EFHC1_HUMAN - dbPTM
EFHC1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID EFHC1_HUMAN
UniProt AC Q5JVL4
Protein Name EF-hand domain-containing protein 1
Gene Name EFHC1
Organism Homo sapiens (Human).
Sequence Length 640
Subcellular Localization Cytoplasm, cytoskeleton, microtubule organizing center, centrosome . Cytoplasm, cytoskeleton, spindle . Cytoplasm, cytoskeleton, spindle pole .
Protein Description Microtubule-associated protein which regulates cell division and neuronal migration during cortical development. Necessary for mitotic spindle organization. [PubMed: 19734894]
Protein Sequence MVSNPVHGLPFLPGTSFKDSTKTAFHRSQTLSYRNGYAIVRRPTVGIGGDRLQFNQLSQAELDELASKAPVLTYGQPKQAPPADFIPAHVAFDKKVLKFDAYFQEDVPMSTEEQYRIRQVNIYYYLEDDSMSVIEPVVENSGILQGKLIKRQRLAKNDRGDHYHWKDLNRGINITIYGKTFRVVDCDQFTQVFLESQGIELNPPEKMALDPYTELRKQPLRKYVTPSDFDQLKQFLTFDKQVLRFYAIWDDTDSMYGECRTYIIHYYLMDDTVEIREVHERNDGRDPFPLLMNRQRVPKVLVENAKNFPQCVLEISDQEVLEWYTAKDFIVGKSLTILGRTFFIYDCDPFTRRYYKEKFGITDLPRIDVSKREPPPVKQELPPYNGFGLVEDSAQNCFALIPKAPKKDVIKMLVNDNKVLRYLAVLESPIPEDKDRRFVFSYFLATDMISIFEPPVRNSGIIGGKYLGRTKVVKPYSTVDNPVYYGPSDFFIGAVIEVFGHRFIILDTDEYVLKYMESNAAQYSPEALASIQNHVRKREAPAPEAESKQTEKDPGVQELEALIDTIQKQLKDHSCKDNIREAFQIYDKEASGYVDRDMFFKICESLNVPVDDSLVKELIRMCSHGEGKINYYNFVRAFSN
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
18AcetylationFLPGTSFKDSTKTAF
CCCCCCCCCCCCCCC
51.0025038526
30PhosphorylationTAFHRSQTLSYRNGY
CCCHHHCCCEEECCE
20.9328857561
58PhosphorylationRLQFNQLSQAELDEL
CCCCCCCCHHHHHHH
19.9930622161
102PhosphorylationKVLKFDAYFQEDVPM
CCCCEEEECCCCCCC
13.9824425749
111PhosphorylationQEDVPMSTEEQYRIR
CCCCCCCHHHHHEEE
36.97-
115PhosphorylationPMSTEEQYRIRQVNI
CCCHHHHHEEEEEEE
15.9924425749
212PhosphorylationEKMALDPYTELRKQP
HHHCCCCCHHHHCCC
16.7127642862
227PhosphorylationLRKYVTPSDFDQLKQ
HHHCCCHHHHHHHHH
41.3625693802
233AcetylationPSDFDQLKQFLTFDK
HHHHHHHHHHHHCCH
33.1125038526
237PhosphorylationDQLKQFLTFDKQVLR
HHHHHHHHCCHHHHH
30.9526657352
246PhosphorylationDKQVLRFYAIWDDTD
CHHHHHHEEEECCCC
7.2526657352
254PhosphorylationAIWDDTDSMYGECRT
EEECCCCCCHHHHHE
18.9226657352
341PhosphorylationSLTILGRTFFIYDCD
CEEECCCEEEEEECC
22.54-
345PhosphorylationLGRTFFIYDCDPFTR
CCCEEEEEECCHHHH
12.83-
351PhosphorylationIYDCDPFTRRYYKEK
EEECCHHHHHHHHHH
21.45-
358UbiquitinationTRRYYKEKFGITDLP
HHHHHHHHHCCCCCC
44.75-
465AcetylationNSGIIGGKYLGRTKV
CCCCCCCEECCCCEE
31.8925038526
523PhosphorylationMESNAAQYSPEALAS
HHHCHHHCCHHHHHH
22.8228555341
524PhosphorylationESNAAQYSPEALASI
HHCHHHCCHHHHHHH
12.2725159151
548AcetylationPAPEAESKQTEKDPG
CCCHHHHHCCCCCCC
53.3925038526
552AcetylationAESKQTEKDPGVQEL
HHHHCCCCCCCHHHH
73.0225038526
588AcetylationEAFQIYDKEASGYVD
HHHHHHCCCCCCCCC
37.9025038526

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 EFHC1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of EFHC1_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 EFHC1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
BRAP_HUMANBRAPphysical
28514442
HAUS4_HUMANHAUS4physical
28514442
HAUS1_HUMANHAUS1physical
28514442
CC150_HUMANCCDC150physical
27173435
COA7_HUMANCOA7physical
27173435

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of EFHC1_HUMAN

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Related Literatures of Post-Translational Modification

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