KTU_HUMAN - dbPTM
KTU_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID KTU_HUMAN
UniProt AC Q9NVR5
Protein Name Protein kintoun {ECO:0000255|HAMAP-Rule:MF_03069}
Gene Name DNAAF2 {ECO:0000255|HAMAP-Rule:MF_03069}
Organism Homo sapiens (Human).
Sequence Length 837
Subcellular Localization Cytoplasm . Localizes in the apical cytoplasm around the gamma-tubulin-positive pericentriolar region, not in the cilia.
Protein Description Required for cytoplasmic pre-assembly of axonemal dyneins, thereby playing a central role in motility in cilia and flagella. Involved in pre-assembly of dynein arm complexes in the cytoplasm before intraflagellar transport loads them for the ciliary compartment..
Protein Sequence MAKAAASSSLEDLDLSGEEVQRLTSAFQDPEFRRMFSQYAEELTDPENRRRYEAEITALERERGVEVRFVHPEPGHVLRTSLDGARRCFVNVCSNALVGAPSSRPGSGGDRGAAPGSHWSLPYSLAPGREYAGRSSSRYMVYDVVFHPDALALARRHEGFRQMLDATALEAVEKQFGVKLDRRNAKTLKAKYKGTPEAAVLRTPLPGVIPARPDGEPKGPLPDFPYPYQYPAAPGPRAPSPPEAALQPAPTEPRYSVVQRHHVDLQDYRCSRDSAPSPVPHELVITIELPLLRSAEQAALEVTRKLLCLDSRKPDYRLRLSLPYPVDDGRGKAQFNKARRQLVVTLPVVLPAARREPAVAVAAAAPEESADRSGTDGQACASAREGEAGPARSRAEDGGHDTCVAGAAGSGVTTLGDPEVAPPPAAAGEERVPKPGEQDLSRHAGSPPGSVEEPSPGGENSPGGGGSPCLSSRSLAWGSSAGRESARGDSSVETREESEGTGGQRSACAMGGPGTKSGEPLCPPLLCNQDKETLTLLIQVPRIQPQSLQGDLNPLWYKLRFSAQDLVYSFFLQFAPENKLSTTEPVISISSNNAVIELAKSPESHGHWREWYYGVNNDSLEERLFVNEENVNEFLEEVLSSPFKQSMSLTPPLIEVLQVTDNKIQINAKLQECSNSDQLQGKEERVNEESHLTEKEYIEHCNTPTTDSDSSIAVKALQIDSFGLVTCFQQESLDVSQMILGKSQQPESKMQSEFIKEKSATCSNEEKDNLNESVITEEKETDGDHLSSLLNKTTVHNIPGFDSIKETNMQDGSVQVIKDHVTNCAFSFQNSLLYDLD
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
24O-linked_GlycosylationGEEVQRLTSAFQDPE
HHHHHHHHHHHCCHH
21.87OGP
25O-linked_GlycosylationEEVQRLTSAFQDPEF
HHHHHHHHHHCCHHH
31.51OGP
52PhosphorylationDPENRRRYEAEITAL
CHHHHHHHHHHHHHH
20.06-
102PhosphorylationNALVGAPSSRPGSGG
CCCCCCCCCCCCCCC
38.1427251275
103PhosphorylationALVGAPSSRPGSGGD
CCCCCCCCCCCCCCC
41.2427251275
107PhosphorylationAPSSRPGSGGDRGAA
CCCCCCCCCCCCCCC
42.1427251275
167PhosphorylationFRQMLDATALEAVEK
HHHHHHHHHHHHHHH
31.29-
192PhosphorylationAKTLKAKYKGTPEAA
CHHHHHHHCCCCCCE
21.3624719451
195PhosphorylationLKAKYKGTPEAAVLR
HHHHHCCCCCCEEEC
17.5024719451
240PhosphorylationAPGPRAPSPPEAALQ
CCCCCCCCCCHHHCC
52.6926657352
268PhosphorylationHHVDLQDYRCSRDSA
CCCCHHHHCCCCCCC
10.68-
345PhosphorylationARRQLVVTLPVVLPA
HHHHHEEEECEECHH
20.19-
446PhosphorylationDLSRHAGSPPGSVEE
HHHHHCCCCCCCCCC
28.8028450419
450PhosphorylationHAGSPPGSVEEPSPG
