ANR52_HUMAN - dbPTM
ANR52_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ANR52_HUMAN
UniProt AC Q8NB46
Protein Name Serine/threonine-protein phosphatase 6 regulatory ankyrin repeat subunit C
Gene Name ANKRD52
Organism Homo sapiens (Human).
Sequence Length 1076
Subcellular Localization
Protein Description Putative regulatory subunit of protein phosphatase 6 (PP6) that may be involved in the recognition of phosphoprotein substrates..
Protein Sequence MGILSITDQPPLVQAIFSRDVEEVRSLLSQKENINVLDQERRTPLHAAAYVGDVPILQLLLMSGANVNAKDTLWLTPLHRAAASRNEKVLGLLLAHSADVNARDKLWQTPLHVAAANRATKCAEALAPLLSSLNVADRSGRSALHHAVHSGHLETVNLLLNKGASLNVCDKKERQPLHWAAFLGHLEVLKLLVARGADLGCKDRKGYGLLHTAAASGQIEVVKYLLRMGAEIDEPNAFGNTALHIACYLGQDAVAIELVNAGANVNQPNDKGFTPLHVAAVSTNGALCLELLVNNGADVNYQSKEGKSPLHMAAIHGRFTRSQILIQNGSEIDCADKFGNTPLHVAARYGHELLISTLMTNGADTARRGIHDMFPLHLAVLFGFSDCCRKLLSSGQLYSIVSSLSNEHVLSAGFDINTPDNLGRTCLHAAASGGNVECLNLLLSSGADLRRRDKFGRTPLHYAAANGSYQCAVTLVTAGAGVNEADCKGCSPLHYAAASDTYRRAEPHTPSSHDAEEDEPLKESRRKEAFFCLEFLLDNGADPSLRDRQGYTAVHYAAAYGNRQNLELLLEMSFNCLEDVESTIPVSPLHLAAYNGHCEALKTLAETLVNLDVRDHKGRTALFLATERGSTECVEVLTAHGASALIKERKRKWTPLHAAAASGHTDSLHLLIDSGERADITDVMDAYGQTPLMLAIMNGHVDCVHLLLEKGSTADAADLRGRTALHRGAVTGCEDCLAALLDHDAFVLCRDFKGRTPIHLASACGHTAVLRTLLQAALSTDPLDAGVDYSGYSPMHWASYTGHEDCLELLLEHSPFSYLEGNPFTPLHCAVINNQDSTTEMLLGALGAKIVNSRDAKGRTPLHAAAFADNVSGLRMLLQHQAEVNATDHTGRTALMTAAENGQTAAVEFLLYRGKADLTVLDENKNTALHLACSKGHEKCALMILAETQDLGLINATNSALQMPLHIAARNGLASVVQALLSHGATVLAVDEEGHTPALACAPNKDVADCLALILSTMKPFPPKDAVSPFSFSLLKNCSIAAAKTVGGCGALPHGASCPYSQERPGAIGLDGCYSE
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---MGILSITDQPPL
---CCCCCCCCCCHH
22.8646164377
7Phosphorylation-MGILSITDQPPLVQ
-CCCCCCCCCCHHHH
25.8046164401
18PhosphorylationPLVQAIFSRDVEEVR
HHHHHHHCCCHHHHH
22.8146164371
26PhosphorylationRDVEEVRSLLSQKEN
CCHHHHHHHHHCHHC
38.5524719451
29PhosphorylationEEVRSLLSQKENINV
HHHHHHHHCHHCCCC
44.49101546263
31UbiquitinationVRSLLSQKENINVLD
HHHHHHCHHCCCCCC
49.72-
43PhosphorylationVLDQERRTPLHAAAY
CCCHHCCCHHHHHHH
36.1027762562
50PhosphorylationTPLHAAAYVGDVPIL
CHHHHHHHCCCHHHH
10.5527762562
105UbiquitinationADVNARDKLWQTPLH
CCCCCCHHHHCCHHH
46.18-
109PhosphorylationARDKLWQTPLHVAAA
CCHHHHCCHHHHHHH
19.0868725167
121UbiquitinationAAANRATKCAEALAP
HHHHHHHHHHHHHHH
30.38-
171UbiquitinationASLNVCDKKERQPLH
CCCCCCCHHCCCCHH
51.94-
205UbiquitinationDLGCKDRKGYGLLHT
CCCCCCCCCCCHHHH
67.62-
307UbiquitinationNYQSKEGKSPLHMAA
CCCCCCCCCCCHHHH
50.41-
337UbiquitinationSEIDCADKFGNTPLH
CEEECCHHHCCCHHH
36.32-
398PhosphorylationLLSSGQLYSIVSSLS
HHHCCCHHHHHHHHC
6.6130461833
488UbiquitinationGVNEADCKGCSPLHY
CCCHHHCCCCCHHHH
64.60-
501PhosphorylationHYAAASDTYRRAEPH
HHHHCCCCCHHCCCC
19.2122250773
