CKAP5_HUMAN - dbPTM
CKAP5_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CKAP5_HUMAN
UniProt AC Q14008
Protein Name Cytoskeleton-associated protein 5
Gene Name CKAP5
Organism Homo sapiens (Human).
Sequence Length 2032
Subcellular Localization Cytoplasm, cytoskeleton, microtubule organizing center, centrosome . Cytoplasm, cytoskeleton, spindle pole . Cytoplasm, cytoskeleton, spindle . Chromosome, centromere, kinetochore . Detected on centrosomes and kinetochores during interphase and mitos
Protein Description Binds to the plus end of microtubules and regulates microtubule dynamics and microtubule organization. Acts as processive microtubule polymerase. Promotes cytoplasmic microtubule nucleation and elongation. Plays a major role in organizing spindle poles. In spindle formation protects kinetochore microtubules from depolymerization by KIF2C and has an essential role in centrosomal microtubule assembly independently of KIF2C activity. Contributes to centrosome integrity. Acts as component of the TACC3/ch-TOG/clathrin complex proposed to contribute to stabilization of kinetochore fibers of the mitotic spindle by acting as inter-microtubule bridge. The TACC3/ch-TOG/clathrin complex is required for the maintenance of kinetochore fiber tension. [PubMed: 23532825 Enhances the strength of NDC80 complex-mediated kinetochore-tip microtubule attachments]
Protein Sequence MGDDSEWLKLPVDQKCEHKLWKARLSGYEEALKIFQKIKDEKSPEWSKFLGLIKKFVTDSNAVVQLKGLEAALVYVENAHVAGKTTGEVVSGVVSKVFNQPKAKAKELGIEICLMYIEIEKGEAVQEELLKGLDNKNPKIIVACIETLRKALSEFGSKIILLKPIIKVLPKLFESREKAVRDEAKLIAVEIYRWIRDALRPPLQNINSVQLKELEEEWVKLPTSAPRPTRFLRSQQELEAKLEQQQSAGGDAEGGGDDGDEVPQIDAYELLEAVEILSKLPKDFYDKIEAKKWQERKEALESVEVLIKNPKLEAGDYADLVKALKKVVGKDTNVMLVALAAKCLTGLAVGLRKKFGQYAGHVVPTILEKFKEKKPQVVQALQEAIDAIFLTTTLQNISEDVLAVMDNKNPTIKQQTSLFIARSFRHCTASTLPKSLLKPFCAALLKHINDSAPEVRDAAFEALGTALKVVGEKAVNPFLADVDKLKLDKIKECSEKVELIHGKKAGLAADKKEFKPLPGRTAASGAAGDKDTKDISAPKPGPLKKAPAAKAGGPPKKGKPAAPGGAGNTGTKNKKGLETKEIVEPELSIEVCEEKASAVLPPTCIQLLDSSNWKERLACMEEFQKAVELMDRTEMPCQALVRMLAKKPGWKETNFQVMQMKLHIVALIAQKGNFSKTSAQVVLDGLVDKIGDVKCGNNAKEAMTAIAEACMLPWTAEQVVSMAFSQKNPKNQSETLNWLSNAIKEFGFSGLNVKAFISNVKTALAATNPAVRTAAITLLGVMYLYVGPSLRMFFEDEKPALLSQIDAEFEKMQGQSPPAPTRGISKHSTSGTDEGEDGDEPDDGSNDVVDLLPRTEISDKITSELVSKIGDKNWKIRKEGLDEVAGIINDAKFIQPNIGELPTALKGRLNDSNKILVQQTLNILQQLAVAMGPNIKQHVKNLGIPIITVLGDSKNNVRAAALATVNAWAEQTGMKEWLEGEDLSEELKKENPFLRQELLGWLAEKLPTLRSTPTDLILCVPHLYSCLEDRNGDVRKKAQDALPFFMMHLGYEKMAKATGKLKPTSKDQVLAMLEKAKVNMPAKPAPPTKATSKPMGGSAPAKFQPASAPAEDCISSSTEPKPDPKKAKAPGLSSKAKSAQGKKMPSKTSLKEDEDKSGPIFIVVPNGKEQRMKDEKGLKVLKWNFTTPRDEYIEQLKTQMSSCVAKWLQDEMFHSDFQHHNKALAVMVDHLESEKEGVIGCLDLILKWLTLRFFDTNTSVLMKALEYLKLLFTLLSEEEYHLTENEASSFIPYLVVKVGEPKDVIRKDVRAILNRMCLVYPASKMFPFIMEGTKSKNSKQRAECLEELGCLVESYGMNVCQPTPGKALKEIAVHIGDRDNAVRNAALNTIVTVYNVHGDQVFKLIGNLSEKDMSMLEERIKRSAKRPSAAPIKQVEEKPQRAQNISSNANMLRKGPAEDMSSKLNQARSMSGHPEAAQMVRREFQLDLDEIENDNGTVRCEMPELVQHKLDDIFEPVLIPEPKIRAVSPHFDDMHSNTASTINFIISQVASGDINTSIQALTQIDEVLRQEDKAEAMSGHIDQFLIATFMQLRLIYNTHMADEKLEKDEIIKLYSCIIGNMISLFQIESLAREASTGVLKDLMHGLITLMLDSRIEDLEEGQQVIRSVNLLVVKVLEKSDQTNILSALLVLLQDSLLATASSPKFSELVMKCLWRMVRLLPDTINSINLDRILLDIHIFMKVFPKEKLKQCKSEFPIRTLKTLLHTLCKLKGPKILDHLTMIDNKNESELEAHLCRMMKHSMDQTGSKSDKETEKGASRIDEKSSKAKVNDFLAEIFKKIGSKENTKEGLAELYEYKKKYSDADIEPFLKNSSQFFQSYVERGLRVIEMEREGKGRISTSTGISPQMEVTCVPTPTSTVSSIGNTNGEEVGPSVYLERLKILRQRCGLDNTKQDDRPPLTSLLSKPAVPTVASSTDMLHSKLSQLRESREQHQHSDLDSNQTHSSGTVTSSSSTANIDDLKKRLERIKSSRK
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
26PhosphorylationKLWKARLSGYEEALK
HHHHHHHCCHHHHHH
33.5028348404
42UbiquitinationFQKIKDEKSPEWSKF
HHHHCCCCCHHHHHH
79.87-
48AcetylationEKSPEWSKFLGLIKK
CCCHHHHHHHHHHHH
45.7619608861
48UbiquitinationEKSPEWSKFLGLIKK
CCCHHHHHHHHHHHH
45.7622817900
48 (in isoform 1)Ubiquitination-45.7621890473
48 (in isoform 2)Ubiquitination-45.7621890473
48 (in isoform 3)Ubiquitination-45.7621890473
150UbiquitinationACIETLRKALSEFGS
HHHHHHHHHHHHHCC
57.7129967540
150 (in isoform 3)Ubiquitination-57.71-
153PhosphorylationETLRKALSEFGSKII
HHHHHHHHHHCCHHH
35.4220860994
158AcetylationALSEFGSKIILLKPI
HHHHHCCHHHHHHHH
33.8619817325
163AcetylationGSKIILLKPIIKVLP
CCHHHHHHHHHHHHH
30.6323749302
171AcetylationPIIKVLPKLFESREK
HHHHHHHHHHHCHHH
62.7425953088
220UbiquitinationELEEEWVKLPTSAPR
HHHHHHHCCCCCCCC
50.2329967540
247PhosphorylationAKLEQQQSAGGDAEG
HHHHHHHHCCCCCCC
25.2528270605
268PhosphorylationEVPQIDAYELLEAVE
CCCCCCHHHHHHHHH
11.8922817900
287UbiquitinationLPKDFYDKIEAKKWQ
CCHHHHHHHHHHHHH
30.9429967540
308UbiquitinationESVEVLIKNPKLEAG
HHCHHHHHCCCCCCC
64.1429967540
311UbiquitinationEVLIKNPKLEAGDYA
HHHHHCCCCCCCCHH
69.2429967540
317PhosphorylationPKLEAGDYADLVKAL
CCCCCCCHHHHHHHH
10.9122817900
322UbiquitinationGDYADLVKALKKVVG
CCHHHHHHHHHHHHC
56.1329967540
332PhosphorylationKKVVGKDTNVMLVAL
HHHHCCCHHHHHHHH
32.95-
