KCTD5_HUMAN - dbPTM
KCTD5_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID KCTD5_HUMAN
UniProt AC Q9NXV2
Protein Name BTB/POZ domain-containing protein KCTD5
Gene Name KCTD5
Organism Homo sapiens (Human).
Sequence Length 234
Subcellular Localization Cytoplasm, cytosol. Nucleus. Predominantly cytoplasmic, translocated to the nucleus upon interaction with Rep proteins.
Protein Description Its interaction with CUL3 suggests that it may act as a substrate adapter in some E3 ligase complex. Does not affect the function of Kv channel Kv2.1/KCNB1, Kv1.2/KCNA2, Kv4.2/KCND2 and Kv3.4/KCNC4..
Protein Sequence MAENHCELLSPARGGIGAGLGGGLCRRCSAGLGALAQRPGSVSKWVRLNVGGTYFLTTRQTLCRDPKSFLYRLCQADPDLDSDKDETGAYLIDRDPTYFGPVLNYLRHGKLVINKDLAEEGVLEEAEFYNITSLIKLVKDKIRERDSKTSQVPVKHVYRVLQCQEEELTQMVSTMSDGWKFEQLVSIGSSYNYGNEDQAEFLCVVSKELHNTPYGTASEPSEKAKILQERGSRM
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
2Acetylation------MAENHCELL
------CCCCCHHCC		26.7120068231
10PhosphorylationENHCELLSPARGGIG
CCCHHCCCCCCCCCC		29.1929255136
13MethylationCELLSPARGGIGAGL
HHCCCCCCCCCCCCC		47.45115388941
26MethylationGLGGGLCRRCSAGLG
CCCCHHHHHHHCCHH		47.91115388947
29PhosphorylationGGLCRRCSAGLGALA
CHHHHHHHCCHHHHH		24.4530266825
41PhosphorylationALAQRPGSVSKWVRL
HHHCCCCCCCCEEEE		26.3726552605
43PhosphorylationAQRPGSVSKWVRLNV
HCCCCCCCCEEEEEC		23.6126552605
57PhosphorylationVGGTYFLTTRQTLCR
CCCEEEEECCHHHHC		15.2720068231
67UbiquitinationQTLCRDPKSFLYRLC
HHHHCCHHHHHHHHH		59.1233845483
98PhosphorylationLIDRDPTYFGPVLNY
ECCCCCCCHHHHHHH		16.3620068231
115UbiquitinationHGKLVINKDLAEEGV
CCCEEECHHHHHCCC		42.8929967540
133PhosphorylationAEFYNITSLIKLVKD
HHHCCHHHHHHHHHH		25.0524719451
147PhosphorylationDKIRERDSKTSQVPV
HHHHHCCCCCCCCCH		44.0118491316
148UbiquitinationKIRERDSKTSQVPVK
HHHHCCCCCCCCCHH		57.3921906983
155UbiquitinationKTSQVPVKHVYRVLQ
CCCCCCHHHHHHHHH		22.6827667366
191PhosphorylationLVSIGSSYNYGNEDQ
EEECCCCCCCCCHHH		17.69-
193PhosphorylationSIGSSYNYGNEDQAE
ECCCCCCCCCHHHHE		17.07-
223UbiquitinationTASEPSEKAKILQER
CCCCHHHHHHHHHHH		60.3521906983
223AcetylationTASEPSEKAKILQER
CCCCHHHHHHHHHHH		60.3525953088
225UbiquitinationSEPSEKAKILQERGS
CCHHHHHHHHHHHHC		55.8322817900
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 KCTD5_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of KCTD5_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 KCTD5_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CUL3_HUMANCUL3physical
18573101
KCTD5_HUMANKCTD5physical
18573101
KCTD5_HUMANKCTD5physical
19361449
GORS2_HUMANGORASP2physical
19361449
NEK6_HUMANNEK6physical
21988832
AAKB2_HUMANPRKAB2physical
21988832
NXF1_HUMANNXF1physical
21988832
ZN711_HUMANZNF711physical
26188516
MCM7_HUMANMCM7physical
26188516
F193B_HUMANFAM193Bphysical
26188516
NHRF2_HUMANSLC9A3R2physical
27173435
CU002_HUMANC21orf2physical
27173435
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 KCTD5_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-10, AND MASS SPECTROMETRY.
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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-10, AND MASS SPECTROMETRY.

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