KLH15_HUMAN - dbPTM
KLH15_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID KLH15_HUMAN
UniProt AC Q96M94
Protein Name Kelch-like protein 15
Gene Name KLHL15
Organism Homo sapiens (Human).
Sequence Length 604
Subcellular Localization Nucleus .
Protein Description Substrate-specific adapter for CUL3 E3 ubiquitin-protein ligase complex. [PubMed: 14528312 Acts as an adapter for CUL3 to target the serine/threonine-protein phosphatase 2A (PP2A) subunit PPP2R5B for ubiquitination and subsequent proteasomal degradation, thus promoting exchange with other regulatory subunits]
Protein Sequence MAGDVEGFCSSIHDTSVSAGFRALYEEGLLLDVTLVIEDHQFQAHKALLATQSDYFRIMFTADMRERDQDKIHLKGLTATGFSHVLQFMYYGTIELSMNTVHEILQAAMYVQLIEVVKFCCSFLLAKICLENCAEIMRLLDDFGVNIEGVREKLDTFLLDNFVPLMSRPDFLSYLSFEKLMSYLDNDHLSRFPEIELYEAVQSWLRHDRRRWRHTDTIIQNIRFCLMTPTSVFEKVKTSEFYRYSRQLRYEVDQALNYFQNVHQQPLLDMKSSRIRSAKPQTTVFRGMIGHSMVNSKILLLKKPRVWWELEGPQVPLRPDCLAIVNNFVFLLGGEELGPDGEFHASSKVFRYDPRQNSWLQMADMSVPRSEFAVGVIGKFIYAVAGRTRDETFYSTERYDITNDKWEFVDPYPVNKYGHEGTVLNNKLFITGGITSSSTSKQVCVFDPSKEGTIEQRTRRTQVVTNCWENKSKMNYARCFHKMISYNGKLYVFGGVCVILRASFESQGCPSTEVYNPETDQWTILASMPIGRSGHGVTVLDKQIMVLGGLCYNGHYSDSILTFDPDENKWKEDEYPRMPCKLDGLQVCNLHFPDYVLDEVRRCN
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
55PhosphorylationLLATQSDYFRIMFTA
HHHCCCCEEEEEEEC
10.45-
217PhosphorylationRRWRHTDTIIQNIRF
HHHCCHHHHHHHHHH
22.57-
237UbiquitinationTSVFEKVKTSEFYRY
CHHHHHHCHHHHHHH
58.35-
271UbiquitinationQQPLLDMKSSRIRSA
CCCCCCCCCHHHHCC
44.9721906983
279UbiquitinationSSRIRSAKPQTTVFR
CHHHHCCCCCCEECC
38.62-
282PhosphorylationIRSAKPQTTVFRGMI
HHCCCCCCEECCHHC
33.1929759185
283PhosphorylationRSAKPQTTVFRGMIG
HCCCCCCEECCHHCC
16.6429759185
292PhosphorylationFRGMIGHSMVNSKIL
CCHHCCHHHHCCEEE
21.1529759185
296PhosphorylationIGHSMVNSKILLLKK
CCHHHHCCEEEEEEC
15.0629759185
358PhosphorylationRYDPRQNSWLQMADM
EECCCCCCEEHHCCC
22.33-
366PhosphorylationWLQMADMSVPRSEFA
EEHHCCCCCCHHHHH
29.5330631047
392PhosphorylationAGRTRDETFYSTERY
HCCCCCCCCCCCEEE
31.96-
396PhosphorylationRDETFYSTERYDITN
CCCCCCCCEEEECCC
17.07-
405UbiquitinationRYDITNDKWEFVDPY
EEECCCCCEEECCCC
51.172190698
450UbiquitinationVCVFDPSKEGTIEQR
EEEECCCCCCCHHHH
66.60-
458PhosphorylationEGTIEQRTRRTQVVT
CCCHHHHHHCEEEEE
24.9728555341
471UbiquitinationVTNCWENKSKMNYAR
EECHHCCCCCCCHHH
39.68-
473UbiquitinationNCWENKSKMNYARCF
CHHCCCCCCCHHHHH
32.54-
581UbiquitinationEYPRMPCKLDGLQVC
CCCCCCCCCCCEEEE
43.68-

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 KLH15_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of KLH15_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 KLH15_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
2ABB_HUMANPPP2R2Bphysical
23135275
KLH15_HUMANKLHL15physical
23135275
PP2AA_HUMANPPP2CAphysical
23135275
2AAA_HUMANPPP2R1Aphysical
23135275
ELP5_HUMANELP5physical
28514442
CACB1_HUMANCACNB1physical
28514442
CUL3_HUMANCUL3physical
27561354
CTIP_HUMANRBBP8physical
27561354

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 KLH15_HUMAN

loading...

Related Literatures of Post-Translational Modification

TOP