KLHL9_HUMAN - dbPTM
KLHL9_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID KLHL9_HUMAN
UniProt AC Q9P2J3
Protein Name Kelch-like protein 9
Gene Name KLHL9
Organism Homo sapiens (Human).
Sequence Length 617
Subcellular Localization
Protein Description Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex required for mitotic progression and cytokinesis. The BCR(KLHL9-KLHL13) E3 ubiquitin ligase complex mediates the ubiquitination of AURKB and controls the dynamic behavior of AURKB on mitotic chromosomes and thereby coordinates faithful mitotic progression and completion of cytokinesis..
Protein Sequence MKVSLGNGEMGVSAHLQPCKAGTTRFFTSNTHSSVVLQGFDQLRIEGLLCDVTLVPGDGDEIFPVHRAMMASASDYFKAMFTGGMKEQDLMCIKLHGVNKVGLKKIIDFIYTAKLSLNMDNLQDTLEAASFLQILPVLDFCKVFLISGVSLDNCVEVGRIANTYNLIEVDKYVNNFILKNFPALLSTGEFLKLPFERLAFVLSSNSLKHCTELELFKAACRWLRLEDPRMDYAAKLMKNIRFPLMTPQDLINYVQTVDFMRTDNTCVNLLLEASNYQMMPYMQPVMQSDRTAIRSDSTHLVTLGGVLRQQLVVSKELRMYDERAQEWRSLAPMDAPRYQHGIAVIGNFLYVVGGQSNYDTKGKTAVDTVFRFDPRYNKWMQVASLNEKRTFFHLSALKGHLYAVGGRSAAGELATVECYNPRMNEWSYVAKMSEPHYGHAGTVYGGLMYISGGITHDTFQNELMCFDPDTDKWMQKAPMTTVRGLHCMCTVGDKLYVIGGNHFRGTSDYDDVLSCEYYSPTLDQWTPIAAMLRGQSDVGVAVFENKIYVVGGYSWNNRCMVEIVQKYDPEKDEWHKVFDLPESLGGIRACTLTVFPPEENPGSPSRESPLSAPSDHS
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
13PhosphorylationGNGEMGVSAHLQPCK
CCCCCEEEEEEEECC		12.3028387310
23PhosphorylationLQPCKAGTTRFFTSN
EEECCCCCEEEEECC		21.4723532336
24PhosphorylationQPCKAGTTRFFTSNT
EECCCCCEEEEECCC		25.2623532336
72PhosphorylationVHRAMMASASDYFKA
HHHHHHHCHHHHHHH		15.4830177828
74PhosphorylationRAMMASASDYFKAMF
HHHHHCHHHHHHHHH		30.2830177828
76PhosphorylationMMASASDYFKAMFTG
HHHCHHHHHHHHHCC		12.4130177828
86UbiquitinationAMFTGGMKEQDLMCI
HHHCCCCCHHCEEEE		56.34-
112O-linked_GlycosylationKIIDFIYTAKLSLNM
HHHHHHHHHHHCCCC		16.7030379171
171UbiquitinationYNLIEVDKYVNNFIL
ECEEEHHHHHHHHHH		57.1621890473
179UbiquitinationYVNNFILKNFPALLS
HHHHHHHHCCHHHHH		52.29-
192UbiquitinationLSTGEFLKLPFERLA
HHCCCHHHCCHHHHH		60.4821890473
232PhosphorylationLEDPRMDYAAKLMKN
CCCCCHHHHHHHHHH		10.1021406692
235UbiquitinationPRMDYAAKLMKNIRF
CCHHHHHHHHHHCCC		40.7321890473
274PhosphorylationVNLLLEASNYQMMPY
HHHHHHHCCCCCCCC		27.0522210691
276PhosphorylationLLLEASNYQMMPYMQ
HHHHHCCCCCCCCCC		8.6922210691
281PhosphorylationSNYQMMPYMQPVMQS
CCCCCCCCCCCCCCC		7.1822210691
288PhosphorylationYMQPVMQSDRTAIRS
CCCCCCCCCCCEECC		15.8022210691
315UbiquitinationRQQLVVSKELRMYDE
HHHHHHCCHHHCHHH		49.51-
320PhosphorylationVSKELRMYDERAQEW
HCCHHHCHHHHHHHH		14.2825332170
358PhosphorylationVVGGQSNYDTKGKTA
EECCCCCCCCCCCCH		30.18-
360PhosphorylationGGQSNYDTKGKTAVD
CCCCCCCCCCCCHHH		31.19-
363UbiquitinationSNYDTKGKTAVDTVF
CCCCCCCCCHHHEEE		34.56-
