WDR19_HUMAN - dbPTM
WDR19_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID WDR19_HUMAN
UniProt AC Q8NEZ3
Protein Name WD repeat-containing protein 19
Gene Name WDR19
Organism Homo sapiens (Human).
Sequence Length 1342
Subcellular Localization Cell projection, cilium . Cytoplasm, cytoskeleton, cilium basal body . Cell projection, cilium, photoreceptor outer segment . Localizes to photoreceptor connecting cilia, to the base of motile cilia in brain ependymal cells and to the base of and alo
Protein Description Component of the IFT complex A (IFT-A), a complex required for retrograde ciliary transport. [PubMed: 20889716 Involved in cilia function and/or assembly (By similarity Associates with the BBSome complex to mediate ciliary transport (By similarity]
Protein Sequence MKRIFSLLEKTWLGAPIQFAWQKTSGNYLAVTGADYIVKIFDRHGQKRSEINLPGNCVAMDWDKDGDVLAVIAEKSSCIYLWDANTNKTSQLDNGMRDQMSFLLWSKVGSFLAVGTVKGNLLIYNHQTSRKIPVLGKHTKRITCGCWNAENLLALGGEDKMITVSNQEGDTIRQTQVRSEPSNMQFFLMKMDDRTSAAESMISVVLGKKTLFFLNLNEPDNPADLEFQQDFGNIVCYNWYGDGRIMIGFSCGHFVVISTHTGELGQEIFQARNHKDNLTSIAVSQTLNKVATCGDNCIKIQDLVDLKDMYVILNLDEENKGLGTLSWTDDGQLLALSTQRGSLHVFLTKLPILGDACSTRIAYLTSLLEVTVANPVEGELPITVSVDVEPNFVAVGLYHLAVGMNNRAWFYVLGENAVKKLKDMEYLGTVASICLHSDYAAALFEGKVQLHLIESEILDAQEERETRLFPAVDDKCRILCHALTSDFLIYGTDTGVVQYFYIEDWQFVNDYRHPVSVKKIFPDPNGTRLVFIDEKSDGFVYCPVNDATYEIPDFSPTIKGVLWENWPMDKGVFIAYDDDKVYTYVFHKDTIQGAKVILAGSTKVPFAHKPLLLYNGELTCQTQSGKVNNIYLSTHGFLSNLKDTGPDELRPMLAQNLMLKRFSDAWEMCRILNDEAAWNELARACLHHMEVEFAIRVYRRIGNVGIVMSLEQIKGIEDYNLLAGHLAMFTNDYNLAQDLYLASSCPIAALEMRRDLQHWDSALQLAKHLAPDQIPFISKEYAIQLEFAGDYVNALAHYEKGITGDNKEHDEACLAGVAQMSIRMGDIRRGVNQALKHPSRVLKRDCGAILENMKQFSEAAQLYEKGLYYDKAASVYIRSKNWAKVGDLLPHVSSPKIHLQYAKAKEADGRYKEAVVAYENAKQWQSVIRIYLDHLNNPEKAVNIVRETQSLDGAKMVARFFLQLGDYGSAIQFLVMSKCNNEAFTLAQQHNKMEIYADIIGSEDTTNEDYQSIALYFEGEKRYLQAGKFFLLCGQYSRALKHFLKCPSSEDNVAIEMAIETVGQAKDELLTNQLIDHLLGENDGMPKDAKYLFRLYMALKQYREAAQTAIIIAREEQSAGNYRNAHDVLFSMYAELKSQKIKIPSEMATNLMILHSYILVKIHVKNGDHMKGARMLIRVANNISKFPSHIVPILTSTVIECHRAGLKNSAFSFAAMLMRPEYRSKIDAKYKKKIEGMVRRPDISEIEEATTPCPFCKFLLPECELLCPGCKNSIPYCIATGRHMLKDDWTVCPHCDFPALYSELKIMLNTESTCPMCSERLNAAQLKKISDCTQYLRTEEEL
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
6Phosphorylation--MKRIFSLLEKTWL
--CCHHHHHHHHHCC
29.6724719451
28PhosphorylationWQKTSGNYLAVTGAD
EEECCCCEEEEECCC
10.28-
36PhosphorylationLAVTGADYIVKIFDR
EEEECCCEEEEEEHH
13.69-
89PhosphorylationWDANTNKTSQLDNGM
EECCCCCCCCCCCCH
24.6322210691
90PhosphorylationDANTNKTSQLDNGMR
ECCCCCCCCCCCCHH
30.2922210691
110PhosphorylationLLWSKVGSFLAVGTV
HHHHCCCCEEEEEEE
21.7822210691
179PhosphorylationIRQTQVRSEPSNMQF
EEEEEECCCCCCCEE
55.8124719451
182PhosphorylationTQVRSEPSNMQFFLM
