APC5_HUMAN - dbPTM
APC5_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID APC5_HUMAN
UniProt AC Q9UJX4
Protein Name Anaphase-promoting complex subunit 5
Gene Name ANAPC5
Organism Homo sapiens (Human).
Sequence Length 755
Subcellular Localization
Protein Description 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..
Protein Sequence MASVHESLYFNPMMTNGVVHANVFGIKDWVTPYKIAVLVLLNEMSRTGEGAVSLMERRRLNQLLLPLLQGPDITLSKLYKLIEESCPQLANSVQIRIKLMAEGELKDMEQFFDDLSDSFSGTEPEVHKTSVVGLFLRHMILAYSKLSFSQVFKLYTALQQYFQNGEKKTVEDADMELTSRDEGERKMEKEELDVSVREEEVSCSGPLSQKQAEFFLSQQASLLKNDETKALTPASLQKELNNLLKFNPDFAEAHYLSYLNNLRVQDVFSSTHSLLHYFDRLILTGAESKSNGEEGYGRSLRYAALNLAALHCRFGHYQQAELALQEAIRIAQESNDHVCLQHCLSWLYVLGQKRSDSYVLLEHSVKKAVHFGLPYLASLGIQSLVQQRAFAGKTANKLMDALKDSDLLHWKHSLSELIDISIAQKTAIWRLYGRSTMALQQAQMLLSMNSLEAVNAGVQQNNTESFAVALCHLAELHAEQGCFAAASEVLKHLKERFPPNSQHAQLWMLCDQKIQFDRAMNDGKYHLADSLVTGITALNSIEGVYRKAVVLQAQNQMSEAHKLLQKLLVHCQKLKNTEMVISVLLSVAELYWRSSSPTIALPMLLQALALSKEYRLQYLASETVLNLAFAQLILGIPEQALSLLHMAIEPILADGAILDKGRAMFLVAKCQVASAASYDQPKKAEALEAAIENLNEAKNYFAKVDCKERIRDVVYFQARLYHTLGKTQERNRCAMLFRQLHQELPSHGVPLINHL
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
15PhosphorylationLYFNPMMTNGVVHAN
HCCCCCCCCCEEEEE		23.6722817900
46 (in isoform 2)Ubiquitination-45.5021890473
47PhosphorylationLLNEMSRTGEGAVSL
HHHCCCCCCCCHHHH		32.0730257219
47 (in isoform 2)Ubiquitination-32.0721890473
55SulfoxidationGEGAVSLMERRRLNQ
CCCHHHHHHHHHHHH		2.6821406390
77UbiquitinationGPDITLSKLYKLIEE
CCCCCHHHHHHHHHH		59.97-
80UbiquitinationITLSKLYKLIEESCP
CCHHHHHHHHHHHCH		54.12-
103 (in isoform 2)Ubiquitination-35.6821890473
108 (in isoform 2)Ubiquitination-4.1021890473
117 (in isoform 2)Ubiquitination-62.0821890473
124 (in isoform 2)Ubiquitination-49.0721890473
167UbiquitinationQYFQNGEKKTVEDAD
HHHHCCCCCCHHHHH		55.9621906983
167 (in isoform 1)Ubiquitination-55.9621890473
168 (in isoform 2)Ubiquitination-54.2021890473
168 (in isoform 1)Ubiquitination-54.2021890473
168UbiquitinationYFQNGEKKTVEDADM
HHHCCCCCCHHHHHH		54.2021906983
169PhosphorylationFQNGEKKTVEDADME
HHCCCCCCHHHHHHH		39.9529449344
178PhosphorylationEDADMELTSRDEGER
HHHHHHHCCCHHHHH		14.3825159151
179PhosphorylationDADMELTSRDEGERK
HHHHHHCCCHHHHHH		50.8121815630
195PhosphorylationEKEELDVSVREEEVS
HHHHHCCCHHHHHCC		18.3430266825
202PhosphorylationSVREEEVSCSGPLSQ
CHHHHHCCCCCCCCH		13.0730266825
204PhosphorylationREEEVSCSGPLSQKQ
HHHHCCCCCCCCHHH		35.6230266825
210UbiquitinationCSGPLSQKQAEFFLS
CCCCCCHHHHHHHHH		48.37-
217PhosphorylationKQAEFFLSQQASLLK
HHHHHHHHHHHHHHC		18.3221712546
221PhosphorylationFFLSQQASLLKNDET
HHHHHHHHHHCCCCH		29.8725159151
224 (in isoform 1)Ubiquitination-68.5921890473
224UbiquitinationSQQASLLKNDETKAL
HHHHHHHCCCCHHCC		68.5921906983
228PhosphorylationSLLKNDETKALTPAS
HHHCCCCHHCCCHHH		25.2028122231
229 (in isoform 1)Ubiquitination-39.0721890473
229UbiquitinationLLKNDETKALTPASL
HHCCCCHHCCCHHHH		39.0721890473
232PhosphorylationNDETKALTPASLQKE
CCCHHCCCHHHHHHH		22.9730266825
235PhosphorylationTKALTPASLQKELNN
HHCCCHHHHHHHHHH		32.3230266825
238 (in isoform 1)Ubiquitination-70.2621890473
238UbiquitinationLTPASLQKELNNLLK
CCHHHHHHHHHHHHH		70.2621890473
245UbiquitinationKELNNLLKFNPDFAE
HHHHHHHHHCCCHHH		46.3821906983
245 (in isoform 1)Ubiquitination-46.3821890473
255PhosphorylationPDFAEAHYLSYLNNL
CCHHHHHHHHHHHCC		12.3729496907
257PhosphorylationFAEAHYLSYLNNLRV
HHHHHHHHHHHCCCH		22.0229496907
258PhosphorylationAEAHYLSYLNNLRVQ
HHHHHHHHHHCCCHH		15.7429496907