378UbiquitinationRFDPRYNKWMQVASL
ECCCCCCCCEEEEEC		34.8021890473
384PhosphorylationNKWMQVASLNEKRTF
CCCEEEEECCCCCEE		32.6328509920
390PhosphorylationASLNEKRTFFHLSAL
EECCCCCEEEEHHHH		41.5421406692
395PhosphorylationKRTFFHLSALKGHLY
CCEEEEHHHHCCCEE		24.0021406692
419PhosphorylationELATVECYNPRMNEW
CCCEEEEECCCCCCE		18.0717053785
476UbiquitinationDTDKWMQKAPMTTVR
CCHHHHHHCCCCCCC		38.05-
506PhosphorylationGGNHFRGTSDYDDVL
CCCCCCCCCCHHCCE		17.7325072903
507PhosphorylationGNHFRGTSDYDDVLS
CCCCCCCCCHHCCEE		36.6825072903
509PhosphorylationHFRGTSDYDDVLSCE
CCCCCCCHHCCEECE		17.5125072903
514PhosphorylationSDYDDVLSCEYYSPT
CCHHCCEECEEECCC		12.5425072903
517PhosphorylationDDVLSCEYYSPTLDQ
HCCEECEEECCCHHH		17.3625072903
518PhosphorylationDVLSCEYYSPTLDQW
CCEECEEECCCHHHC		5.9626657352
519PhosphorylationVLSCEYYSPTLDQWT
CEECEEECCCHHHCH		15.5426657352
521PhosphorylationSCEYYSPTLDQWTPI
ECEEECCCHHHCHHH		36.7125072903
526PhosphorylationSPTLDQWTPIAAMLR
CCCHHHCHHHHHHHC		10.1325072903
554PhosphorylationIYVVGGYSWNNRCMV
EEEECCCCCCCEEEE		26.9723532336
576UbiquitinationPEKDEWHKVFDLPES
CCCCCCEEECCCCHH		45.75-
591PhosphorylationLGGIRACTLTVFPPE
HCCEEEEEEEEECCC		25.2029978859
593PhosphorylationGIRACTLTVFPPEEN
CEEEEEEEEECCCCC		11.2729978859
603PhosphorylationPPEENPGSPSRESPL
CCCCCCCCCCCCCCC		22.4330266825
605PhosphorylationEENPGSPSRESPLSA
CCCCCCCCCCCCCCC		50.8330266825
608PhosphorylationPGSPSRESPLSAPSD
CCCCCCCCCCCCCCC		29.9930108239
611PhosphorylationPSRESPLSAPSDHS-
CCCCCCCCCCCCCC-		41.3330108239
614PhosphorylationESPLSAPSDHS----
CCCCCCCCCCC----		47.9030108239
617PhosphorylationLSAPSDHS-------
CCCCCCCC-------		47.0830108239
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 KLHL9_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of KLHL9_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 KLHL9_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
AURKB_HUMANAURKBphysical
19995937
AURKB_HUMANAURKBphysical
17543862
CUL3_HUMANCUL3physical
17543862
KLH13_HUMANKLHL13physical
17543862
CUL3_HUMANCUL3physical
19295130
UB2D1_HUMANUBE2D1physical
17543862
PLK1_HUMANPLK1physical
23455478
KLH22_HUMANKLHL22physical
19995937
KLH21_HUMANKLHL21physical
19995937
CUL3_HUMANCUL3physical
19995937
KLH13_HUMANKLHL13physical
19995937
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 KLHL9_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Tyrosine phosphorylated Par3 regulates epithelial tight junctionassembly promoted by EGFR signaling.";
Wang Y., Du D., Fang L., Yang G., Zhang C., Zeng R., Ullrich A.,Lottspeich F., Chen Z.;
EMBO J. 25:5058-5070(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-419, AND MASSSPECTROMETRY.

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