335SulfoxidationVGKDTNVMLVALAAK
HCCCHHHHHHHHHHH
2.4321406390
354AcetylationLAVGLRKKFGQYAGH
HHHHHHHHHHHHHCC
48.5725953088
423PhosphorylationTSLFIARSFRHCTAS
HHHHHHHHHCCCCCC
20.0122817900
427S-nitrosylationIARSFRHCTASTLPK
HHHHHCCCCCCCCCH
2.722212679
435PhosphorylationTASTLPKSLLKPFCA
CCCCCCHHHHHHHHH
36.6724719451
438AcetylationTLPKSLLKPFCAALL
CCCHHHHHHHHHHHH
41.1426051181
438UbiquitinationTLPKSLLKPFCAALL
CCCHHHHHHHHHHHH
41.14-
438 (in isoform 3)Ubiquitination-41.14-
468UbiquitinationEALGTALKVVGEKAV
HHHHHHHHHHHHHHH
32.2029967540
473AcetylationALKVVGEKAVNPFLA
HHHHHHHHHHCHHHH
52.2725953088
473UbiquitinationALKVVGEKAVNPFLA
HHHHHHHHHHCHHHH
52.2732015554
515AcetylationAADKKEFKPLPGRTA
CCCCCCCCCCCCCCC
46.8925953088
521PhosphorylationFKPLPGRTAASGAAG
CCCCCCCCCCCCCCC
32.2722817900
536PhosphorylationDKDTKDISAPKPGPL
CCCCCCCCCCCCCCC
48.9628555341
569PhosphorylationAPGGAGNTGTKNKKG
CCCCCCCCCCCCCCC
45.3623403867
571PhosphorylationGGAGNTGTKNKKGLE
CCCCCCCCCCCCCCC
29.4323403867
619GlutathionylationNWKERLACMEEFQKA
CHHHHHHHHHHHHHH
4.1122555962
632MethylationKAVELMDRTEMPCQA
HHHHHHHCCCCHHHH
20.72-
689UbiquitinationVLDGLVDKIGDVKCG
HHHHHHHHHCCCCCC
40.9029967540
689 (in isoform 3)Ubiquitination-40.90-
733PhosphorylationQKNPKNQSETLNWLS
CCCCCCHHHHHHHHH
41.7821712546
754UbiquitinationGFSGLNVKAFISNVK
CCCCCCHHHHHHHHH
36.1821890473
754 (in isoform 1)Ubiquitination-36.1821890473
754 (in isoform 2)Ubiquitination-36.1821890473
754 (in isoform 3)Ubiquitination-36.1821890473
816PhosphorylationFEKMQGQSPPAPTRG
HHHHCCCCCCCCCCC
39.4129255136
821PhosphorylationGQSPPAPTRGISKHS
CCCCCCCCCCCCCCC
43.5729255136
825PhosphorylationPAPTRGISKHSTSGT
CCCCCCCCCCCCCCC
27.4330624053
828PhosphorylationTRGISKHSTSGTDEG
CCCCCCCCCCCCCCC
28.1823401153
829PhosphorylationRGISKHSTSGTDEGE
CCCCCCCCCCCCCCC
30.7822167270
830PhosphorylationGISKHSTSGTDEGED
CCCCCCCCCCCCCCC
42.5922167270
832PhosphorylationSKHSTSGTDEGEDGD
CCCCCCCCCCCCCCC
30.5522167270
845PhosphorylationGDEPDDGSNDVVDLL
CCCCCCCCCCHHHHC
36.5322167270
855PhosphorylationVVDLLPRTEISDKIT
HHHHCCCCHHCHHHH
35.4121406692
858PhosphorylationLLPRTEISDKITSEL
HCCCCHHCHHHHHHH
26.9821406692
862PhosphorylationTEISDKITSELVSKI
CHHCHHHHHHHHHHH
23.1430206219
863PhosphorylationEISDKITSELVSKIG
HHCHHHHHHHHHHHC
32.1930206219
875MalonylationKIGDKNWKIRKEGLD
HHCCCCCHHCCCCHH
41.8626320211
878UbiquitinationDKNWKIRKEGLDEVA
CCCCHHCCCCHHHHH
60.6529967540
906UbiquitinationGELPTALKGRLNDSN