277PhosphorylationSTHSLLHYFDRLILT
CHHHHHHHHHHHHHC		13.72-
289UbiquitinationILTGAESKSNGEEGY
HHCCCCCCCCCCCCC		39.1721890473
289 (in isoform 1)Ubiquitination-39.1721890473
357PhosphorylationLGQKRSDSYVLLEHS
HCCCCCCCEEEEHHH		20.5628555341
364PhosphorylationSYVLLEHSVKKAVHF
CEEEEHHHHHHHHHC		26.6828555341
366 (in isoform 1)Ubiquitination-37.7221890473
366UbiquitinationVLLEHSVKKAVHFGL
EEEHHHHHHHHHCCH		37.7221906983
367UbiquitinationLLEHSVKKAVHFGLP
EEHHHHHHHHHCCHH		54.18-
393UbiquitinationQQRAFAGKTANKLMD
HHHHHCCHHHHHHHH		40.8221906983
393 (in isoform 1)Ubiquitination-40.8221890473
397UbiquitinationFAGKTANKLMDALKD
HCCHHHHHHHHHHCC		42.6021906983
397 (in isoform 1)Ubiquitination-42.6021890473
403 (in isoform 1)Ubiquitination-57.8321890473
403UbiquitinationNKLMDALKDSDLLHW
HHHHHHHCCCCCHHH		57.8321890473
413PhosphorylationDLLHWKHSLSELIDI
CCHHHCCCHHHHHHH		29.8420068231
415PhosphorylationLHWKHSLSELIDISI
HHHCCCHHHHHHHHH		33.1120068231
421PhosphorylationLSELIDISIAQKTAI
HHHHHHHHHHHHHHH		14.2320068231
524UbiquitinationDRAMNDGKYHLADSL
HHHHCCCCCCHHHHH		32.1521906983
524 (in isoform 1)Ubiquitination-32.1521890473
530PhosphorylationGKYHLADSLVTGITA
CCCCHHHHHHHHHHH		21.0929496907
545PhosphorylationLNSIEGVYRKAVVLQ
HHCCHHHHHHHHHHH		19.7729496907
547UbiquitinationSIEGVYRKAVVLQAQ
CCHHHHHHHHHHHHH		28.0421906983
547 (in isoform 1)Ubiquitination-28.0421890473
562UbiquitinationNQMSEAHKLLQKLLV
HHHHHHHHHHHHHHH		58.9221890473
562 (in isoform 1)Ubiquitination-58.9221890473
566UbiquitinationEAHKLLQKLLVHCQK
HHHHHHHHHHHHHHH		43.70-
596PhosphorylationELYWRSSSPTIALPM
HHHHHCCCHHHHHHH		27.58-
598PhosphorylationYWRSSSPTIALPMLL
HHHCCCHHHHHHHHH		22.34-
669UbiquitinationRAMFLVAKCQVASAA
HHEEHEEHHHHHHHC		20.09-
674PhosphorylationVAKCQVASAASYDQP
EEHHHHHHHCCCCCH		26.0522817900
682UbiquitinationAASYDQPKKAEALEA
HCCCCCHHHHHHHHH		60.01-
683 (in isoform 1)Ubiquitination-59.1321890473
683UbiquitinationASYDQPKKAEALEAA
CCCCCHHHHHHHHHH		59.1321906983
698UbiquitinationIENLNEAKNYFAKVD
HHHHHHHHHHHHCCC		46.106983
698 (in isoform 1)Ubiquitination-46.1021890473
703UbiquitinationEAKNYFAKVDCKERI
HHHHHHHCCCHHHHH		28.80-
703AcetylationEAKNYFAKVDCKERI
HHHHHHHCCCHHHHH		28.8026051181
726 (in isoform 1)Ubiquitination-50.5821890473
726UbiquitinationRLYHTLGKTQERNRC
HHHHHHCCHHHHHHH		50.582190698
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 APC5_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of APC5_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 APC5_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PABP1_HUMANPABPC1physical
15082755
CDC27_HUMANCDC27physical
15082755
ZBT16_HUMANZBTB16physical
16169070
CDC27_HUMANCDC27physical
22939629
APC7_HUMANANAPC7physical
22939629
CDC23_HUMANCDC23physical
22939629
CDC16_HUMANCDC16physical
22939629
TRI33_HUMANTRIM33physical
23160376
BACH1_HUMANBACH1physical
21988832
E2F1_HUMANE2F1physical
25368385
TFDP1_HUMANTFDP1physical
25368385
APC1_HUMANANAPC1physical
12956947
ANC2_HUMANANAPC2physical
12956947
APC4_HUMANANAPC4physical
12956947
APC1_HUMANANAPC1physical
26344197
APC16_HUMANANAPC16physical
26344197
APC4_HUMANANAPC4physical
26344197
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 APC5_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-217, 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-195.
"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 THR-178, AND MASSSPECTROMETRY.

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