509PhosphorylationYRRAEPHTPSSHDAE
CHHCCCCCCCCCCCC
35.2622250783
511PhosphorylationRAEPHTPSSHDAEED
HCCCCCCCCCCCCCC
41.2720068231
512PhosphorylationAEPHTPSSHDAEEDE
CCCCCCCCCCCCCCC
26.9620068231
522UbiquitinationAEEDEPLKESRRKEA
CCCCCCCCHHHHHHH
65.44-
607PhosphorylationALKTLAETLVNLDVR
HHHHHHHHHHCCCCC
30.3319845377
647UbiquitinationHGASALIKERKRKWT
CCHHHHHHHHHCCCC
52.93-
654PhosphorylationKERKRKWTPLHAAAA
HHHHCCCCHHHHHHH
21.0046164389
681PhosphorylationSGERADITDVMDAYG
CCCCCCHHHHHHHHC
24.0846164395
723PhosphorylationAADLRGRTALHRGAV
HHHHCCCHHHHCCCC
36.0726546556
893PhosphorylationATDHTGRTALMTAAE
CCCCCCHHHHHHHHH
26.0320068231
897PhosphorylationTGRTALMTAAENGQT
CCHHHHHHHHHHCCE
24.4620068231
904PhosphorylationTAAENGQTAAVEFLL
HHHHHCCEEEEEHHH
20.2720068231
912PhosphorylationAAVEFLLYRGKADLT
EEEEHHHHCCCCCEE
21.3320068231
915UbiquitinationEFLLYRGKADLTVLD
EHHHHCCCCCEEEEE
29.72-
925UbiquitinationLTVLDENKNTALHLA
EEEEECCCCCHHHHH
54.34-
935UbiquitinationALHLACSKGHEKCAL
HHHHHHCCCCHHHHE
65.26-
1016PhosphorylationDCLALILSTMKPFPP
HHHHHHHHCCCCCCC
21.3346164365
1017PhosphorylationCLALILSTMKPFPPK
HHHHHHHCCCCCCCH
26.2646164383
1028PhosphorylationFPPKDAVSPFSFSLL
CCCHHCCCCCCHHHH
23.1929255136
1031PhosphorylationKDAVSPFSFSLLKNC
HHCCCCCCHHHHCCC
19.8125850435
1033PhosphorylationAVSPFSFSLLKNCSI
CCCCCCHHHHCCCHH
31.4325850435
1036MethylationPFSFSLLKNCSIAAA
CCCHHHHCCCHHHCC
62.29-
1036UbiquitinationPFSFSLLKNCSIAAA
CCCHHHHCCCHHHCC
62.29-
1044UbiquitinationNCSIAAAKTVGGCGA
CCHHHCCEECCCCCC
38.73-
1045PhosphorylationCSIAAAKTVGGCGAL
CHHHCCEECCCCCCC
21.4727080861
1057PhosphorylationGALPHGASCPYSQER
CCCCCCCCCCCCCCC
21.8827080861
1060PhosphorylationPHGASCPYSQERPGA
CCCCCCCCCCCCCCC
27.5825159151
1061PhosphorylationHGASCPYSQERPGAI
CCCCCCCCCCCCCCC
15.6525159151
1074PhosphorylationAIGLDGCYSE-----
CCCCCCCCCC-----
22.7423663014
1075PhosphorylationIGLDGCYSE------
CCCCCCCCC------
40.6925159151

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 ANR52_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ANR52_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 ANR52_HUMAN !!

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

Oops, there are no PPI records of ANR52_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
There are no disease associations of PTM sites.
Regulatory Network of ANR52_HUMAN

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Related Literatures of Post-Translational Modification
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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1028, 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-1028, AND MASSSPECTROMETRY.

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