F111A_HUMAN - dbPTM
F111A_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID F111A_HUMAN
UniProt AC Q96PZ2
Protein Name Protein FAM111A
Gene Name FAM111A
Organism Homo sapiens (Human).
Sequence Length 611
Subcellular Localization Nucleus. Cytoplasm. Mainly localizes to nucleus: colocalizes with PCNA on replication sites.
Protein Description Chromatin-associated protein required for PCNA loading on replication sites. Promotes S-phase entry and DNA synthesis. [PubMed: 24561620 May directly function at replication forks, explaining why Simian virus 40 (SV40) interacts with FAM111A to overcome host range restriction]
Protein Sequence MSCKKQRSRKHSVNEKCNMKIEHYFSPVSKEQQNNCSTSLMRMESRGDPRATTNTQAQRFHSPKKNPEDQTMPQNRTIYVTLKVNHRRNQDMKLKLTHSENSSLYMALNTLQAVRKEIETHQGQEMLVRGTEGIKEYINLGMPLSCFPEGGQVVITFSQSKSKQKEDNHIFGRQDKASTECVKFYIHAIGIGKCKRRIVKCGKLHKKGRKLCVYAFKGETIKDALCKDGRFLSFLENDDWKLIENNDTILESTQPVDELEGRYFQVEVEKRMVPSAAASQNPESEKRNTCVLREQIVAQYPSLKRESEKIIENFKKKMKVKNGETLFELHRTTFGKVTKNSSSIKVVKLLVRLSDSVGYLFWDSATTGYATCFVFKGLFILTCRHVIDSIVGDGIEPSKWATIIGQCVRVTFGYEELKDKETNYFFVEPWFEIHNEELDYAVLKLKENGQQVPMELYNGITPVPLSGLIHIIGHPYGEKKQIDACAVIPQGQRAKKCQERVQSKKAESPEYVHMYTQRSFQKIVHNPDVITYDTEFFFGASGSPVFDSKGSLVAMHAAGFAYTYQNETRSIIEFGSTMESILLDIKQRHKPWYEEVFVNQQDVEMMSDEDL
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
12PhosphorylationKQRSRKHSVNEKCNM
HHHHCCCCHHHHHCC		29.6729743597
16UbiquitinationRKHSVNEKCNMKIEH
CCCCHHHHHCCEEEE		26.21-
20SumoylationVNEKCNMKIEHYFSP
HHHHHCCEEEEECCC		30.8328112733
20UbiquitinationVNEKCNMKIEHYFSP
HHHHHCCEEEEECCC		30.83-
24PhosphorylationCNMKIEHYFSPVSKE
HCCEEEEECCCCCHH		7.9230266825
26PhosphorylationMKIEHYFSPVSKEQQ
CEEEEECCCCCHHHH		19.7530266825
29PhosphorylationEHYFSPVSKEQQNNC
EEECCCCCHHHHCCC		33.5830266825
30UbiquitinationHYFSPVSKEQQNNCS
EECCCCCHHHHCCCC		60.83-
30SumoylationHYFSPVSKEQQNNCS
EECCCCCHHHHCCCC		60.8328112733
53PhosphorylationRGDPRATTNTQAQRF
CCCCCCCCCHHHHHH		34.9726074081
55PhosphorylationDPRATTNTQAQRFHS
CCCCCCCHHHHHHCC		24.1626074081
62PhosphorylationTQAQRFHSPKKNPED
HHHHHHCCCCCCHHH		35.3923401153
64UbiquitinationAQRFHSPKKNPEDQT
HHHHCCCCCCHHHCC		69.10-
65UbiquitinationQRFHSPKKNPEDQTM
HHHCCCCCCHHHCCC		79.64-
65SumoylationQRFHSPKKNPEDQTM
HHHCCCCCCHHHCCC		79.6428112733
71PhosphorylationKKNPEDQTMPQNRTI
CCCHHHCCCCCCCEE		43.0425404012
97PhosphorylationQDMKLKLTHSENSSL
CCCEEEEEECCCHHH		23.0526074081
99PhosphorylationMKLKLTHSENSSLYM
CEEEEEECCCHHHHH		32.9826074081
102PhosphorylationKLTHSENSSLYMALN
EEEECCCHHHHHHHH		20.0526074081
103PhosphorylationLTHSENSSLYMALNT
EEECCCHHHHHHHHH		34.7926074081
105PhosphorylationHSENSSLYMALNTLQ
ECCCHHHHHHHHHHH		5.1426074081
110PhosphorylationSLYMALNTLQAVRKE
HHHHHHHHHHHHHHH		22.5426074081
116SumoylationNTLQAVRKEIETHQG
HHHHHHHHHHHHHCC		57.34-
116UbiquitinationNTLQAVRKEIETHQG
HHHHHHHHHHHHHCC		57.34-
116SumoylationNTLQAVRKEIETHQG
HHHHHHHHHHHHHCC		57.34-
163UbiquitinationTFSQSKSKQKEDNHI
EEECCCCCCCCCCCC		69.95-
165UbiquitinationSQSKSKQKEDNHIFG
ECCCCCCCCCCCCCC		71.43-
176UbiquitinationHIFGRQDKASTECVK
CCCCCCCCCHHHHHH		35.58-
270UbiquitinationYFQVEVEKRMVPSAA
EEEEEEEEECCCCHH		51.47-
272SulfoxidationQVEVEKRMVPSAAAS
EEEEEEECCCCHHHH		8.4421406390
279PhosphorylationMVPSAAASQNPESEK
CCCCHHHHCCCHHHH		26.26-
286UbiquitinationSQNPESEKRNTCVLR
HCCCHHHHCCCEEHH		61.2921906983
304MethylationVAQYPSLKRESEKII
HHHCHHHHHHHHHHH		59.46-
304UbiquitinationVAQYPSLKRESEKII
HHHCHHHHHHHHHHH		59.46-
309UbiquitinationSLKRESEKIIENFKK
HHHHHHHHHHHHHHH		59.26-
315UbiquitinationEKIIENFKKKMKVKN
HHHHHHHHHHHCCCC		64.17-
316UbiquitinationKIIENFKKKMKVKNG
HHHHHHHHHHCCCCC		54.70-
317UbiquitinationIIENFKKKMKVKNGE
HHHHHHHHHCCCCCC		44.54-
321UbiquitinationFKKKMKVKNGETLFE
HHHHHCCCCCCEEEE		54.43-
336UbiquitinationLHRTTFGKVTKNSSS
EEECCCCCCCCCCCH		42.41-
480UbiquitinationGHPYGEKKQIDACAV
CCCCCCCCCCCEEEE		48.46-
505UbiquitinationQERVQSKKAESPEYV
HHHHHHCCCCCHHHH		63.73-
508PhosphorylationVQSKKAESPEYVHMY
HHHCCCCCHHHHHHH		28.0825159151
511PhosphorylationKKAESPEYVHMYTQR
CCCCCHHHHHHHHHC		10.07-
568PhosphorylationAYTYQNETRSIIEFG
EEEECCCCEEEEEEC		36.95-
607PhosphorylationQQDVEMMSDEDL---
HHHHHCCCCCCC---		36.2227422710
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 F111A_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of F111A_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 F111A_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
P53_HUMANTP53physical
28514442
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
127000Kenny-Caffey syndrome 2 (KCS2)
602361Gracile bone dysplasia (GCLEB)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of F111A_HUMAN

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Related Literatures of Post-Translational Modification

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