CCCCHHHCCCCCCCC
39.2529967540
906 (in isoform 3)Ubiquitination-39.25-
953PhosphorylationIITVLGDSKNNVRAA
EEEEECCCCCHHHHH
35.1721712546
954UbiquitinationITVLGDSKNNVRAAA
EEEECCCCCHHHHHH
58.2332015554
1058PhosphorylationYEKMAKATGKLKPTS
HHHHHHHHCCCCCCC
33.8623911959
1065PhosphorylationTGKLKPTSKDQVLAM
HCCCCCCCHHHHHHH
42.6423911959
1066UbiquitinationGKLKPTSKDQVLAML
CCCCCCCHHHHHHHH
55.4429967540
1072SulfoxidationSKDQVLAMLEKAKVN
CHHHHHHHHHHHCCC
4.3121406390
1088PhosphorylationPAKPAPPTKATSKPM
CCCCCCCCCCCCCCC
32.0520860994
1091PhosphorylationPAPPTKATSKPMGGS
CCCCCCCCCCCCCCC
38.5521406692
1092PhosphorylationAPPTKATSKPMGGSA
CCCCCCCCCCCCCCC
39.3521406692
1093"N6,N6-dimethyllysine"PPTKATSKPMGGSAP
CCCCCCCCCCCCCCC
34.37-
1093MethylationPPTKATSKPMGGSAP
CCCCCCCCCCCCCCC
34.37-
1095SulfoxidationTKATSKPMGGSAPAK
CCCCCCCCCCCCCCC
12.4930846556
1098PhosphorylationTSKPMGGSAPAKFQP
CCCCCCCCCCCCCCC
25.9121406692
1102AcetylationMGGSAPAKFQPASAP
CCCCCCCCCCCCCCC
43.4026051181
1107PhosphorylationPAKFQPASAPAEDCI
CCCCCCCCCCHHHHC
41.2828555341
1115PhosphorylationAPAEDCISSSTEPKP
CCHHHHCCCCCCCCC
25.2723312004
1116PhosphorylationPAEDCISSSTEPKPD
CHHHHCCCCCCCCCC
22.7423312004
1117PhosphorylationAEDCISSSTEPKPDP
HHHHCCCCCCCCCCH
29.9623312004
1118PhosphorylationEDCISSSTEPKPDPK
HHHCCCCCCCCCCHH
59.2523312004
1121AcetylationISSSTEPKPDPKKAK
CCCCCCCCCCHHHCC
56.6826051181
1121UbiquitinationISSSTEPKPDPKKAK
CCCCCCCCCCHHHCC
56.6822817900
1121 (in isoform 1)Ubiquitination-56.6821890473
1121 (in isoform 2)Ubiquitination-56.6821890473
1121 (in isoform 3)Ubiquitination-56.6821890473
1125UbiquitinationTEPKPDPKKAKAPGL
CCCCCCHHHCCCCCC
73.1422817900
1126UbiquitinationEPKPDPKKAKAPGLS
CCCCCHHHCCCCCCC
61.5822817900
1138PhosphorylationGLSSKAKSAQGKKMP
CCCHHHHHHCCCCCC
30.5922817900
1146PhosphorylationAQGKKMPSKTSLKED
HCCCCCCCCCCCCCC
45.1028270605
1148PhosphorylationGKKMPSKTSLKEDED
CCCCCCCCCCCCCCC
43.5628060719
1149PhosphorylationKKMPSKTSLKEDEDK
CCCCCCCCCCCCCCC
40.9826657352
1182UbiquitinationEKGLKVLKWNFTTPR
CCCCEEEECCCCCCH
42.98-
1197UbiquitinationDEYIEQLKTQMSSCV
HHHHHHHHHHHHHHH
36.0829967540
1256PhosphorylationLTLRFFDTNTSVLMK
HHHHHCCCCHHHHHH
34.93-
1258PhosphorylationLRFFDTNTSVLMKAL
HHHCCCCHHHHHHHH
23.46-
1259PhosphorylationRFFDTNTSVLMKALE
HHCCCCHHHHHHHHH
18.47-
1262SulfoxidationDTNTSVLMKALEYLK
CCCHHHHHHHHHHHH
1.9321406390
1302UbiquitinationVVKVGEPKDVIRKDV
EEECCCCHHHHHHHH
61.3929967540
1315MethylationDVRAILNRMCLVYPA
