PACE1_HUMAN - dbPTM
PACE1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PACE1_HUMAN
UniProt AC Q8IZE3
Protein Name Protein-associating with the carboxyl-terminal domain of ezrin
Gene Name SCYL3
Organism Homo sapiens (Human).
Sequence Length 742
Subcellular Localization Cytoplasm . Golgi apparatus . Cell projection, lamellipodium . Colocalized with EZR/VIL2, actin and CD44 in lamellipodia.
Protein Description May play a role in regulating cell adhesion/migration complexes in migrating cells..
Protein Sequence MGSENSALKSYTLREPPFTLPSGLAVYPAVLQDGKFASVFVYKRENEDKVNKAAKHLKTLRHPCLLRFLSCTVEADGIHLVTERVQPLEVALETLSSAEVCAGIYDILLALIFLHDRGHLTHNNVCLSSVFVSEDGHWKLGGMETVCKVSQATPEFLRSIQSIRDPASIPPEEMSPEFTTLPECHGHARDAFSFGTLVESLLTILNEQVSADVLSSFQQTLHSTLLNPIPKCRPALCTLLSHDFFRNDFLEVVNFLKSLTLKSEEEKTEFFKFLLDRVSCLSEELIASRLVPLLLNQLVFAEPVAVKSFLPYLLGPKKDHAQGETPCLLSPALFQSRVIPVLLQLFEVHEEHVRMVLLSHIEAYVEHFTQEQLKKVILPQVLLGLRDTSDSIVAITLHSLAVLVSLLGPEVVVGGERTKIFKRTAPSFTKNTDLSLEDSPMCVVCSHHSQISPILENPFSSIFPKCFFSGSTPINSKKHIQRDYYNTLLQTGDPFSQPIKFPINGLSDVKNTSEDSENFPSSSKKSEEWPDWSEPEEPENQTVNIQIWPREPCDDVKSQCTTLDVEESSWDDCEPSSLDTKVNPGGGITATKPVTSGEQKPIPALLSLTEESMPWKSSLPQKISLVQRGDDADQIEPPKVSSQERPLKVPSELGLGEEFTIQVKKKPVKDPEMDWFADMIPEIKPSAAFLILPELRTEMVPKKDDVSPVMQFSSKFAAAEITEGEAEGWEEEGELNWEDNNW
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
2Myristoylation------MGSENSALK
------CCCCCCCCC
43.6012651155
2N-myristoyl glycine------MGSENSALK
------CCCCCCCCC
43.60-
12PhosphorylationNSALKSYTLREPPFT
CCCCCCCCCCCCCCC
26.8224719451
70PhosphorylationPCLLRFLSCTVEADG
HHHHHHHHCEEEECC
12.6724247654
72PhosphorylationLLRFLSCTVEADGIH
HHHHHHCEEEECCEE
20.2927251275
125UbiquitinationGHLTHNNVCLSSVFV
CCCCCCCEEEEEEEE
4.1623000965
130UbiquitinationNNVCLSSVFVSEDGH
CCEEEEEEEECCCCC
5.0221890473
153PhosphorylationVCKVSQATPEFLRSI
EEEHHHCCHHHHHHH
18.7323927012
258PhosphorylationEVVNFLKSLTLKSEE
HHHHHHHHCCCCCHH
28.8224719451
267UbiquitinationTLKSEEEKTEFFKFL
CCCCHHHHHHHHHHH
57.5423000965
272 (in isoform 2)Ubiquitination-40.1821890473
272 (in isoform 1)Ubiquitination-40.1821890473
272UbiquitinationEEKTEFFKFLLDRVS
HHHHHHHHHHHHHHH
40.1823000965
308AcetylationAEPVAVKSFLPYLLG
CCCCHHHHHHHHHHC
25.9719413330
364PhosphorylationLLSHIEAYVEHFTQE
HHHHHHHHHHHCCHH
8.12-
369PhosphorylationEAYVEHFTQEQLKKV
HHHHHHCCHHHHHHH
32.86-
389PhosphorylationLLGLRDTSDSIVAIT
HHCCCCCCCHHHHHH
33.38-
391PhosphorylationGLRDTSDSIVAITLH
CCCCCCCHHHHHHHH
20.80-
405PhosphorylationHSLAVLVSLLGPEVV
HHHHHHHHHHCCEEE
17.45-
424PhosphorylationRTKIFKRTAPSFTKN
CEEEEECCCCCCCCC
43.4423312004
