CEP70_HUMAN - dbPTM
CEP70_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CEP70_HUMAN
UniProt AC Q8NHQ1
Protein Name Centrosomal protein of 70 kDa
Gene Name CEP70
Organism Homo sapiens (Human).
Sequence Length 597
Subcellular Localization Cytoplasm, cytoskeleton, microtubule organizing center, centrosome . Localized at the center of the radial microtubule array in interphase and at the spindle poles during various stages of mitosis.
Protein Description Plays a role in the organization of both preexisting and nascent microtubules in interphase cells. During mitosis, required for the organization and orientation of the mitotic spindle..
Protein Sequence MFPVAPKPQDSSQPSDRLMTEKQQEEAEWESINVLLMMHGLKPLSLVKRTDLKDLIIFDKQSSQRMRQNLKLLVEETSCQQNMIQELIETNQQLRNELQLEQSRAANQEQRANDLEQIMESVKSKIGELEDESLSRACHQQNKIKDLQKEQKTLQVKCQHYKKKRTEQEETIASLQMEVCRLKKEEEDRIVTQNRVFAYLCKRVPHTVLDRQLLCLIDYYESKIRKIHTQRQYKEDESQSEEENDYRNLDASPTYKGLLMSLQNQLKESKSKIDALSSEKLNLQKDLETRPTQHELRLYKQQVKKLEKALKKNVKLQELINHKKAEDTEKKDEPSKYNQQQALIDQRYFQVLCSINSIIHNPRAPVIIYKQTKGGVQNFNKDLVQDCGFEHLVPVIEMWADQLTSLKDLYKSLKTLSAELVPWLNLKKQDENEGIKVEDLLFIVDTMLEEVENKEKDSNMPHFQTLQAIVSHFQKLFDVPSLNGVYPRMNEVYTRLGEMNNAVRNLQELLELDSSSSLCVLVSTVGKLCRLINEDVNEQVMQVLGPEDLQSIIYKLEEHEEFFPAFQAFTNDLLEILEIDDLDAIVPAVKKLKVLSY
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
45PhosphorylationMHGLKPLSLVKRTDL
HCCCCCHHHCCCCCC		39.3824719451
53UbiquitinationLVKRTDLKDLIIFDK
HCCCCCCCHHEEECH		53.98-
60UbiquitinationKDLIIFDKQSSQRMR
CHHEEECHHHHHHHH		41.13-
77PhosphorylationLKLLVEETSCQQNMI
HHHHHHHHHHHHHHH		22.6929978859
78PhosphorylationKLLVEETSCQQNMIQ
HHHHHHHHHHHHHHH		17.1329978859
90PhosphorylationMIQELIETNQQLRNE
HHHHHHHHHHHHHHH		31.1929978859
121PhosphorylationDLEQIMESVKSKIGE
HHHHHHHHHHHHHHH		19.9126074081
123 (in isoform 3)Ubiquitination-56.1421906983
123 (in isoform 2)Ubiquitination-56.1421906983
123 (in isoform 1)Ubiquitination-56.1421906983
123UbiquitinationEQIMESVKSKIGELE
HHHHHHHHHHHHHCC		56.1421906983
124PhosphorylationQIMESVKSKIGELED
HHHHHHHHHHHHCCH		27.6124719451
125UbiquitinationIMESVKSKIGELEDE
HHHHHHHHHHHCCHH		49.35-
133PhosphorylationIGELEDESLSRACHQ
HHHCCHHHHHHHHHH		43.9228348404
135PhosphorylationELEDESLSRACHQQN
HCCHHHHHHHHHHHH		27.4124719451
153PhosphorylationDLQKEQKTLQVKCQH
HHHHHHHHHHHHHHH		23.3223403867
157UbiquitinationEQKTLQVKCQHYKKK
HHHHHHHHHHHHHCC		18.40-
202UbiquitinationRVFAYLCKRVPHTVL
HHHHHHHCCCCCCHH		54.56-
233PhosphorylationKIHTQRQYKEDESQS
HHHHHHCHHCCCCCC		20.6628634120
238PhosphorylationRQYKEDESQSEEEND
HCHHCCCCCCHHHHC		51.8628985074
240PhosphorylationYKEDESQSEEENDYR
HHCCCCCCHHHHCCC		57.1428985074
246PhosphorylationQSEEENDYRNLDASP
CCHHHHCCCCCCCCH		17.0023090842
252PhosphorylationDYRNLDASPTYKGLL
CCCCCCCCHHHHHHH		19.9028985074
256UbiquitinationLDASPTYKGLLMSLQ
CCCCHHHHHHHHHHH		45.63-
267UbiquitinationMSLQNQLKESKSKID
HHHHHHHHHCHHHHH		50.61-
271PhosphorylationNQLKESKSKIDALSS
HHHHHCHHHHHHHHH		44.0924719451
272UbiquitinationQLKESKSKIDALSSE
HHHHCHHHHHHHHHH		48.63-
277PhosphorylationKSKIDALSSEKLNLQ
HHHHHHHHHHHHCCC		37.8730622161
278PhosphorylationSKIDALSSEKLNLQK