HHHHHHHHHCHHHCH
17.47-
1317GlutathionylationRAILNRMCLVYPASK
HHHHHHHCHHHCHHH
1.7822555962
1323PhosphorylationMCLVYPASKMFPFIM
HCHHHCHHHHHHHHH
21.8323322592
1324MethylationCLVYPASKMFPFIME
CHHHCHHHHHHHHHC
46.82-
1363PhosphorylationGMNVCQPTPGKALKE
CCCCCCCCCCHHHHH
20.8522067460
1369AcetylationPTPGKALKEIAVHIG
CCCCHHHHHHHHHHC
52.51156407
1409PhosphorylationFKLIGNLSEKDMSML
HHHHCCCCHHHHHHH
46.7522210691
1411AcetylationLIGNLSEKDMSMLEE
HHCCCCHHHHHHHHH
56.1925953088
1411UbiquitinationLIGNLSEKDMSMLEE
HHCCCCHHHHHHHHH
56.1932015554
1414PhosphorylationNLSEKDMSMLEERIK
CCCHHHHHHHHHHHH
30.2822210691
1421AcetylationSMLEERIKRSAKRPS
HHHHHHHHHHCCCCC
46.6619822151
1428PhosphorylationKRSAKRPSAAPIKQV
HHHCCCCCCCCCHHH
40.8927134283
1433AcetylationRPSAAPIKQVEEKPQ
CCCCCCCHHHHCCCH
47.4326051181
1433UbiquitinationRPSAAPIKQVEEKPQ
CCCCCCCHHHHCCCH
47.4329967540
1438UbiquitinationPIKQVEEKPQRAQNI
CCHHHHCCCHHHHHH
32.7024816145
1446PhosphorylationPQRAQNISSNANMLR
CHHHHHHHHHHHHHH
25.7020860994
1447PhosphorylationQRAQNISSNANMLRK
HHHHHHHHHHHHHHC
35.8420860994
1451SulfoxidationNISSNANMLRKGPAE
HHHHHHHHHHCCCHH
3.3921406390
1454UbiquitinationSNANMLRKGPAEDMS
HHHHHHHCCCHHHHH
66.3424816145
1463AcetylationPAEDMSSKLNQARSM
CHHHHHHHHHHHHHH
44.1225953088
1469PhosphorylationSKLNQARSMSGHPEA
HHHHHHHHHCCCHHH
21.9525159151
1470SulfoxidationKLNQARSMSGHPEAA
HHHHHHHHCCCHHHH
4.6630846556
1471PhosphorylationLNQARSMSGHPEAAQ
HHHHHHHCCCHHHHH
34.8925159151
1479SulfoxidationGHPEAAQMVRREFQL
CCHHHHHHHHHHHCC
1.8630846556
1509UbiquitinationMPELVQHKLDDIFEP
CHHHHHHCCCCCCCC
36.2029967540
1523UbiquitinationPVLIPEPKIRAVSPH
CCCCCCCCCCEECCC
43.0722817900
1523 (in isoform 1)Ubiquitination-43.0721890473
1523 (in isoform 2)Ubiquitination-43.0721890473
1523 (in isoform 3)Ubiquitination-43.0721890473
1528PhosphorylationEPKIRAVSPHFDDMH
CCCCCEECCCCCCCC
16.2127422710
1536PhosphorylationPHFDDMHSNTASTIN
CCCCCCCCCCHHHHH
29.2821406692
1538PhosphorylationFDDMHSNTASTINFI
CCCCCCCCHHHHHHH
25.6221406692
1540PhosphorylationDMHSNTASTINFIIS
CCCCCCHHHHHHHHH
27.9921406692
1541PhosphorylationMHSNTASTINFIISQ
CCCCCHHHHHHHHHH
19.9221406692
1547PhosphorylationSTINFIISQVASGDI
HHHHHHHHHHHCCCC
17.4921406692
1551PhosphorylationFIISQVASGDINTSI
HHHHHHHCCCCHHHH
37.8421406692
1556PhosphorylationVASGDINTSIQALTQ
HHCCCCHHHHHHHHH
27.7821406692
1557PhosphorylationASGDINTSIQALTQI
HCCCCHHHHHHHHHH
14.2821406692
1562PhosphorylationNTSIQALTQIDEVLR
HHHHHHHHHHHHHHC