HCCCCCCCCCCCCCC
31.9328450419
455PhosphorylationPGSVEEPSPGGENSP
CCCCCCCCCCCCCCC
39.1823090842
461PhosphorylationPSPGGENSPGGGGSP
CCCCCCCCCCCCCCC
22.1823927012
467PhosphorylationNSPGGGGSPCLSSRS
CCCCCCCCCCCCCCC
18.7323927012
471PhosphorylationGGGSPCLSSRSLAWG
CCCCCCCCCCCCCCC
30.3523663014
472PhosphorylationGGSPCLSSRSLAWGS
CCCCCCCCCCCCCCC
16.9723663014
485PhosphorylationGSSAGRESARGDSSV
CCCCCCHHHCCCCCC
23.16-
498PhosphorylationSVETREESEGTGGQR
CCCCHHHCCCCCCCC
36.25-
501PhosphorylationTREESEGTGGQRSAC
CHHHCCCCCCCCCCC
33.80-
558 (in isoform 2)Ubiquitination-22.9221890473
558UbiquitinationDLNPLWYKLRFSAQD
CCCHHHHHHHHCHHH
22.9221890473
558 (in isoform 1)Ubiquitination-22.9221890473
558UbiquitinationDLNPLWYKLRFSAQD
CCCHHHHHHHHCHHH
22.9221890473
640PhosphorylationEFLEEVLSSPFKQSM
HHHHHHHCCCHHHCC
40.9318691976
641PhosphorylationFLEEVLSSPFKQSMS
HHHHHHCCCHHHCCC
30.1425159151
646PhosphorylationLSSPFKQSMSLTPPL
HCCCHHHCCCCCCCE
15.7823403867
648PhosphorylationSPFKQSMSLTPPLIE
CCHHHCCCCCCCEEE
34.0522199227
650PhosphorylationFKQSMSLTPPLIEVL
HHHCCCCCCCEEEEE
18.6321815630
674PhosphorylationNAKLQECSNSDQLQG
HHHHHHCCCCHHHCC
38.3226074081
676PhosphorylationKLQECSNSDQLQGKE
HHHHCCCCHHHCCHH
15.5026074081
697PhosphorylationSHLTEKEYIEHCNTP
CCCCHHHHHHHCCCC
23.7628450419
703PhosphorylationEYIEHCNTPTTDSDS
HHHHHCCCCCCCCCC
27.6625159151
705PhosphorylationIEHCNTPTTDSDSSI
HHHCCCCCCCCCCCH
40.9928450419
706PhosphorylationEHCNTPTTDSDSSIA
HHCCCCCCCCCCCHH
34.4128450419
708PhosphorylationCNTPTTDSDSSIAVK
CCCCCCCCCCCHHHE
36.9827251275
710PhosphorylationTPTTDSDSSIAVKAL
CCCCCCCCCHHHEEE
27.8327251275
711PhosphorylationPTTDSDSSIAVKALQ
CCCCCCCCHHHEEEE
21.4027251275
731UbiquitinationLVTCFQQESLDVSQM
CEEEEECCCCCHHHH
42.3529967540
744UbiquitinationQMILGKSQQPESKMQ
HHHHCCCCCCCHHHH
67.3529967540
759PhosphorylationSEFIKEKSATCSNEE
HHHHHHHHCCCCHHH
29.8728102081
761PhosphorylationFIKEKSATCSNEEKD
HHHHHHCCCCHHHHC
24.4528102081
763PhosphorylationKEKSATCSNEEKDNL
HHHHCCCCHHHHCCC
42.8128102081
773PhosphorylationEKDNLNESVITEEKE
HHCCCCCCCCCCCHH
20.1125159151
776PhosphorylationNLNESVITEEKETDG
CCCCCCCCCCHHCCC
35.6220068231
779UbiquitinationESVITEEKETDGDHL
CCCCCCCHHCCCHHH
60.7329967540
781PhosphorylationVITEEKETDGDHLSS
CCCCCHHCCCHHHHH
57.2421712546
787PhosphorylationETDGDHLSSLLNKTT
HCCCHHHHHHHHHCC
18.6025627689
788PhosphorylationTDGDHLSSLLNKTTV
CCCHHHHHHHHHCCC
43.1424719451
792UbiquitinationHLSSLLNKTTVHNIP
HHHHHHHHCCCCCCC
45.6129967540
793PhosphorylationLSSLLNKTTVHNIPG
HHHHHHHCCCCCCCC