HHHHHHHHHHHCCCH		39.3330622161
280UbiquitinationIDALSSEKLNLQKDL
HHHHHHHHHCCCHHH		44.62-
285UbiquitinationSEKLNLQKDLETRPT
HHHHCCCHHHCCCCC		68.40-
300UbiquitinationQHELRLYKQQVKKLE
HHHHHHHHHHHHHHH		38.55-
315UbiquitinationKALKKNVKLQELINH
HHHHHCCCHHHHHHC		54.57-
323UbiquitinationLQELINHKKAEDTEK
HHHHHHCCCHHHCCC		49.55-
324UbiquitinationQELINHKKAEDTEKK
HHHHHCCCHHHCCCC		49.83-
336UbiquitinationEKKDEPSKYNQQQAL
CCCCCCCHHHHHHHH		59.96-
357PhosphorylationQVLCSINSIIHNPRA
HHHHHHHHHHCCCCC		22.6530631047
370UbiquitinationRAPVIIYKQTKGGVQ
CCCEEEEECCCCCCC		40.87-
370 (in isoform 2)Ubiquitination-40.87-
373UbiquitinationVIIYKQTKGGVQNFN
EEEEECCCCCCCCCC		51.69-
427UbiquitinationLVPWLNLKKQDENEG
HHHHHCCCCCCCCCC		47.522190698
427 (in isoform 1)Ubiquitination-47.5221906983
427 (in isoform 2)Ubiquitination-47.5221906983
428UbiquitinationVPWLNLKKQDENEGI
HHHHCCCCCCCCCCC		67.17-
471PhosphorylationQTLQAIVSHFQKLFD
HHHHHHHHHHHHHHC		16.6929391485
493PhosphorylationYPRMNEVYTRLGEMN
CCHHHHHHHHHHHHH		4.6722210691
494PhosphorylationPRMNEVYTRLGEMNN
CHHHHHHHHHHHHHH		25.2922210691
593UbiquitinationVPAVKKLKVLSY---
HHHHHHCCCCCC---		50.43-
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 CEP70_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CEP70_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 CEP70_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
KANL1_HUMANKANSL1physical
16189514
ENKD1_HUMANENKD1physical
16189514
ZBT8A_HUMANZBTB8Aphysical
16189514
KDM1A_HUMANKDM1Aphysical
23455924
SUV92_HUMANSUV39H2physical
23455924
TBA3C_HUMANTUBA3Cphysical
23443559
HNRPU_HUMANHNRNPUphysical
23443559
GRP78_HUMANHSPA5physical
23443559
CEP70_HUMANCEP70physical
25416956
CLPB_HUMANCLPBphysical
25416956
TTC25_HUMANTTC25physical
25416956
ENKD1_HUMANENKD1physical
25416956
F161A_HUMANFAM161Aphysical
25416956
ZGPAT_HUMANZGPATphysical
25416956
BEX2_HUMANBEX2physical
25416956
ZN587_HUMANZNF587physical
25416956
ZN439_HUMANZNF439physical
25416956
SYTL4_HUMANSYTL4physical
25416956
SYTL5_HUMANSYTL5physical
25416956
LENG8_HUMANLENG8physical
25416956
HAUS1_HUMANHAUS1physical
25416956
SFR1_HUMANSFR1physical
25416956
HMGB4_HUMANHMGB4physical
25416956
ZN572_HUMANZNF572physical
25416956
ZN578_HUMANZNF578physical
25416956
ZN417_HUMANZNF417physical
25416956
ZN555_HUMANZNF555physical
25416956
ZBT49_HUMANZBTB49physical
25416956
ZN366_HUMANZNF366physical
25416956
TXLNB_HUMANTXLNBphysical
25416956
ZN169_HUMANZNF169physical
25416956
ZC3H1_HUMANZFC3H1physical
25416956
F124A_HUMANFAM124Aphysical
25416956
CFA53_HUMANCFAP53physical
25416956
FA13C_HUMANFAM13Cphysical
25416956
TTL10_HUMANTTLL10physical
25416956
T10IP_HUMANTSGA10IPphysical
25416956
KANL1_HUMANKANSL1physical
25416956
CE57L_HUMANCEP57L1physical
25416956
F133A_HUMANFAM133Aphysical
25416956
TRI42_HUMANTRIM42physical
25416956
ZN607_HUMANZNF607physical
21516116
HDAC6_HUMANHDAC6physical
26112604
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 CEP70_HUMAN

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Related Literatures of Post-Translational Modification

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