECCCC		23.2528111955
720DimethylationFSVIEEERPQDRDNM
EEEEECCCCCCCCCE		37.14-
732PhosphorylationDNMVLIDSDDESDSG
CCEEEECCCCCCCCC		39.7122167270
736PhosphorylationLIDSDDESDSGMASQ
EECCCCCCCCCCCCC		44.0322167270
738PhosphorylationDSDDESDSGMASQAD
CCCCCCCCCCCCCCC		39.4823663014
742PhosphorylationESDSGMASQADQKEE
CCCCCCCCCCCHHHH		19.6022167270
810PhosphorylationVRDQQLVYSAGVYRL
HCCCHHHHEEEEEEC		11.0325147952
811PhosphorylationRDQQLVYSAGVYRLP
CCCHHHHEEEEEECC		15.8621815630
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 ANC2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ANC2_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 ANC2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
APC11_HUMANANAPC11physical
11739784
UBE2C_HUMANUBE2Cphysical
11739784
EP300_HUMANEP300physical
16319895
CBP_HUMANCREBBPphysical
16319895
EPHA4_HUMANEPHA4physical
21186356
GRIA1_HUMANGRIA1physical
21186356
FZR1_HUMANFZR1physical
21135578
RNF34_HUMANRNF34physical
21903591
CDC27_HUMANCDC27physical
22939629
APC1_HUMANANAPC1physical
22939629
APC5_HUMANANAPC5physical
22939629
CDC23_HUMANCDC23physical
22939629
CDC16_HUMANCDC16physical
22939629
APC4_HUMANANAPC4physical
22939629
APC7_HUMANANAPC7physical
22939629
APC10_HUMANANAPC10physical
22939629
MDM2_HUMANMDM2physical
24804778
APC1_HUMANANAPC1physical
10922056
CDC27_HUMANCDC27physical
10922056
APC4_HUMANANAPC4physical
10922056
APC5_HUMANANAPC5physical
10922056
CDC16_HUMANCDC16physical
10922056
CDC23_HUMANCDC23physical
10922056
CDC26_HUMANCDC26physical
10922056
APC7_HUMANANAPC7physical
10922056
CDC27_HUMANCDC27physical
21768287
FZR1_HUMANFZR1physical
12956947
PTTG1_HUMANPTTG1physical
12956947
UB2D2_HUMANUBE2D2physical
12956947
APC11_HUMANANAPC11physical
12956947
APC1_HUMANANAPC1physical
12956947
CDC27_HUMANCDC27physical
12956947
APC4_HUMANANAPC4physical
12956947
APC5_HUMANANAPC5physical
12956947
CDC16_HUMANCDC16physical
12956947
APC7_HUMANANAPC7physical
12956947
CDC23_HUMANCDC23physical
12956947
APC10_HUMANANAPC10physical
12956947
CDC26_HUMANCDC26physical
12956947
UBE2C_HUMANUBE2Cphysical
25825779
UBE2S_HUMANUBE2Sphysical
25306923
PRKDC_HUMANPRKDCphysical
26221070
PTTG1_HUMANPTTG1physical
27114510
CDC20_HUMANCDC20physical
27114510
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 ANC2_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-470, AND MASSSPECTROMETRY.
"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218, AND MASSSPECTROMETRY.
"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-218; SER-470 ANDSER-534, AND MASS SPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218; SER-314 ANDSER-534, AND MASS SPECTROMETRY.
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis.";
Wang B., Malik R., Nigg E.A., Korner R.;
Anal. Chem. 80:9526-9533(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-314, AND MASSSPECTROMETRY.
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218, AND MASSSPECTROMETRY.
"Mitotic regulation of the human anaphase-promoting complex byphosphorylation.";
Kraft C., Herzog F., Gieffers C., Mechtler K., Hagting A., Pines J.,Peters J.-M.;
EMBO J. 22:6598-6609(2003).
Cited for: PHOSPHORYLATION AT SER-314 AND SER-534.

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