CKAP5_MOUSE - dbPTM
CKAP5_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CKAP5_MOUSE
UniProt AC A2AGT5
Protein Name Cytoskeleton-associated protein 5
Gene Name Ckap5 {ECO:0000312|MGI:MGI:1923036}
Organism Mus musculus (Mouse).
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. Enhances the strength of NDC80 complex-mediated kinetochore-tip microtubule attachments..
Protein Sequence MGDDSEWLKLPVDQKCEHKLWKARLSGYEEALKIFQKIKDEKSPEWSKYLGLIKKFVTDSNAVVQLKGLEAALVYVENAHVAGKTTGEVVSGVVSKVFNQPKAKAKELGIEICLMYVEIEKGESVQEELLKGLDNKNPKIIVACIETLRKALSEFGSKIISLKPIIKVLPKLFESRDKAVRDEAKLFAIEIYRWNRDAVKHTLQNINSVQLKELEEEWVKLPTGAPKPSRFLRSQQELEAKLEQQQSAGGDAEGGGDDGDEVPQVDAYELLDAVEILSKLPKDFYDKIEAKKWQERKEALEAVEVLVKNPKLEAGDYADLVKALKKVVGKDTNVMLVALAAKCLTGLAVGLRKKFGQYAGHVVPTILEKFKEKKPQVVQALQEAIDAIFLTTTLQNISEDVLAVMDNKNPTIKQQTSLFIARSFRHCTSSTLPKSLLKPFCAALLKHINDSAPEVRDAAFEALGTALKVVGEKSVNPFLADVDKLKLDRIKECSEKVELVHGKKSGLATEKKESKPLPGRAAASGAAGDKDTKDVSGPKPGPLKKTPTAKAGGPSKKGKTTAPGGSASAGTKNKKGLETKEIVEPELSIEVCEEKASAVLPPTCIQLLDSSNWKERLACMEEFQKAVELMERTEMPCQALVKMLAKKPGWKETNFQVMQMKLHIVALIAQKGNFSKTSAQIVLDGLVDKIGDVKCGNNAKEAMTAIAEACMLPWTAEQVMSMAFSQKNPKNQSETLNWLSNAIKEFGFSELNVKAFISNVKTALAATNPAVRTSAITLLGVMYLYVGPSLRMIFEDEKPALLSQIDAEFQKMQGQSPPAPTRGIAKHSTSATDEGEDGEEPGEGGNDVVDLLPRIEISDKITSELVSKIGDKNWKIRKEGLDEVAGIINEAKFIQPNIGELPTALKGRLNDSNKILVQQTLNILQQLAVAMGANIRQHVKNLGIPVITVLGDSKNNVRAAALATVNAWAEQTGMKEWLEGEDLSEELKKENPFLRQELLGWLAEKLPTLRSTPTDLILCVPHLYSCLKDRNGDVRKKAQDALPFFMMHLGYEKMAKATGKLKPTSKDQVLAMLEKAKANMPSKPAAPAKAMSKPMGGSAPAKTQPIPAPVEDSVSSTIEAKPDLKKAKAPGVSSKAKSVQGKKVPSKTTLKEDDDKSGPIFIVVPNGKEQRMRDEKGLKVLKWNFTTPRDEYIEQLKTQMSTCVAKWLQDEMFHSDFQHHNKALAVMVDHLESEKDGVISCLDLILKWLTLRFFDTNTSVLMKALEYLKLLFTLLSEEEYHLTENEASSFIPYLILKVGEPKDVIRKDVRAILNRMCLVYPASKMFPFIMEGTKSKNSKQRAECLEELGCLIESYGMNVCQPTPGKALKEIAIHIGDRDNAVRNAALNTIVTVYNVHGDQVFKLIGNLSEKDMSMLEERIKRSAKRPSAAPVKQAEEKPQRTQNINSNANMLRKGPAEDMSSKLNQARSLSGHPEAAQMVRREFQLDLDEIENDNGTVRCEMPELVQHKLDDIFEPVLIPEPKIRAVSPHFDDMHSNTASTINFIISQVASGDINTSIQALTQIDEVLRQEDKAEAMSGHIDQFLIATFMQLRLIYSTHMADEKLDKDEIIKLYSCIIGNMISLFQIESLAREASTGVLKDLMHGLITLMLDSRIEDLEEGQQVIRSVNLLVVKVLEKSDQTNILSALLVLLQDSLLATASSPKFSELVMKCLWRMVRLLPDTINSINLDRILLDIHIFMKVFPKEKLKQCKSEFPIRTLKTLLHTLCKLKGPKILDHLTMIDNKNESELEAHLCRMMKHSMDQTGSKSDKETEKGASRIDEKSSKAKVNDFLAEIFKKIGSKENTKEGLAELYEYKKKYSDTDIEPFLKNSSQFFQSYVERGLRVIEMERESKGRIPTSTGISPQMEVTCVPTPTSTVSSLGNTNGEEVGPSVYLERLKILRQRCGLDNTKQDDRPPLTSLLSKPAIPPVASSTDMLHSKLSQLRESREQHQHSDLDSNQTHSAGTMTSSSSTTNIDDLKKRLERIKSSRK
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		33.5024759943
48AcetylationEKSPEWSKYLGLIKK
CCCHHHHHHHHHHHH		45.64-
96UbiquitinationVVSGVVSKVFNQPKA
HHHHHHHHHHCCCHH		38.9622790023
116PhosphorylationGIEICLMYVEIEKGE
CCEEEEEEEEECCCC		5.0827742792
167UbiquitinationISLKPIIKVLPKLFE
HCHHHHHHHHHHHHH		38.1422790023
175PhosphorylationVLPKLFESRDKAVRD
HHHHHHHCCCHHHHH		38.1419737024
247PhosphorylationAKLEQQQSAGGDAEG
HHHHHHHHCCCCCCC		25.2529899451
438AcetylationTLPKSLLKPFCAALL
CCCHHHHHHHHHHHH		41.14-
438SuccinylationTLPKSLLKPFCAALL
CCCHHHHHHHHHHHH		41.14-
514PhosphorylationLATEKKESKPLPGRA
CCCCCCCCCCCCCCH		48.7529514104
524PhosphorylationLPGRAAASGAAGDKD
CCCCHHHCCCCCCCC		25.0028059163
546PhosphorylationKPGPLKKTPTAKAGG
CCCCCCCCCCCCCCC		25.0427180971
566PhosphorylationKTTAPGGSASAGTKN
CCCCCCCCCCCCCCC		25.6027841257