26.8820363803
1612UbiquitinationLEKDEIIKLYSCIIG
CCHHHHHHHHHHHHH
47.21-
1636PhosphorylationSLAREASTGVLKDLM
HHHHHHCHHHHHHHH
38.05-
1648PhosphorylationDLMHGLITLMLDSRI
HHHHHHHHHHHCCCC
15.9124043423
1653PhosphorylationLITLMLDSRIEDLEE
HHHHHHCCCCCCHHH
31.0624043423
1692UbiquitinationLSALLVLLQDSLLAT
HHHHHHHHHHHHHHC
4.0829967540
1701UbiquitinationDSLLATASSPKFSEL
HHHHHCCCCHHHHHH
42.7029967540
1709UbiquitinationSPKFSELVMKCLWRM
CHHHHHHHHHHHHHH
2.7922817900
1711UbiquitinationKFSELVMKCLWRMVR
HHHHHHHHHHHHHHH
20.7822817900
1714UbiquitinationELVMKCLWRMVRLLP
HHHHHHHHHHHHHCH
8.8721890473
1714 (in isoform 2)Ubiquitination-8.8721890473
1725UbiquitinationRLLPDTINSINLDRI
HHCHHHHHHCCHHHH
38.6429967540
1739UbiquitinationILLDIHIFMKVFPKE
HHHHHHHHHHHCCHH
2.1029967540
1748UbiquitinationKVFPKEKLKQCKSEF
HHCCHHHHHHCCCCC
4.9324816145
1752UbiquitinationKEKLKQCKSEFPIRT
HHHHHHCCCCCCHHH
50.9929967540
1761AcetylationEFPIRTLKTLLHTLC
CCCHHHHHHHHHHHH
36.1925953088
1761UbiquitinationEFPIRTLKTLLHTLC
CCCHHHHHHHHHHHH
36.1929967540
1769AcetylationTLLHTLCKLKGPKIL
HHHHHHHHCCCCHHH
57.2425953088
1769UbiquitinationTLLHTLCKLKGPKIL
HHHHHHHHCCCCHHH
57.2422817900
1771UbiquitinationLHTLCKLKGPKILDH
HHHHHHCCCCHHHHE
59.6722817900
1774UbiquitinationLCKLKGPKILDHLTM
HHHCCCCHHHHEEEE
65.6522817900
1774 (in isoform 1)Ubiquitination-65.6521890473
1775 (in isoform 3)Phosphorylation-6.5128450419
1778UbiquitinationKGPKILDHLTMIDNK
CCCHHHHEEEECCCC
21.5429967540
1785UbiquitinationHLTMIDNKNESELEA
EEEECCCCCHHHHHH
59.3429967540
1787UbiquitinationTMIDNKNESELEAHL
EECCCCCHHHHHHHH
47.3929967540
1787 (in isoform 3)Phosphorylation-47.3928450419
1788PhosphorylationMIDNKNESELEAHLC
ECCCCCHHHHHHHHH
57.80-
1797UbiquitinationLEAHLCRMMKHSMDQ
HHHHHHHHHHHHHHC
4.0229967540
1799UbiquitinationAHLCRMMKHSMDQTG
HHHHHHHHHHHHCCC
24.1629967540
1801PhosphorylationLCRMMKHSMDQTGSK
HHHHHHHHHHCCCCC
20.6628348404
1805PhosphorylationMKHSMDQTGSKSDKE
HHHHHHCCCCCCHHH
38.8828985074
1807PhosphorylationHSMDQTGSKSDKETE
HHHHCCCCCCHHHHH
32.1629449344
1808UbiquitinationSMDQTGSKSDKETEK
HHHCCCCCCHHHHHH
65.1124816145
1809PhosphorylationMDQTGSKSDKETEKG
HHCCCCCCHHHHHHH
56.4624719451
1813PhosphorylationGSKSDKETEKGASRI
CCCCHHHHHHHHHHC
49.0629449344
1824PhosphorylationASRIDEKSSKAKVND
HHHCCHHHHHHHHHH
34.7230576142
1825PhosphorylationSRIDEKSSKAKVNDF
HHCCHHHHHHHHHHH
47.9330576142
1828AcetylationDEKSSKAKVNDFLAE
CHHHHHHHHHHHHHH
45.3626051181
1828UbiquitinationDEKSSKAKVNDFLAE
