FREM1_HUMAN - dbPTM
FREM1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FREM1_HUMAN
UniProt AC Q5H8C1
Protein Name FRAS1-related extracellular matrix protein 1 {ECO:0000305}
Gene Name FREM1 {ECO:0000312|HGNC:HGNC:23399}
Organism Homo sapiens (Human).
Sequence Length 2179
Subcellular Localization Secreted, extracellular space, extracellular matrix, basement membrane. Localizes at the basement membrane zone of embryonic epidermis and hair follicles..
Protein Description Extracellular matrix protein that plays a role in epidermal differentiation and is required for epidermal adhesion during embryonic development..
Protein Sequence MNSLSWGAANAVLLLLLLAWASPTFISINRGVRVMKGHSAFLSGDDLKFAIPKEKDACKVEVVMNEPITQRVGKLTPQVFDCHFLPNEVKYVHNGCPILDEDTVKLRLYRFTERDTFIETFILWVYLLEPDCNIIHMSNNVLEVPEFNGLSQAIDKNLLRFDYDRMASLECTVSLDTARTRLPAHGQMVLGEPRPEEPRGDQPHSFFPESQLRAKLKCPGGSCTPGLKKIGSLKVSCEEFLLMGLRYQHLDPPSPNIDYISIQLDLTDTRSKIVYKSESAWLPVYIRAGIPNQIPKAAFMAVFILEVDQFILTSLTTSVLDCEEDETPKPLLVFNITKAPLQGYVTHLLDHTRPISSFTWKDLSDMQIAYQPPNSSHSERRHDEVELEVYDFFFERSAPMTVHISIRTADTNAPRVSWNTGLSLLEGQSRAITWEQFQVVDNDDIGAVRLVTVGGLQHGWLTLRGGKGFLFTVADLQAGVVRYHHDDSDSTKDFVVFRIFDGHHSIRHKFPINVLPKDDSPPFLITNVVIELEEGQTILIQGSMLRASDVDASDDYIFFNITKPPQAGEIMKKPGPGLIGYPVHGFLQRDLFNGIIYYRHFGGEIFEDSFQFVLWDSHEPPNLSVPQVATIHITPVDDQLPKEAPGVSRHLVVKETEVAYITKKQLHFIDSESYDRELVYTITTPPFFSFSHRHLDAGKLFMVDSIPKVVKNPTALELRSFTQHAVNYMKVAYMPPMQDIGPHCRDVQFTFSVSNQHGGTLHGICFNITILPVDNQVPEAFTNPLKVTEGGQSIISTEHILISDADTKLDNIDLSLRELPLHGRVELNGFPLNSGGTFSWGDLHTLKVRYQHDGTEVLQDDLLLEVTDGTNSAEFVLHVEVFPVNDEPPVLKADLMPVMNCSEGGEVVITSEYIFATDVDSDNLKLMFVIAREPQHGVVRRAGVTVDQFSQRDVISEAVTYKHTGGEIGLMPCFDTITLVVSDGEAGPFVNGCCYNGPNPSVPLHASFPVYDLNITVYPVDNQPPSIAIGPVFVVDEGCSTALTVNHLSATDPDTAADDLEFVLVSPPQFGYLENILPSVGFEKSNIGISIDSFQWKDMNAFHINYVQSRHLRIEPTADQFTVYVTDGKHHSLEIPFSIIINPTNDEAPDFVVQNITVCEGQMKELDSSIISAVDLDIPQDALLFSITQKPRHGLLIDRGFSKDFSENKQPANPHQKHAPVHSFSMELLKTGMRLTYMHDDSESLADDFTIQLSDGKHKILKTISVEVIPVNDEKPMLSKKAEIAMNMGETRIISSAILSAIDEDSPREKIYYVFERLPQNGQLQLKIGRDWVPLSPGMKCTQEEVDLNLLRYTHTGAMDSQNQDSFTFYLWDGNNRSPALDCQITIKDMEKGDIVILTKPLVVSKGDRGFLTTTTLLAVDGTDKPEELLYVITSPPRYGQIEYVHYPGVPITNFSQMDVVGQTVCYVHKSKVTVSSDRFRFIISNGLRTEHGVFEITLETVDRALPVVTRNKGLRLAQGAVGLLSPDLLQLTDPDTPAENLTFLLVQLPQHGQLYLWGTGLLQHNFTQQDVDSKNVAYRHSGGDSQTDCFTFMATDGTNQGFIVNGRVWEEPVLFTIQVDQLDKTAPRITLLHSPSQVGLLKNGCYGIYITSRVLKASDPDTEDDQIIFKILQGPKHGHLENTTTGEFIHEKFSQKDLNSKTILYIINPSLEVNSDTVEFQIMDPTGNSATPQILELKWSHIEWSQTEYEVCENVGLLPLEIIRRGYSMDSAFVGIKVNQVSAAVGKDFTVIPSKLIQFDPGMSTKMWNIAITYDGLEEDDEVFEVILNSPVNAVLGTKTKAAVKILDSKGGQCHPSYSSNQSKHSTWEKGIWHLLPPGSSSSTTSGSFHLERRPLPSSMQLAVIRGDTLRGFDSTDLSQRKLRTRGNGKTVRPSSVYRNGTDIIYNYHGIVSLKLEDDSFPTHKRKAKVSIISQPQKTIKVAELPQADKVESTTDSHFPRQDQLPSFPKNCTLELKGLFHFEEGIQKLYQCNGIAWKAWSPQTKDVEDKSCPAGWHQHSGYCHILITEQKGTWNAAAQACREQYLGNLVTVFSRQHMRWLWDIGGRKSFWIGLNDQVHAGHWEWIGGEPVAFTNGRRGPSQRSKLGKSCVLVQRQGKWQTKDCRRAKPHNYVCSRKL
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
43PhosphorylationKGHSAFLSGDDLKFA
CCCCEEECCCCCCCC
33.45-
112PhosphorylationKLRLYRFTERDTFIE
EEEEEECCCCCCHHH
22.5524275569
163PhosphorylationKNLLRFDYDRMASLE
HCCCCCCHHHHHCCE
11.61-
204 (in isoform 4)Phosphorylation-31.4429116813
222PhosphorylationKLKCPGGSCTPGLKK
CCCCCCCCCCCCHHH
22.2624719451
335N-linked_GlycosylationPKPLLVFNITKAPLQ
CCCEEEEEECCCCCC
33.27UniProtKB CARBOHYD
405PhosphorylationAPMTVHISIRTADTN
CCEEEEEEEEECCCC
7.3724719451
560N-linked_GlycosylationSDDYIFFNITKPPQA
CCCEEEEEECCCCCC
30.21UniProtKB CARBOHYD
622N-linked_GlycosylationWDSHEPPNLSVPQVA
ECCCCCCCCCCCCEE
56.51UniProtKB CARBOHYD
714PhosphorylationPKVVKNPTALELRSF
CCCCCCCCHHHHHHH
53.9525002506
815PhosphorylationKLDNIDLSLRELPLH
CHHCCCEEECCCCCC
22.9524719451
950PhosphorylationGVTVDQFSQRDVISE
CCCHHHCCCHHHHCC
20.76-
1014N-linked_GlycosylationSFPVYDLNITVYPVD
ECCEEEEEEEEEECC
25.61UniProtKB CARBOHYD
1223PhosphorylationQKHAPVHSFSMELLK
CCCCCCCHHHHHHHH
21.17-
1306PhosphorylationLSAIDEDSPREKIYY
HHHCCCCCCHHHEEE
24.65-
1312PhosphorylationDSPREKIYYVFERLP
CCCHHHEEEEEECCC
12.49-
1353PhosphorylationVDLNLLRYTHTGAMD
HCHHHEEEECCCCCC
11.6624043423
1354PhosphorylationDLNLLRYTHTGAMDS
CHHHEEEECCCCCCC
13.4124043423
1356PhosphorylationNLLRYTHTGAMDSQN
HHEEEECCCCCCCCC
20.8824043423
1361PhosphorylationTHTGAMDSQNQDSFT
ECCCCCCCCCCCCEE
20.2524043423
1366PhosphorylationMDSQNQDSFTFYLWD
CCCCCCCCEEEEEEC
19.2024043423
1368PhosphorylationSQNQDSFTFYLWDGN
CCCCCCEEEEEECCC
18.4724043423
1370PhosphorylationNQDSFTFYLWDGNNR
CCCCEEEEEECCCCC
12.1124043423
1439PhosphorylationVITSPPRYGQIEYVH
