F172A_HUMAN - dbPTM
F172A_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID F172A_HUMAN
UniProt AC Q8WUF8
Protein Name Protein FAM172A
Gene Name FAM172A
Organism Homo sapiens (Human).
Sequence Length 416
Subcellular Localization Secreted .
Protein Description
Protein Sequence MSISLSSLILLPIWINMAQIQQGGPDEKEKTTALKDLLSRIDLDELMKKDEPPLDFPDTLEGFEYAFNEKGQLRHIKTGEPFVFNYREDLHRWNQKRYEALGEIITKYVYELLEKDCNLKKVSIPVDATESEPKSFIFMSEDALTNPQKLMVLIHGSGVVRAGQWARRLIINEDLDSGTQIPFIKRAVAEGYGVIVLNPNENYIEVEKPKIHVQSSSDSSDEPAEKRERKDKVSKETKKRRDFYEKYRNPQREKEMMQLYIRENGSPEEHAIYVWDHFIAQAAAENVFFVAHSYGGLAFVELMIQREADVKNKVTAVALTDSVHNVWHQEAGKTIREWMRENCCNWVSSSEPLDTSVESMLPDCPRVSAGTDRHELTSWKSFPSIFKFFTEASEAKTSSLKPAVTRRSHRIKHEEL
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
35 (in isoform 2)Ubiquitination-43.8121890473
35 (in isoform 1)Ubiquitination-43.8121890473
35UbiquitinationKEKTTALKDLLSRID
HHHHHHHHHHHHCCC
43.8121890473
39PhosphorylationTALKDLLSRIDLDEL
HHHHHHHHCCCHHHH
34.1928060719
48UbiquitinationIDLDELMKKDEPPLD
CCHHHHHCCCCCCCC
70.47-
49UbiquitinationDLDELMKKDEPPLDF
CHHHHHCCCCCCCCC
54.05-
98PhosphorylationHRWNQKRYEALGEII
HHHHHHHHHHHHHHH
16.76-
121UbiquitinationEKDCNLKKVSIPVDA
HHHCCCCEEECCCCC
44.36-
123PhosphorylationDCNLKKVSIPVDATE
HCCCCEEECCCCCCC
30.0129083192
129PhosphorylationVSIPVDATESEPKSF
EECCCCCCCCCCCCE
35.2629083192
131PhosphorylationIPVDATESEPKSFIF
CCCCCCCCCCCCEEE
55.6429083192
135PhosphorylationATESEPKSFIFMSED
CCCCCCCCEEEECCC
34.0029083192
140PhosphorylationPKSFIFMSEDALTNP
CCCEEEECCCCCCCC
22.9029083192
145PhosphorylationFMSEDALTNPQKLMV
EECCCCCCCCCEEEE
46.7229083192
185UbiquitinationGTQIPFIKRAVAEGY
CCCCHHHHHHHHCCC
34.38-
215PhosphorylationKPKIHVQSSSDSSDE
CCEEEEECCCCCCCC
30.6220363803
216PhosphorylationPKIHVQSSSDSSDEP
CEEEEECCCCCCCCH
22.5225159151
217PhosphorylationKIHVQSSSDSSDEPA
EEEEECCCCCCCCHH
46.9225159151
219PhosphorylationHVQSSSDSSDEPAEK
EEECCCCCCCCHHHH
41.4525159151
220PhosphorylationVQSSSDSSDEPAEKR
EECCCCCCCCHHHHH
51.4925159151
223UbiquitinationSSDSSDEPAEKRERK
CCCCCCCHHHHHHHH
51.1921890473
260PhosphorylationEKEMMQLYIRENGSP
HHHHHHHHHHHCCCH
4.8925159151
287UbiquitinationAQAAAENVFFVAHSY
HHHHHHCCEEEEECC
2.7221890473
333 (in isoform 1)Ubiquitination-48.0721890473
333UbiquitinationVWHQEAGKTIREWMR
HHHHHHHHHHHHHHH
48.0721890473
381PhosphorylationHELTSWKSFPSIFKF
HHHCCCHHCHHHHHH
35.8127499020
384PhosphorylationTSWKSFPSIFKFFTE
CCCHHCHHHHHHHHH
38.3524719451
401AcetylationEAKTSSLKPAVTRRS
HHHCCCCCHHHCCCH
32.6425953088
408PhosphorylationKPAVTRRSHRIKHEE
CHHHCCCHHHCCCCC
17.52-
412SumoylationTRRSHRIKHEEL---
CCCHHHCCCCCC---
44.94-
412SumoylationTRRSHRIKHEEL---
CCCHHHCCCCCC---
44.94-

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 F172A_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of F172A_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 F172A_HUMAN !!

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

Oops, there are no PPI records of F172A_HUMAN !!

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 F172A_HUMAN

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Related Literatures of Post-Translational Modification

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