KLH12_HUMAN - dbPTM
KLH12_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID KLH12_HUMAN
UniProt AC Q53G59
Protein Name Kelch-like protein 12
Gene Name KLHL12
Organism Homo sapiens (Human).
Sequence Length 568
Subcellular Localization Cytoplasmic vesicle, COPII-coated vesicle .
Protein Description Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complex that acts as a negative regulator of Wnt signaling pathway and ER-Golgi transport. [PubMed: 22358839]
Protein Sequence MGGIMAPKDIMTNTHAKSILNSMNSLRKSNTLCDVTLRVEQKDFPAHRIVLAACSDYFCAMFTSELSEKGKPYVDIQGLTASTMEILLDFVYTETVHVTVENVQELLPAACLLQLKGVKQACCEFLESQLDPSNCLGIRDFAETHNCVDLMQAAEVFSQKHFPEVVQHEEFILLSQGEVEKLIKCDEIQVDSEEPVFEAVINWVKHAKKEREESLPNLLQYVRMPLLTPRYITDVIDAEPFIRCSLQCRDLVDEAKKFHLRPELRSQMQGPRTRARLGANEVLLVVGGFGSQQSPIDVVEKYDPKTQEWSFLPSITRKRRYVASVSLHDRIYVIGGYDGRSRLSSVECLDYTADEDGVWYSVAPMNVRRGLAGATTLGDMIYVSGGFDGSRRHTSMERYDPNIDQWSMLGDMQTAREGAGLVVASGVIYCLGGYDGLNILNSVEKYDPHTGHWTNVTPMATKRSGAGVALLNDHIYVVGGFDGTAHLSSVEAYNIRTDSWTTVTSMTTPRCYVGATVLRGRLYAIAGYDGNSLLSSIECYDPIIDSWEVVTSMGTQRCDAGVCVLREK
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
5Sulfoxidation---MGGIMAPKDIMT
---CCCCCCCHHHCC		6.2130846556
12PhosphorylationMAPKDIMTNTHAKSI
CCCHHHCCHHHHHHH		36.9829083192
14PhosphorylationPKDIMTNTHAKSILN
CHHHCCHHHHHHHHH		17.6529083192
18PhosphorylationMTNTHAKSILNSMNS
CCHHHHHHHHHHHHH		32.8428464451
31PhosphorylationNSLRKSNTLCDVTLR
HHHHHCCCCCEEEEE		35.5422817900
36PhosphorylationSNTLCDVTLRVEQKD
CCCCCEEEEEEECCC		8.8022817900
119UbiquitinationLLQLKGVKQACCEFL
HHHCCCHHHHHHHHH		40.63-
157 (in isoform 2)Ubiquitination-4.88-
175PhosphorylationHEEFILLSQGEVEKL
CCEEEEECCCHHHHH		32.47-
181UbiquitinationLSQGEVEKLIKCDEI
ECCCHHHHHEECCEE		61.77-
231PhosphorylationMPLLTPRYITDVIDA
CCCCCCCCCCCCCCC		14.9120071362
256UbiquitinationRDLVDEAKKFHLRPE
HHHHHHHHHHCCCHH		54.6621906983
257UbiquitinationDLVDEAKKFHLRPEL
HHHHHHHHHCCCHHH		45.09-
294UbiquitinationGGFGSQQSPIDVVEK
CCCCCCCCCCCEECC		19.0421906983
294 (in isoform 2)Ubiquitination-19.04-
295 (in isoform 2)Ubiquitination-23.59-
301UbiquitinationSPIDVVEKYDPKTQE
CCCCEECCCCCCCCC		43.2621906983
305UbiquitinationVVEKYDPKTQEWSFL
EECCCCCCCCCCCCC		61.002190698
332PhosphorylationVSLHDRIYVIGGYDG
EECCCCEEEECCCCC		6.2128152594
337PhosphorylationRIYVIGGYDGRSRLS
CEEEECCCCCCCCCC		15.2628152594
339UbiquitinationYVIGGYDGRSRLSSV
EEECCCCCCCCCCEE		22.4521906983
343UbiquitinationGYDGRSRLSSVECLD
CCCCCCCCCEEEEEE		4.7621906983
343 (in isoform 2)Ubiquitination-4.76-
446PhosphorylationILNSVEKYDPHTGHW
CHHHHHHCCCCCCCC		22.6228122231
450PhosphorylationVEKYDPHTGHWTNVT
HHHCCCCCCCCCCCC		35.8128122231
454PhosphorylationDPHTGHWTNVTPMAT
CCCCCCCCCCCCCCC		17.7128122231
462UbiquitinationNVTPMATKRSGAGVA
CCCCCCCCCCCCEEE		34.72-
500 (in isoform 2)Ubiquitination-10.01-
516PhosphorylationPRCYVGATVLRGRLY
CCCEEECEEECCEEE		17.7222985185
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 KLH12_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of KLH12_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 KLH12_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
KLH12_HUMANKLHL12physical
16189514
MED28_HUMANMED28physical
16189514
SNX20_HUMANSNX20physical
16189514
LNX1_HUMANLNX1physical
16189514
CUL3_HUMANCUL3physical
18303015
RIT1_HUMANRIT1physical
18303015
DRD4_HUMANDRD4physical
20100572
KLHL2_HUMANKLHL2physical
15383316
KLH12_HUMANKLHL12physical
25416956
ZBP1_HUMANZBP1physical
25416956
C1QT2_HUMANC1QTNF2physical
25416956
SNX20_HUMANSNX20physical
25416956
RM10_HUMANMRPL10physical
25416956
GLCTK_HUMANGLYCTKphysical
25416956
RP25L_HUMANRPP25Lphysical
25416956
TTBK2_HUMANTTBK2physical
25416956
CCBE1_HUMANCCBE1physical
25416956
SYNE4_HUMANSYNE4physical
25416956
FGD2_HUMANFGD2physical
25416956
TB10C_HUMANTBC1D10Cphysical
25416956
PEF1_HUMANPEF1physical
25416956
FUBP2_HUMANKHSRPphysical
27899653
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 KLH12_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-31 AND THR-36, AND MASSSPECTROMETRY.

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