32.7428555341
794PhosphorylationSSLLNKTTVHNIPGF
HHHHHHCCCCCCCCC
22.7528555341
803PhosphorylationHNIPGFDSIKETNMQ
CCCCCCCCCCCCCCC
33.0428555341
809SulfoxidationDSIKETNMQDGSVQV
CCCCCCCCCCCCEEE
5.1221406390
831PhosphorylationCAFSFQNSLLYDLD-
CEEEECCCCCCCCC-
14.68-
834PhosphorylationSFQNSLLYDLD----
EECCCCCCCCC----
21.54-

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 KTU_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of KTU_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 KTU_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
NCAM1_HUMANNCAM1physical
26186194
DPYL1_HUMANCRMP1physical
26186194
DPYL3_HUMANDPYSL3physical
26186194
DPYL2_HUMANDPYSL2physical
26186194
DPYL5_HUMANDPYSL5physical
26186194
LSAMP_HUMANLSAMPphysical
26186194
STXB1_HUMANSTXBP1physical
26186194
ATP4A_HUMANATP4Aphysical
26186194
AT2B2_HUMANATP2B2physical
26186194
HPCA_HUMANHPCAphysical
26186194
NCALD_HUMANNCALDphysical
26186194
KCC2B_HUMANCAMK2Bphysical
26186194
KCC2A_HUMANCAMK2Aphysical
26186194
H2AW_HUMANH2AFY2physical
26186194
STX1A_HUMANSTX1Aphysical
26186194
STX1B_HUMANSTX1Bphysical
26186194
GPM6B_HUMANGPM6Bphysical
26186194
DNM1L_HUMANDNM1Lphysical
26186194
H2B1L_HUMANHIST1H2BLphysical
26186194
CNTN1_HUMANCNTN1physical
26186194
DCLK1_HUMANDCLK1physical
26186194
ALS2_HUMANALS2physical
26186194
FA49B_HUMANFAM49Bphysical
26186194
AP180_HUMANSNAP91physical
26186194
SYT1_HUMANSYT1physical
26186194
HPCL4_HUMANHPCAL4physical
26186194
VISL1_HUMANVSNL1physical
26186194
AMPH_HUMANAMPHphysical
26186194
DYN3_HUMANDNM3physical
26186194
DYN1_HUMANDNM1physical
26186194
CAD13_HUMANCDH13physical
26186194
E41L1_HUMANEPB41L1physical
26186194
ARL8B_HUMANARL8Bphysical
26186194
CA2D1_HUMANCACNA2D1physical
26186194
GNAQ_HUMANGNAQphysical
26186194
DPP6_HUMANDPP6physical
26186194
GNAO_HUMANGNAO1physical
26186194
GBG2_HUMANGNG2physical
26186194
GPM6A_HUMANGPM6Aphysical
26186194
ANK2_HUMANANK2physical
26186194
SYUB_HUMANSNCBphysical
26186194
SYUA_HUMANSNCAphysical
26186194
RAB6B_HUMANRAB6Bphysical
26186194
RAB6A_HUMANRAB6Aphysical
26186194
SYN2_HUMANSYN2physical
26186194
SYN1_HUMANSYN1physical
26186194
SYPH_HUMANSYPphysical
26186194
MARE2_HUMANMAPRE2physical
26186194
RAB3A_HUMANRAB3Aphysical
26186194
RAB5A_HUMANRAB5Aphysical
26186194
LASP1_HUMANLASP1physical
26186194
NDRG4_HUMANNDRG4physical
26186194
SNAB_HUMANNAPBphysical
26186194
CALB2_HUMANCALB2physical
26186194
TAU_HUMANMAPTphysical
26186194
DPYL4_HUMANDPYSL4physical
26186194
RAB2A_HUMANRAB2Aphysical
