KCD17_HUMAN - dbPTM
KCD17_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID KCD17_HUMAN
UniProt AC Q8N5Z5
Protein Name BTB/POZ domain-containing protein KCTD17
Gene Name KCTD17
Organism Homo sapiens (Human).
Sequence Length 321
Subcellular Localization Cytoplasm .
Protein Description Is a positive regulator of ciliogenesis, playing a crucial role in the initial steps of axoneme extension. It acts as a substrate-adapter for CUL3-RING ubiquitin ligase complexes which mediate the ubiquitination and subsequent proteasomal degradation of TCHP, a protein involved in ciliogenesis down-regulation. [PubMed: 25270598 May be involved in endoplasmic reticulum calcium ion homeostasis]
Protein Sequence MQTPRPAMRMEAGEAAPPAGAGGRAAGGWGKWVRLNVGGTVFLTTRQTLCREQKSFLSRLCQGEELQSDRDETGAYLIDRDPTYFGPILNFLRHGKLVLDKDMAEEGVLEEAEFYNIGPLIRIIKDRMEEKDYTVTQVPPKHVYRVLQCQEEELTQMVSTMSDGWRFEQLVNIGSSYNYGSEDQAEFLCVVSKELHSTPNGLSSESSRKTKSTEEQLEEQQQQEEEVEEVEVEQVQVEADAQEKAQSSQDPANLFSLPPLPPPPLPAGGSRPHPLRPEAELAVRASPRPLARPQSCHPCCYKPEAPGCEAPDHLQGLGVPI
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
3Phosphorylation-----MQTPRPAMRM
-----CCCCCCCCCC
21.7029759185
31UbiquitinationRAAGGWGKWVRLNVG
CCCCCCCCEEEEECC
35.69-
54UbiquitinationQTLCREQKSFLSRLC
HHHHHHHHHHHHHHH
38.12-
58PhosphorylationREQKSFLSRLCQGEE
HHHHHHHHHHHCCCC
22.6124719451
96UbiquitinationLNFLRHGKLVLDKDM
HHHHHCCCEEECHHH
29.33-
101UbiquitinationHGKLVLDKDMAEEGV
CCCEEECHHHHHCCC
45.29-
133PhosphorylationDRMEEKDYTVTQVPP
HHHHCCCCEEEECCH
17.7427642862
134PhosphorylationRMEEKDYTVTQVPPK
HHHCCCCEEEECCHH
27.49-
136PhosphorylationEEKDYTVTQVPPKHV
HCCCCEEEECCHHHH
18.95-
203PhosphorylationHSTPNGLSSESSRKT
HCCCCCCCCHHHHHC
33.20-
204PhosphorylationSTPNGLSSESSRKTK
CCCCCCCCHHHHHCC
46.6828555341
206PhosphorylationPNGLSSESSRKTKST
CCCCCCHHHHHCCCH
37.0728555341
207PhosphorylationNGLSSESSRKTKSTE
CCCCCHHHHHCCCHH
33.47-
246 (in isoform 2)Phosphorylation-55.4722210691

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 KCD17_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of KCD17_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 KCD17_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RWDD4_HUMANRWDD4physical
16189514
LNX1_HUMANLNX1physical
16189514
NUD18_HUMANNUDT18physical
16189514
KCD17_HUMANKCTD17physical
16189514
LRC18_HUMANLRRC18physical
16189514
SUV92_HUMANSUV39H2physical
23455924
ACD11_HUMANACAD11physical
26186194
RECQ4_HUMANRECQL4physical
26186194
CYTSA_HUMANSPECC1Lphysical
26186194
POLK_HUMANPOLKphysical
26186194
PI51A_HUMANPIP5K1Aphysical
26186194
NEB1_HUMANPPP1R9Aphysical
26186194
KCTD2_HUMANKCTD2physical
26186194
KCTD5_HUMANKCTD5physical
26186194
ZN687_HUMANZNF687physical
26186194
CK5P1_HUMANCDK5RAP1physical
26186194
MRCKA_HUMANCDC42BPAphysical
26186194
FRMD6_HUMANFRMD6physical
26186194
RPOM_HUMANPOLRMTphysical
26186194
PLD1_HUMANPLD1physical
26186194
CBX4_HUMANCBX4physical
26186194
TFAM_HUMANTFAMphysical
26186194
MTMR6_HUMANMTMR6physical
26186194
PKCB1_HUMANZMYND8physical
26186194
DUS11_HUMANDUSP11physical
26186194
DBR1_HUMANDBR1physical
26186194
KC1D_HUMANCSNK1Dphysical
26186194
THAP9_HUMANTHAP9physical
26186194
CERK1_HUMANCERKphysical
26186194
CU002_HUMANC21orf2physical
26186194
MTMR9_HUMANMTMR9physical
26186194
IF1AX_HUMANEIF1AXphysical
26186194
PTN4_HUMANPTPN4physical
26186194
ZN696_HUMANZNF696physical
26186194
MPLKI_HUMANMPLKIPphysical
26186194
PCBP3_HUMANPCBP3physical
26186194
CTC1_HUMANCTC1physical
26186194
CTU2_HUMANCTU2physical
26186194
REPI1_HUMANREPIN1physical
26186194
RBX1_HUMANRBX1physical
25270598
CUL3_HUMANCUL3physical
25270598
TCHP_HUMANTCHPphysical
25270598
UB2D1_HUMANUBE2D1physical
25270598
POLK_HUMANPOLKphysical
28514442
KCTD2_HUMANKCTD2physical
28514442
PKCB1_HUMANZMYND8physical
28514442
KCTD5_HUMANKCTD5physical
28514442
RPOM_HUMANPOLRMTphysical
28514442
ZN687_HUMANZNF687physical
28514442
MRCKA_HUMANCDC42BPAphysical
28514442
THAP9_HUMANTHAP9physical
28514442
PTN4_HUMANPTPN4physical
28514442
MTMR9_HUMANMTMR9physical
28514442
CBX4_HUMANCBX4physical
28514442
CERK1_HUMANCERKphysical
28514442
MTMR6_HUMANMTMR6physical
28514442
ACD11_HUMANACAD11physical
28514442
CU002_HUMANC21orf2physical
28514442
CTC1_HUMANCTC1physical
28514442
REPI1_HUMANREPIN1physical
28514442
PCBP3_HUMANPCBP3physical
28514442
PLD1_HUMANPLD1physical
28514442
NEB1_HUMANPPP1R9Aphysical
28514442
RECQ4_HUMANRECQL4physical
28514442
PI51A_HUMANPIP5K1Aphysical
28514442
TYW3_HUMANTYW3physical
28514442
ZN696_HUMANZNF696physical
28514442
MPLKI_HUMANMPLKIPphysical
28514442
PP1RA_HUMANPPP1R10physical
28514442
FRMD6_HUMANFRMD6physical
28514442

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of KCD17_HUMAN

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Related Literatures of Post-Translational Modification

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