CHHHHHHHHHHHHHH
45.36-
1835 (in isoform 3)Ubiquitination-51.62-
1838UbiquitinationDFLAEIFKKIGSKEN
HHHHHHHHHHCCCCC
49.4929967540
1847UbiquitinationIGSKENTKEGLAELY
HCCCCCCHHHHHHHH
62.4629967540
1854PhosphorylationKEGLAELYEYKKKYS
HHHHHHHHHHHHHCC
14.55-
1857UbiquitinationLAELYEYKKKYSDAD
HHHHHHHHHHCCCCC
30.7429967540
1859UbiquitinationELYEYKKKYSDADIE
HHHHHHHHCCCCCCH
45.9229967540
1860PhosphorylationLYEYKKKYSDADIEP
HHHHHHHCCCCCCHH
22.2123927012
1861PhosphorylationYEYKKKYSDADIEPF
HHHHHHCCCCCCHHH
34.8928355574
1861 (in isoform 3)Phosphorylation-34.8927642862
1870MethylationADIEPFLKNSSQFFQ
CCCHHHHCCHHHHHH
55.98-
1870UbiquitinationADIEPFLKNSSQFFQ
CCCHHHHCCHHHHHH
55.98-
1872PhosphorylationIEPFLKNSSQFFQSY
CHHHHCCHHHHHHHH
24.75-
1873PhosphorylationEPFLKNSSQFFQSYV
HHHHCCHHHHHHHHH
40.1621712546
1878PhosphorylationNSSQFFQSYVERGLR
CHHHHHHHHHHHCCE
26.4524076635
1882MethylationFFQSYVERGLRVIEM
HHHHHHHHCCEEEEE
39.13-
1898O-linked_GlycosylationREGKGRISTSTGISP
ECCCCCEECCCCCCC
18.2330379171
1898PhosphorylationREGKGRISTSTGISP
ECCCCCEECCCCCCC
18.2325627689
1899PhosphorylationEGKGRISTSTGISPQ
CCCCCEECCCCCCCC
28.1225627689
1901PhosphorylationKGRISTSTGISPQME
CCCEECCCCCCCCEE
38.3326074081
1904O-linked_GlycosylationISTSTGISPQMEVTC
EECCCCCCCCEEEEE
15.4930379171
1904PhosphorylationISTSTGISPQMEVTC
EECCCCCCCCEEEEE
15.4925159151
1905UbiquitinationSTSTGISPQMEVTCV
ECCCCCCCCEEEEEE
35.3029967540
1921UbiquitinationTPTSTVSSIGNTNGE
CCCCCCCCCCCCCCC
30.1323000965
1921 (in isoform 2)Ubiquitination-30.1321890473
1935PhosphorylationEEVGPSVYLERLKIL
CCCCCHHHHHHHHHH
13.74-
1960PhosphorylationQDDRPPLTSLLSKPA
CCCCCCHHHHHCCCC
24.0921406692
1961PhosphorylationDDRPPLTSLLSKPAV
CCCCCHHHHHCCCCC
34.6924719451
1964PhosphorylationPPLTSLLSKPAVPTV
CCHHHHHCCCCCCCC
41.7225159151
1965AcetylationPLTSLLSKPAVPTVA
CHHHHHCCCCCCCCC
36.6426051181
1965UbiquitinationPLTSLLSKPAVPTVA
CHHHHHCCCCCCCCC
36.6429967540
1970PhosphorylationLSKPAVPTVASSTDM
HCCCCCCCCCCCHHH
23.3121406692
1973PhosphorylationPAVPTVASSTDMLHS
CCCCCCCCCHHHHHH
29.4521406692
1974PhosphorylationAVPTVASSTDMLHSK
CCCCCCCCHHHHHHH
20.7721406692
1975PhosphorylationVPTVASSTDMLHSKL
CCCCCCCHHHHHHHH
23.9621406692
1980PhosphorylationSSTDMLHSKLSQLRE
CCHHHHHHHHHHHHH
31.1925159151
1981AcetylationSTDMLHSKLSQLRES
CHHHHHHHHHHHHHH
41.2225953088
1981UbiquitinationSTDMLHSKLSQLRES
CHHHHHHHHHHHHHH
41.2223000965
1981 (in isoform 1)Ubiquitination-41.2221890473
