KLDC4_HUMAN - dbPTM
KLDC4_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID KLDC4_HUMAN
UniProt AC Q8TBB5
Protein Name Kelch domain-containing protein 4
Gene Name KLHDC4
Organism Homo sapiens (Human).
Sequence Length 520
Subcellular Localization
Protein Description
Protein Sequence MGKKGKKEKKGRGAEKTAAKMEKKVSKRSRKEEEDLEALIAHFQTLDAKRTQTVELPCPPPSPRLNASLSVHPEKDELILFGGEYFNGQKTFLYNELYVYNTRKDTWTKVDIPSPPPRRCAHQAVVVPQGGGQLWVFGGEFASPNGEQFYHYKDLWVLHLATKTWEQVKSTGGPSGRSGHRMVAWKRQLILFGGFHESTRDYIYYNDVYAFNLDTFTWSKLSPSGTGPTPRSGCQMSVTPQGGIVVYGGYSKQRVKKDVDKGTRHSDMFLLKPEDGREDKWVWTRMNPSGVKPTPRSGFSVAMAPNHQTLFFGGVCDEEEEESLSGEFFNDLYFYDATRNRWFEGQLKGPKSEKKKRRRGRKEEPEGGSRPACGGAGTQGPVQLVKEVVAEDGTVVTIKQVLTAPGSAGQPRSEDEDSLEEAGSPAPGPCPRSNAMLAVKHGVLYVYGGMFEAGDRQVTLSDLHCLDLHRMEAWKALVEMDPETQEWLEETDSEEDSEEVEGAEGGVDDEDSGEESGAED
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
3Ubiquitination-----MGKKGKKEKK
-----CCCCCCCCCC		57.9924816145
4Acetylation----MGKKGKKEKKG
----CCCCCCCCCCC		70.957214705
9AcetylationGKKGKKEKKGRGAEK
CCCCCCCCCCCCHHH		70.21130403
10AcetylationKKGKKEKKGRGAEKT
CCCCCCCCCCCHHHH		55.73130407
20UbiquitinationGAEKTAAKMEKKVSK
CHHHHHHHHHHHHHH		45.1624816145
26PhosphorylationAKMEKKVSKRSRKEE
HHHHHHHHHHHHCHH		31.09-
31UbiquitinationKVSKRSRKEEEDLEA
HHHHHHHCHHHHHHH		71.3829967540
49 (in isoform 3)Ubiquitination-56.4921906983
49 (in isoform 1)Ubiquitination-56.4921906983
49UbiquitinationHFQTLDAKRTQTVEL
HHHHHCCCCCCEEEE		56.4921963094
62PhosphorylationELPCPPPSPRLNASL
EECCCCCCCCCCEEE		28.5528450419
68PhosphorylationPSPRLNASLSVHPEK
CCCCCCEEEEECCCC		21.8025159151
71UbiquitinationRLNASLSVHPEKDEL
CCCEEEEECCCCCEE		12.0821963094
75UbiquitinationSLSVHPEKDELILFG
EEEECCCCCEEEEEC		62.0422817900
76UbiquitinationLSVHPEKDELILFGG
EEECCCCCEEEEECC		55.0322817900
80UbiquitinationPEKDELILFGGEYFN
CCCCEEEEECCCEEC		5.2224816145
111UbiquitinationKDTWTKVDIPSPPPR
CCCCEECCCCCCCCC		48.9524816145
112UbiquitinationDTWTKVDIPSPPPRR
CCCEECCCCCCCCCC		3.9921963094
114PhosphorylationWTKVDIPSPPPRRCA
CEECCCCCCCCCCCC		50.8225159151
169UbiquitinationTKTWEQVKSTGGPSG
CCCHHHHHHCCCCCC		41.8321963094
195UbiquitinationQLILFGGFHESTRDY
EEEEECCCCCCCCCE		6.2221963094
199UbiquitinationFGGFHESTRDYIYYN
ECCCCCCCCCEEEEC		25.2822817900
200UbiquitinationGGFHESTRDYIYYND
CCCCCCCCCEEEECC		43.9722817900
204UbiquitinationESTRDYIYYNDVYAF
CCCCCEEEECCEEEE		7.0324816145
221UbiquitinationDTFTWSKLSPSGTGP
CEEEEECCCCCCCCC		8.3121963094
222PhosphorylationTFTWSKLSPSGTGPT
EEEEECCCCCCCCCC		22.2822985185
224PhosphorylationTWSKLSPSGTGPTPR
EEECCCCCCCCCCCC		45.6822985185
225UbiquitinationWSKLSPSGTGPTPRS
EECCCCCCCCCCCCC		37.7722817900
226UbiquitinationSKLSPSGTGPTPRSG
ECCCCCCCCCCCCCC		44.3022817900
226PhosphorylationSKLSPSGTGPTPRSG
ECCCCCCCCCCCCCC		44.3023312004
229PhosphorylationSPSGTGPTPRSGCQM
CCCCCCCCCCCCCCE		32.4522985185