568PhosphorylationTAPGGSASAGTKNKK
CCCCCCCCCCCCCCC		29.00-
735PhosphorylationNPKNQSETLNWLSNA
CCCCHHHHHHHHHHH		30.5528576409
754UbiquitinationGFSELNVKAFISNVK
CCCHHHHHHHHHHHH		36.1822790023
762PhosphorylationAFISNVKTALAATNP
HHHHHHHHHHHHCCH		23.7125195567
767PhosphorylationVKTALAATNPAVRTS
HHHHHHHCCHHHHHH		35.8125195567
777PhosphorylationAVRTSAITLLGVMYL
HHHHHHHHHHHHHHH		18.6921454597
789PhosphorylationMYLYVGPSLRMIFED
HHHHHCCHHHHHHCC		23.7621454597
816PhosphorylationFQKMQGQSPPAPTRG
HHHHCCCCCCCCCCC		39.4125521595
821PhosphorylationGQSPPAPTRGIAKHS
CCCCCCCCCCCCCCC		43.5729472430
828PhosphorylationTRGIAKHSTSATDEG
CCCCCCCCCCCCCCC		24.2929472430
829PhosphorylationRGIAKHSTSATDEGE
CCCCCCCCCCCCCCC		23.3125293948
830PhosphorylationGIAKHSTSATDEGED
CCCCCCCCCCCCCCC		31.9921659605
832PhosphorylationAKHSTSATDEGEDGE
CCCCCCCCCCCCCCC		34.0628507225
1125AcetylationIEAKPDLKKAKAPGV
EECCCCHHHCCCCCC		59.057630957
1320PhosphorylationLNRMCLVYPASKMFP
HHHHCHHHCHHHHHH		4.7119655815
1333PhosphorylationFPFIMEGTKSKNSKQ
HHHHHCCCCCCCHHH		20.8819655815
1469PhosphorylationSKLNQARSLSGHPEA
HHHHHHHHHCCCHHH		29.8724899341
1471PhosphorylationLNQARSLSGHPEAAQ
HHHHHHHCCCHHHHH		35.9828066266
1801PhosphorylationLCRMMKHSMDQTGSK
HHHHHHHHHHCCCCC		20.6622807455
1805PhosphorylationMKHSMDQTGSKSDKE
HHHHHHCCCCCCHHH		38.8828576409
1809PhosphorylationMDQTGSKSDKETEKG
HHCCCCCCHHHHHHH		56.4629899451
1828AcetylationDEKSSKAKVNDFLAE
CHHHHHHHHHHHHHH		45.3615608963
1838AcetylationDFLAEIFKKIGSKEN
HHHHHHHHHHCCCCC		49.4915608971
1860PhosphorylationLYEYKKKYSDTDIEP
HHHHHHHCCCCCCHH		22.2125521595
1861PhosphorylationYEYKKKYSDTDIEPF
HHHHHHCCCCCCHHH		42.8021082442
1863PhosphorylationYKKKYSDTDIEPFLK
HHHHCCCCCCHHHHC		32.7023984901
1904PhosphorylationIPTSTGISPQMEVTC
CCCCCCCCCCCEEEE		15.4922067460
2029PhosphorylationKRLERIKSSRK----
HHHHHHHHHCC----		32.76-
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_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CKAP5_MOUSE !!
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_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
APC_HUMANAPCphysical
20360068
CKAP5_HUMANCKAP5physical
20360068
TACC3_HUMANTACC3physical
20360068
SLAI2_HUMANSLAIN2physical
20360068
SET_HUMANSETphysical
20360068
DYHC1_HUMANDYNC1H1physical
20360068
ACADM_HUMANACADMphysical
26496610
ATPA_HUMANATP5A1physical
26496610
BLMH_HUMANBLMHphysical
26496610
ETFB_HUMANETFBphysical
26496610
MTOR_HUMANMTORphysical
26496610
CH60_HUMANHSPD1physical
26496610
K2C5_HUMANKRT5physical
26496610
PYC_HUMANPCphysical
26496610
EFTU_HUMANTUFMphysical
26496610
LONM_HUMANLONP1physical
26496610
TACC3_HUMANTACC3physical
26496610
TACC2_HUMANTACC2physical
26496610
ERLN1_HUMANERLIN1physical
26496610
MIC60_HUMANIMMTphysical
26496610
RBPMS_HUMANRBPMSphysical
26496610
RB6I2_HUMANERC1physical
26496610
S18L2_HUMANSS18L2physical
26496610
CCHCR_HUMANCCHCR1physical
26496610
KI26B_HUMANKIF26Bphysical
26496610
SLAI2_HUMANSLAIN2physical
26496610
GCC1_HUMANGCC1physical
26496610
TRI47_HUMANTRIM47physical
26496610
CC127_HUMANCCDC127physical
26496610
FILA2_HUMANFLG2physical
26496610
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CKAP5_MOUSE

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Related Literatures of Post-Translational Modification

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