ADCK1_HUMAN - dbPTM
ADCK1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ADCK1_HUMAN
UniProt AC Q86TW2
Protein Name Uncharacterized aarF domain-containing protein kinase 1
Gene Name ADCK1
Organism Homo sapiens (Human).
Sequence Length 530
Subcellular Localization Secreted .
Protein Description The function of this protein is not yet clear. It is not known if it has protein kinase activity and what type of substrate it would phosphorylate (Ser, Thr or Tyr)..
Protein Sequence MARKALKLASWTSMALAASGIYFYSNKYLDPNDFGAVRVGRAVATTAVISYDYLTSLKSVPYGSEEYLQLRSKSWPVFLQVHLRSARRLCELCCANRGTFIKVGQHLGALDYLLPEEYTSTLKVLHSQAPQSSMQEIRQVIREDLGKEIHDLFQSFDDTPLGTASLAQVHKAVLHDGRTVAVKVQHPKVRAQSSKDILLMEVLVLAVKQLFPEFEFMWLVDEAKKNLPLELDFLNEGRNAEKVSQMLRHFDFLKVPRIHWDLSTERVLLMEFVDGGQVNDRDYMERNKIDVNEISRHLGKMYSEMIFVNGFVHCDPHPGNVLVRKHPGTGKAEIVLLDHGLYQMLTEEFRLNYCHLWQSLIWTDMKRVKEYSQRLGAGDLYPLFACMLTARSWDSVNRGISQAPVTATEDLEIRNNAANYLPQISHLLNHVPRQMLLILKTNDLLRGIEAALGTRASASSFLNMSRCCIRALAEHKKKNTCSFFRRTQISFSEAFNLWQINLHELILRVKGLKLADRVLALICWLFPAPL
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
67PhosphorylationVPYGSEEYLQLRSKS
CCCCCHHHHHHHCCC
8.83110753941
72 (in isoform 2)Phosphorylation-39.37-
108UbiquitinationIKVGQHLGALDYLLP
EEHHCCCCHHHHHCC
23.2029967540
112PhosphorylationQHLGALDYLLPEEYT
CCCCHHHHHCCHHHH
15.8129759185
132PhosphorylationLHSQAPQSSMQEIRQ
HHCCCCCCHHHHHHH
27.0724114839
150UbiquitinationEDLGKEIHDLFQSFD
HHHHHHHHHHHHCCC
27.1529967540
176UbiquitinationVHKAVLHDGRTVAVK
HHHHHCCCCCEEEEE
44.0729967540
218UbiquitinationFPEFEFMWLVDEAKK
CCCCCCCHHHHHHHH
9.8829967540
263PhosphorylationPRIHWDLSTERVLLM
CCEECCCCCCEEEEE
26.2523532336
329PhosphorylationLVRKHPGTGKAEIVL
EEEECCCCCCEEEEE
39.7046159535
441PhosphorylationQMLLILKTNDLLRGI
HHHHHHHHHHHHHHH
30.445053929
454PhosphorylationGIEAALGTRASASSF
HHHHHHCCCCCHHHH
24.7425247763
482PhosphorylationHKKKNTCSFFRRTQI
HHCCCCCHHHHHCCC
25.9424719451

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 ADCK1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ADCK1_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 ADCK1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
EXOC5_HUMANEXOC5physical
21988832
ADCK1_HUMANADCK1physical
27499296
STML2_HUMANSTOML2physical
27499296
TOM5_HUMANTOMM5physical
27499296
MIC19_HUMANCHCHD3physical
27499296
MIC60_HUMANIMMTphysical
27499296
ATP5H_HUMANATP5Hphysical
27499296
DCMC_HUMANMLYCDphysical
27499296
CHCH2_HUMANCHCHD2physical
27499296
ECH1_HUMANECH1physical
27499296
MPPB_HUMANPMPCBphysical
27499296
ATPO_HUMANATP5Ophysical
27499296
MTX1_HUMANMTX1physical
27499296
C1QBP_HUMANC1QBPphysical
27499296
MTCH2_HUMANMTCH2physical
27499296

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 ADCK1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
Anal. Sci. 24:161-166(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-441, AND MASSSPECTROMETRY.

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