1983PhosphorylationDMLHSKLSQLRESRE
HHHHHHHHHHHHHHH
30.7925159151
1988 (in isoform 3)Ubiquitination-34.3821890473
2002PhosphorylationSDLDSNQTHSSGTVT
CCCCCCCCCCCCCEE
28.1630576142
2007PhosphorylationNQTHSSGTVTSSSST
CCCCCCCCEECCCCC
23.6630576142
2009PhosphorylationTHSSGTVTSSSSTAN
CCCCCCEECCCCCCC
23.8030576142
2010PhosphorylationHSSGTVTSSSSTANI
CCCCCEECCCCCCCH
24.7230576142
2021AcetylationTANIDDLKKRLERIK
CCCHHHHHHHHHHHH
42.737379983
2022AcetylationANIDDLKKRLERIKS
CCHHHHHHHHHHHHH
70.3024431261
2030PhosphorylationRLERIKSSRK-----
HHHHHHHHCC-----
38.80-

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 CKAP5_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CKAP5_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 CKAP5_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TACC1_HUMANTACC1physical
14603251
CKAP5_HUMANCKAP5physical
20360068
SLAI2_HUMANSLAIN2physical
20360068
SNW1_HUMANSNW1physical
20360068
TACC3_HUMANTACC3physical
20360068
TACC2_HUMANTACC2physical
20360068
INT2_HUMANINTS2physical
26344197
MARE1_HUMANMAPRE1physical
26344197
MARE3_HUMANMAPRE3physical
26344197
ACADV_HUMANACADVLphysical
26496610
XIAP_HUMANXIAPphysical
26496610
DHC24_HUMANDHCR24physical
26496610
H33_HUMANH3F3Aphysical
26496610
GRP78_HUMANHSPA5physical
26496610
LDHA_HUMANLDHAphysical
26496610
LDHB_HUMANLDHBphysical
26496610
TAU_HUMANMAPTphysical
26496610
PFKAM_HUMANPFKMphysical
26496610
RT12_HUMANMRPS12physical
26496610
RS16_HUMANRPS16physical
26496610
RS17_HUMANRPS17physical
26496610
TACC1_HUMANTACC1physical
26496610
TAP2_HUMANTAP2physical
26496610
TOP2A_HUMANTOP2Aphysical
26496610
ZNHI3_HUMANZNHIT3physical
26496610
TACC3_HUMANTACC3physical
26496610
TACC2_HUMANTACC2physical
26496610
INT7_HUMANINTS7physical
26496610
ACAD8_HUMANACAD8physical
26496610
TRM6_HUMANTRMT6physical
26496610
KLHL7_HUMANKLHL7physical
26496610
SLAI2_HUMANSLAIN2physical
26496610
DDX31_HUMANDDX31physical
26496610
DOT1L_HUMANDOT1Lphysical
26496610
CAVN3_HUMANPRKCDBPphysical
26496610
CCYL1_HUMANCCNYL1physical
26496610
CAVN1_HUMANPTRFphysical
26496610
NDC80_HUMANNDC80physical
27156448

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 CKAP5_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-48, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-816, AND MASSSPECTROMETRY.
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-816, AND MASSSPECTROMETRY.

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