EEECCCCCCCEEEEE
21.1124043423
1444PhosphorylationPRYGQIEYVHYPGVP
CCCCCEEEEECCCCC
8.3124043423
1447PhosphorylationGQIEYVHYPGVPITN
CCEEEEECCCCCCCC
7.5224043423
1453PhosphorylationHYPGVPITNFSQMDV
ECCCCCCCCCHHCCC
24.9224043423
1456PhosphorylationGVPITNFSQMDVVGQ
CCCCCCCHHCCCCCC
27.0224043423
1464PhosphorylationQMDVVGQTVCYVHKS
HCCCCCCEEEEEECC
13.4524043423
1467PhosphorylationVVGQTVCYVHKSKVT
CCCCEEEEEECCEEE
10.9724043423
1566N-linked_GlycosylationGTGLLQHNFTQQDVD
CCCCCCCCCCCCCCC
28.80UniProtKB CARBOHYD
1631PhosphorylationDKTAPRITLLHSPSQ
CCCCCEEEEECCHHH
25.2525921289
1635PhosphorylationPRITLLHSPSQVGLL
CEEEEECCHHHHCCC
26.6425921289
1768PhosphorylationLEIIRRGYSMDSAFV
HHHHHCCCCCCCCEE
10.06-
1769PhosphorylationEIIRRGYSMDSAFVG
HHHHCCCCCCCCEEC
20.9529116813
1772PhosphorylationRRGYSMDSAFVGIKV
HCCCCCCCCEECEEH
18.2429116813
1783PhosphorylationGIKVNQVSAAVGKDF
CEEHHEEEECCCCCE
10.7629116813
1791PhosphorylationAAVGKDFTVIPSKLI
ECCCCCEEEEEHHHE
27.8825954137
1795PhosphorylationKDFTVIPSKLIQFDP
CCEEEEEHHHEECCC
29.0425954137
1858PhosphorylationKGGQCHPSYSSNQSK
CCCCCCCCCCCCCCC
17.62-
1859PhosphorylationGGQCHPSYSSNQSKH
CCCCCCCCCCCCCCC
22.14-
1900PhosphorylationERRPLPSSMQLAVIR
EECCCCCCCEEEEEE
14.49-
1910PhosphorylationLAVIRGDTLRGFDST
EEEEECCCCCCCCCC
22.60-
1943PhosphorylationSSVYRNGTDIIYNYH
HHHEECCCEEEEEEC
27.81-
1954PhosphorylationYNYHGIVSLKLEDDS
EEECCEEEEEECCCC
20.19-
1964PhosphorylationLEDDSFPTHKRKAKV
ECCCCCCCCCCCEEE
37.71-
1970UbiquitinationPTHKRKAKVSIISQP
CCCCCCEEEEEECCC
39.28-
1995O-linked_GlycosylationQADKVESTTDSHFPR
CCCCCCCCCCCCCCC
22.55OGP
1996O-linked_GlycosylationADKVESTTDSHFPRQ
CCCCCCCCCCCCCCH
44.79OGP
2142PhosphorylationTNGRRGPSQRSKLGK
CCCCCCHHHHHHCCC
40.84-

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 FREM1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of FREM1_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 FREM1_HUMAN !!

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

Oops, there are no PPI records of FREM1_HUMAN !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of FREM1_HUMAN

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Related Literatures of Post-Translational Modification

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