26186194
CAMKV_HUMANCAMKVphysical
26186194
GRIA2_HUMANGRIA2physical
26186194
L1CAM_HUMANL1CAMphysical
26186194
SNP25_HUMANSNAP25physical
26186194
PLXA4_HUMANPLXNA4physical
26186194
SFXN3_HUMANSFXN3physical
26186194
ALS2_HUMANALS2physical
28514442
H2B1L_HUMANHIST1H2BLphysical
28514442
STX1B_HUMANSTX1Bphysical
28514442
GRIA2_HUMANGRIA2physical
28514442
VISL1_HUMANVSNL1physical
28514442
L1CAM_HUMANL1CAMphysical
28514442
ATP4A_HUMANATP4Aphysical
28514442
HPCL4_HUMANHPCAL4physical
28514442
SNAB_HUMANNAPBphysical
28514442
DCLK1_HUMANDCLK1physical
28514442
SYN1_HUMANSYN1physical
28514442
KCC2A_HUMANCAMK2Aphysical
28514442
TAU_HUMANMAPTphysical
28514442
HPCA_HUMANHPCAphysical
28514442
SYT1_HUMANSYT1physical
28514442
CALB2_HUMANCALB2physical
28514442
DPP6_HUMANDPP6physical
28514442
AP180_HUMANSNAP91physical
28514442
DPYL1_HUMANCRMP1physical
28514442
DPYL3_HUMANDPYSL3physical
28514442
LSAMP_HUMANLSAMPphysical
28514442
NDRG4_HUMANNDRG4physical
28514442
H2AW_HUMANH2AFY2physical
28514442
STX1A_HUMANSTX1Aphysical
28514442
SYN2_HUMANSYN2physical
28514442
STXB1_HUMANSTXBP1physical
28514442
SYUB_HUMANSNCBphysical
28514442
DNM1L_HUMANDNM1Lphysical
28514442
E41L1_HUMANEPB41L1physical
28514442
SNP25_HUMANSNAP25physical
28514442
GPM6A_HUMANGPM6Aphysical
28514442
CNTN1_HUMANCNTN1physical
28514442
RAB6B_HUMANRAB6Bphysical
28514442
DYN1_HUMANDNM1physical
28514442
DPYL2_HUMANDPYSL2physical
28514442
MARE2_HUMANMAPRE2physical
28514442
FA49B_HUMANFAM49Bphysical
28514442
PHIPL_HUMANPHYHIPLphysical
28514442
RAB3A_HUMANRAB3Aphysical
28514442
CAMKV_HUMANCAMKVphysical
28514442
LASP1_HUMANLASP1physical
28514442
ANK2_HUMANANK2physical
28514442
GBG2_HUMANGNG2physical
28514442
SYUA_HUMANSNCAphysical
28514442
KCC2B_HUMANCAMK2Bphysical
28514442
CAD13_HUMANCDH13physical
28514442
GNAO_HUMANGNAO1physical
28514442
DCX_HUMANDCXphysical
28514442
NCALD_HUMANNCALDphysical
28514442
VATC1_HUMANATP6V1C1physical
28514442
NCAM1_HUMANNCAM1physical
28514442
DPYL5_HUMANDPYSL5physical
28514442
SEPT3_HUMANSEPT3physical
28514442
GNAQ_HUMANGNAQphysical
28514442
ARL8B_HUMANARL8Bphysical
28514442
PLXA4_HUMANPLXNA4physical
28514442
DAAF4_HUMANDYX1C1physical
27173435

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
612518Ciliary dyskinesia, primary, 10 (CILD10)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of KTU_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-641, AND MASSSPECTROMETRY.

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