427PhosphorylationIFKRTAPSFTKNTDL
EEECCCCCCCCCCCC
42.9824719451
429PhosphorylationKRTAPSFTKNTDLSL
ECCCCCCCCCCCCCC
27.9423312004
430UbiquitinationRTAPSFTKNTDLSLE
CCCCCCCCCCCCCCC
56.7029967540
435 (in isoform 2)Phosphorylation-32.3021815630
439PhosphorylationTDLSLEDSPMCVVCS
CCCCCCCCCEEEEEC
12.73-
446UbiquitinationSPMCVVCSHHSQISP
CCEEEEECCCCCCHH
16.7829967540
476PhosphorylationSGSTPINSKKHIQRD
CCCCCCCCCHHHCHH
43.7424260401
484PhosphorylationKKHIQRDYYNTLLQT
CHHHCHHHHHHHHHC
10.7821082442
487PhosphorylationIQRDYYNTLLQTGDP
HCHHHHHHHHHCCCC
16.8421082442
500UbiquitinationDPFSQPIKFPINGLS
CCCCCCCCCCCCCCC
52.34-
513PhosphorylationLSDVKNTSEDSENFP
CCCCCCCCCCCCCCC
49.1221815630
515PhosphorylationDVKNTSEDSENFPSS
CCCCCCCCCCCCCCC
62.1033259812
516PhosphorylationVKNTSEDSENFPSSS
CCCCCCCCCCCCCCC
30.3221815630
521PhosphorylationEDSENFPSSSKKSEE
CCCCCCCCCCCCCCC
43.0125627689
522PhosphorylationDSENFPSSSKKSEEW
CCCCCCCCCCCCCCC
46.5525627689
524UbiquitinationENFPSSSKKSEEWPD
CCCCCCCCCCCCCCC
63.37-
526PhosphorylationFPSSSKKSEEWPDWS
CCCCCCCCCCCCCCC
44.4728122231
533PhosphorylationSEEWPDWSEPEEPEN
CCCCCCCCCCCCCCC
51.1326657352
542PhosphorylationPEEPENQTVNIQIWP
CCCCCCCCEEEEEEC
27.4028122231
558PhosphorylationEPCDDVKSQCTTLDV
CCCCCHHHCCEEEEC
30.2728348404
561PhosphorylationDDVKSQCTTLDVEES
CCHHHCCEEEECCCC
23.8228348404
568PhosphorylationTTLDVEESSWDDCEP
EEEECCCCCCCCCCC
24.1925849741
569PhosphorylationTLDVEESSWDDCEPS
EEECCCCCCCCCCCH
37.4926657352
576PhosphorylationSWDDCEPSSLDTKVN
CCCCCCCHHCCCCCC
22.6528348404
577PhosphorylationWDDCEPSSLDTKVNP
CCCCCCHHCCCCCCC
40.7728348404
641PhosphorylationQIEPPKVSSQERPLK
HCCCCCCCCCCCCCC
32.2228102081
642PhosphorylationIEPPKVSSQERPLKV
CCCCCCCCCCCCCCC
38.7625159151
651PhosphorylationERPLKVPSELGLGEE
CCCCCCCCCCCCCCC
48.7326074081
653PhosphorylationPLKVPSELGLGEEFT
CCCCCCCCCCCCCEE
8.8932645325
707PhosphorylationVPKKDDVSPVMQFSS
CCCCCCCCHHHHHHH
20.8330266825
713PhosphorylationVSPVMQFSSKFAAAE
CCHHHHHHHHHEEEE
18.7426330541
714PhosphorylationSPVMQFSSKFAAAEI
CHHHHHHHHHEEEEC
32.8326330541

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 PACE1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PACE1_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 PACE1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
LHX8_HUMANLHX8physical
25416956

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 PACE1_HUMAN

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Related Literatures of Post-Translational Modification

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