EEECCCCCCCEEEEE
40.6624719451
275UbiquitinationIFQARNHKDNLTSIA
HHHHHCCCCCCHHHH
52.43-
519UbiquitinationRHPVSVKKIFPDPNG
CCCEEEEEEECCCCC
47.63-
536PhosphorylationLVFIDEKSDGFVYCP
EEEEECCCCCEEEEE
40.7022468782
541PhosphorylationEKSDGFVYCPVNDAT
CCCCCEEEEECCCEE
6.7022468782
548PhosphorylationYCPVNDATYEIPDFS
EEECCCEEEECCCCC
25.2622468782
644PhosphorylationFLSNLKDTGPDELRP
HHHCCCCCCHHHHHH
49.37-
761PhosphorylationRDLQHWDSALQLAKH
HHHHCHHHHHHHHHH
26.2024247654
836UbiquitinationRGVNQALKHPSRVLK
HHHHHHHHCHHHHHH
57.39-
854UbiquitinationGAILENMKQFSEAAQ
HHHHHHHHHHHHHHH
60.83-
857PhosphorylationLENMKQFSEAAQLYE
HHHHHHHHHHHHHHH
24.6730243723
865UbiquitinationEAAQLYEKGLYYDKA
HHHHHHHCCCCCCCC
40.43-
871UbiquitinationEKGLYYDKAASVYIR
HCCCCCCCCEEEEEE
29.72-
893PhosphorylationGDLLPHVSSPKIHLQ
HHCCCCCCCCCCHHE
37.5825159151
894PhosphorylationDLLPHVSSPKIHLQY
HCCCCCCCCCCHHEE
29.1725159151
911PhosphorylationAKEADGRYKEAVVAY
HHHCCCCCEEEEEEC
20.7918083107
912UbiquitinationKEADGRYKEAVVAYE
HHCCCCCEEEEEECC
37.52-
918PhosphorylationYKEAVVAYENAKQWQ
CEEEEEECCCHHHHH
9.71-
940UbiquitinationDHLNNPEKAVNIVRE
HHCCCHHHHHHHHHH
59.91-
955UbiquitinationTQSLDGAKMVARFFL
HCCCCHHHHHHHHHH
39.16-
1102PhosphorylationLYMALKQYREAAQTA
HHHHHHHHHHHHHHE
14.6122210691
1108PhosphorylationQYREAAQTAIIIARE
HHHHHHHHEEEEEEH
18.3329978859
1118PhosphorylationIIAREEQSAGNYRNA
EEEEHHHCCCCCCCH
41.2329978859
1122PhosphorylationEEQSAGNYRNAHDVL
HHHCCCCCCCHHHHH
12.3429978859
1230PhosphorylationRSKIDAKYKKKIEGM
HHHCCHHHHHHHCCC
29.75-
1233MalonylationIDAKYKKKIEGMVRR
CCHHHHHHHCCCCCC
41.6726320211
1273PhosphorylationLCPGCKNSIPYCIAT
ECCCCCCCCCCCEEC
15.50-
1276PhosphorylationGCKNSIPYCIATGRH
CCCCCCCCCEECCCC
8.53-
1328UbiquitinationLNAAQLKKISDCTQY
CCHHHHHHHHHHHHH
56.91-

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 WDR19_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of WDR19_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 WDR19_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
IF122_HUMANIFT122physical
27173435
WDR35_HUMANWDR35physical
27173435
IFT43_HUMANIFT43physical
27173435
TT21B_HUMANTTC21Bphysical
27173435
PFKAP_HUMANPFKPphysical
27173435
SCO1_HUMANSCO1physical
27173435

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
614378Cranioectodermal dysplasia 4 (CED4)
614376Short-rib thoracic dysplasia 5 with or without polydactyly (SRTD5)
614377Nephronophthisis 13 (NPHP13)
616307Senior-Loken syndrome 8 (SLSN8)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of WDR19_HUMAN

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Related Literatures of Post-Translational Modification

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