230UbiquitinationPSGTGPTPRSGCQMS
CCCCCCCCCCCCCEE		31.4124816145
235UbiquitinationPTPRSGCQMSVTPQG
CCCCCCCCEEEECCC		30.6124816145
252UbiquitinationVVYGGYSKQRVKKDV
EEECCCCCCEEECCC		33.3721963094
256UbiquitinationGYSKQRVKKDVDKGT
CCCCCEEECCCCCCC		45.5022817900
257UbiquitinationYSKQRVKKDVDKGTR
CCCCEEECCCCCCCC		61.1921963094
261UbiquitinationRVKKDVDKGTRHSDM
EEECCCCCCCCCCCE		63.1324816145
262UbiquitinationVKKDVDKGTRHSDMF
EECCCCCCCCCCCEE		24.4222817900
266UbiquitinationVDKGTRHSDMFLLKP
CCCCCCCCCEEEECC		27.7224816145
289PhosphorylationVWTRMNPSGVKPTPR
EEEECCCCCCCCCCC		51.7428509920
292UbiquitinationRMNPSGVKPTPRSGF
ECCCCCCCCCCCCCC		46.8524816145
294PhosphorylationNPSGVKPTPRSGFSV
CCCCCCCCCCCCCEE		26.1429083192
297UbiquitinationGVKPTPRSGFSVAMA
CCCCCCCCCCEEEEC		45.4524816145
305UbiquitinationGFSVAMAPNHQTLFF
CCEEEECCCCCEEEE		26.2529967540
329UbiquitinationESLSGEFFNDLYFYD
HHCCCCCCCCCEEEE		6.3929967540
331UbiquitinationLSGEFFNDLYFYDAT
CCCCCCCCCEEEECC		37.2729967540
342UbiquitinationYDATRNRWFEGQLKG
EECCCCCCCCCCCCC		10.1329967540
348UbiquitinationRWFEGQLKGPKSEKK
CCCCCCCCCCHHHHH		66.34-
355UbiquitinationKGPKSEKKKRRRGRK
CCCHHHHHHHHCCCC		47.6729967540
356PhosphorylationGPKSEKKKRRRGRKE
CCHHHHHHHHCCCCC		63.3033259812
362UbiquitinationKKRRRGRKEEPEGGS
HHHHCCCCCCCCCCC		70.0729967540
368UbiquitinationRKEEPEGGSRPACGG
CCCCCCCCCCCCCCC		20.8629967540
382PhosphorylationGAGTQGPVQLVKEVV
CCCCCCHHHHEEEEE		9.8233259812
386UbiquitinationQGPVQLVKEVVAEDG
CCHHHHEEEEECCCC		54.0829967540
399UbiquitinationDGTVVTIKQVLTAPG
CCCEEEEEEEEECCC		25.6229967540
403PhosphorylationVTIKQVLTAPGSAGQ
EEEEEEEECCCCCCC		31.7630278072
407PhosphorylationQVLTAPGSAGQPRSE
EEEECCCCCCCCCCC		28.3223401153
413PhosphorylationGSAGQPRSEDEDSLE
CCCCCCCCCCCCHHH		56.9619664994
418PhosphorylationPRSEDEDSLEEAGSP
CCCCCCCHHHHCCCC		35.3229255136
424PhosphorylationDSLEEAGSPAPGPCP
CHHHHCCCCCCCCCC		25.5722167270
433PhosphorylationAPGPCPRSNAMLAVK
CCCCCCCHHHEEEEE		17.6826074081
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 KLDC4_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of KLDC4_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 KLDC4_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
KDM1A_HUMANKDM1Aphysical
23455924
SUV91_HUMANSUV39H1physical
23455924
SUV92_HUMANSUV39H2physical
23455924
CEP76_HUMANCEP76physical
25416956
RS19_HUMANRPS19physical
26344197
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 KLDC4_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-413 AND SER-418, ANDMASS SPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-413 AND SER-418, ANDMASS SPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-413 AND SER-418, ANDMASS SPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-413 AND SER-418, ANDMASS SPECTROMETRY.

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