CCD87_HUMAN - dbPTM
CCD87_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CCD87_HUMAN
UniProt AC Q9NVE4
Protein Name Coiled-coil domain-containing protein 87
Gene Name CCDC87
Organism Homo sapiens (Human).
Sequence Length 849
Subcellular Localization
Protein Description
Protein Sequence MMEPPKPEPELQRFYHRLLRPLSLFPTRTTSPEPQKRPPQEGRILQSFPLAKLTVASLCSQVAKLLAGSGIAAGVPPEARLRLIKVILDELKCSWREPPAELSLSHKNNQKLRKRLEAYVLLSSEQLFLRYLHLLVTMSTPRGVFTESATLTRLAASLARDCTLFLTSPNVYRGLLADFQALLRAEQASGDVDKLHPVCPAGTFKLCPIPWPHSTGFAQVQCSNLNLNYLIQLSRPPEFLNEPGRMDPVKELKSIPRLKRKKPFHWLPSIGKKREIDISSSQMVSLPSYPVAPTSRASPSPFCPELRRGQSMPSLREGWRLADELGLPPLPSRPLTPLVLATESKPELTGLIVAEDLKQLIKKMKLEGTRYPPLDSGLPPLLGVVTRHPAAGHRLEELEKMLRNLQEEEASGQWDPQPPKSFPLHPQPVTITLKLRNEVVVQAAAVRVSDRNFLDSFHIEGAGALYNHLAGELDPKAIEKMDIDNFVGSTTREVYKELMSHVSSDHLHFDQGPLVEPAADKDWSTFLSSAFLRQEKQPQIINPELVGLYSQRANTLQSNTKKMPSLPSLQATKSWEKWSNKASLMNSWKTTLSVDDYFKYLTNHETDFLHVIFQMHEEEVPVEIVAPARESLEIQHPPPLLEDEEPDFVPGEWDWNTVLEHRLGAGKTPHLGEPHKILSLQKHLEQLWSVLEVPDKDQVDMTIKYSSKARLRQLPSLVNAWERALKPIQLREALLARLEWFEGQASNPNRFFKKTNLSSSHFLEENQVRSHLHRKLNLMESSLVSLLEEIELIFGEPVIFKGRPYLDKMKSDKVEMLYWLQQQRRVRHLVSALKDPHQSTLFRSSAASL
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
47PhosphorylationQEGRILQSFPLAKLT
CCCCCCCCCCHHHHH
25.9526270265
54PhosphorylationSFPLAKLTVASLCSQ
CCCHHHHHHHHHHHH
17.2026270265
57PhosphorylationLAKLTVASLCSQVAK
HHHHHHHHHHHHHHH
26.1026270265
60PhosphorylationLTVASLCSQVAKLLA
HHHHHHHHHHHHHHH
32.7426270265
103PhosphorylationREPPAELSLSHKNNQ
CCCCCHHCCCCCCHH
21.2328509920
123PhosphorylationLEAYVLLSSEQLFLR
HHHHHHHCHHHHHHH
27.89-
124PhosphorylationEAYVLLSSEQLFLRY
HHHHHHCHHHHHHHH
29.36-
131PhosphorylationSEQLFLRYLHLLVTM
HHHHHHHHHHHHHHC
10.7124719451
139PhosphorylationLHLLVTMSTPRGVFT
HHHHHHCCCCCCCCC
26.37-
140PhosphorylationHLLVTMSTPRGVFTE
HHHHHCCCCCCCCCC
13.2424719451
254PhosphorylationDPVKELKSIPRLKRK
CHHHHHHCCCHHHCC
50.9127174698
254O-linked_GlycosylationDPVKELKSIPRLKRK
CHHHHHHCCCHHHCC
50.9131492838
281PhosphorylationREIDISSSQMVSLPS
CEEEECCCCCEECCC
18.5922210691
295PhosphorylationSYPVAPTSRASPSPF
CCCCCCCCCCCCCCC
25.4522210691
311PhosphorylationPELRRGQSMPSLREG
HHHHCCCCCCCHHHH
35.1724719451
314PhosphorylationRRGQSMPSLREGWRL
HCCCCCCCHHHHHHH
31.2724719451
456PhosphorylationSDRNFLDSFHIEGAG
CCCCCHHHEEECCHH
22.3725003641
562UbiquitinationTLQSNTKKMPSLPSL
HHHHCCCCCCCCCCH
54.74-
565PhosphorylationSNTKKMPSLPSLQAT
HCCCCCCCCCCHHCC
49.7918691976
568PhosphorylationKKMPSLPSLQATKSW
CCCCCCCCHHCCCCH
38.11-
573UbiquitinationLPSLQATKSWEKWSN
CCCHHCCCCHHHHCC
57.49-
679PhosphorylationGEPHKILSLQKHLEQ
CCCHHHHHHHHHHHH
32.0224719451

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 CCD87_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CCD87_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 CCD87_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
KASH5_HUMANCCDC155physical
16189514
TRI54_HUMANTRIM54physical
25416956
USBP1_HUMANUSHBP1physical
25416956

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 CCD87_HUMAN

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Related Literatures of Post-Translational Modification

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