UniProt ID | FREM2_HUMAN | |
---|---|---|
UniProt AC | Q5SZK8 | |
Protein Name | FRAS1-related extracellular matrix protein 2 | |
Gene Name | FREM2 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 3169 | |
Subcellular Localization |
Cell membrane Single-pass type I membrane protein Extracellular side . |
|
Protein Description | Extracellular matrix protein required for maintenance of the integrity of the skin epithelium and for maintenance of renal epithelia. May be required for epidermal adhesion.. | |
Protein Sequence | MHSAGTPGLSSRRTGNSTSFQPGPPPPPRLLLLLLLLLSLVSRVPAQPAAFGRALLSPGLAGAAGVPAEEAIVLANRGLRVPFGREVWLDPLHDLVLQVQPGDRCAVSVLDNDALAQRPGRLSPKRFPCDFGPGEVRYSHLGARSPSRDRVRLQLRYDAPGGAVVLPLVLEVEVVFTQLEVVTRNLPLVVEELLGTSNALDARSLEFAFQPETEECRVGILSGLGALPRYGELLHYPQVPGGAREGGAPETLLMDCKAFQELGVRYRHTAASRSPNRDWIPMVVELRSRGAPVGSPALKREHFQVLVRIRGGAENTAPKPSFVAMMMMEVDQFVLTALTPDMLAAEDAESPSDLLIFNLTSPFQPGQGYLVSTDDRSLPLSSFTQRDLRLLKIAYQPPSEDSDQERLFELELEVVDLEGAASDPFAFMVVVKPMNTMAPVVTRNTGLILYEGQSRPLTGPAGSGPQNLVISDEDDLEAVRLEVVAGLRHGHLVILGASSGSSAPKSFTVAELAAGQVVYQHDDRDGSLSDNLVLRMVDGGGRHQVQFLFPITLVPVDDQPPVLNANTGLTLAEGETVPILPLSLSATDMDSDDSLLLFVLESPFLTTGHLLLRQTHPPHEKQELLRGLWRKEGAFYERTVTEWQQQDITEGRLFYRHSGPHSPGPVTDQFTFRVQDNHDPPNQSGLQRFVIRIHPVDRLPPELGSGCPLRMVVQESQLTPLRKKWLRYTDLDTDDRELRYTVTQSPTDTDENHLPAPLGTLVLTDNPSVVVTHFTQAQINHHKIAYRPPGQELGVATRVAQFQFQVEDRAGNVAPGTFTLYLHPVDNQPPEILNTGFTIQEKGHHILSETELHVNDVDTDVAHISFTLTQAPKHGHMRVSGQILHVGGLFHLEDIKQGRVSYAHNGDKSLTDSCSLEVSDRHHVVPITLRVNVRPVDDEVPILSHPTGTLESYLDVLENGATEITANVIKGTNEETDDLMLTFLLEDPPLYGEILVNGIPAEQFTQRDILEGSVVYTHTSGEIGLLPKADSFNLSLSDMSQEWRIGGNTIQGVTIWVTILPVDSQAPEIFVGEQLIVMEGDKSVITSVHISAEDVDSLNDDILCTIVIQPTSGYVENISPAPGSEKSRAGIAISAFNLKDLRQGHINYVQSVHKGVEPVEDRFVFRCSDGINFSERQFFPIVIIPTNDEQPEMFMREFMVMEGMSLVIDTPILNAADADVPLDDLTFTITQFPTHGHIMNQLINGTVLVESFTLDQIIESSSIIYEHDDSETQEDSFVIKLTDGKHSVEKTVLIIVIPVDDETPRMTINNGLEIEIGDTKIINNKILMATDLDSEDKSLVYIIRYGPGHGLLQRRKPTGAFENITLGMNFTQDEVDRNLIQYVHLGQEGIRDLIKFDVTDGINPLIDRYFYVSIGSIDIVFPDVISKGVSLKEGGKVTLTTDLLSTSDLNSPDENLVFTITRAPMRGHLECTDQPGVSITSFTQLQLAGNKIYYIHTADDEVKMDSFEFQVTDGRNPVFRTFRISISDVDNKKPVVTIHKLVVSESENKLITPFELTVEDRDTPDKLLKFTITQVPIHGHLLFNNTRPVMVFTKQDLNENLISYKHDGTESSEDSFSFTVTDGTHTDFYVFPDTVFETRRPQVMKIQVLAVDNSVPQIAVNKGASTLRTLATGHLGFMITSKILKVEDRDSLHISLRFIVTEAPQHGYLLNLDKGNHSITQFTQADIDDMKICYVLREGANATSDMFYFAVEDGGGNKLTYQNFRLNWAWISFEKEYYLVNEDSKFLDVVLKRRGYLGETSFISIGTRDRTAEKDKDFKGKAQKQVQFNPGQTRATWRVRILSDGEHEQSETFQVVLSEPVLAALEFPTVATVEIVDPGDEPTVFIPQSKYSVEEDVGELFIPIRRSGDVSQELMVVCYTQQGTATGTVPTSVLSYSDYISRPEDHTSVVRFDKDEREKLCRIVIIDDSLYEEEETFHVLLSMPMGGRIGSEFPGAQVTIVPDKDDEPIFYFGDVEYSVDESAGYVEVQVWRTGTDLSKSSSVTVRSRKTDPPSADAGTDYVGISRNLDFAPGVNMQPVRVVILDDLGQPALEGIEKFELVLRMPMNAALGEPSKATVSINDSVSDLPKMQFKERIYTGSESDGQIVTMIHRTGDVQYRSSVRCYTRQGSAQVMMDFEERPNTDTSIITFLPGETEKPCILELMDDVLYEEVEELRLVLGTPQSNSPFGAAVGEQNETLIRIRDDADKTVIKFGETKFSVTEPKEPGESVVIRIPVIRQGDTSKVSIVRVHTKDGSATSGEDYHPVSEEIEFKEGETQHVVEIEVTFDGVREMREAFTVHLKPDENMIAEMQLTKAIVYIEEMSSMADVTFPSVPQIVSLLMYDDTSKAKESAEPMSGYPVICITACNPKYSDYDKTGSICASENINDTLTRYRWLISAPAGPDGVTSPMREVDFDTFFTSSKMVTLDSIYFQPGSRVQCAARAVNTNGDEGLELMSPIVTISREEGLCQPRVPGVVGAEPFSAKLRYTGPEDADYTNLIKLTVTMPHIDGMLPVISTRELSNFELTLSPDGTRVGNHKCSNLLDYTEVKTHYGFLTDATKNPEIIGETYPYQYSLSIRGSTTLRFYRNLNLEACLWEFVSYYDMSELLADCGGTIGTDGQVLNLVQSYVTLRVPLYVSYVFHSPVGVGGWQHFDLKSELRLTFVYDTAILWNDGIGSPPEAELQGSLYPTSMRIGDEGRLAVHFKTEAQFHGLFVLSHPASFTSSVIMSADHPGLTFSLRLIRSEPTYNQPVQQWSFVSDFAVRDYSGTYTVKLVPCTAPSHQEYRLPVTCNPREPVTFDLDIRFQQVSDPVAAEFSLNTQMYLLSKKSLWLSDGSMGFGQESDVAFAEGDIIYGRVMVDPVQNLGDSFYCSIEKVFLCTGADGYVPKYSPMNAEYGCLADSPSLLYRFKIVDKAQPETQATSFGNVLFNAKLAVDDPEAILLVNQPGSDGFKVDSTPLFQVALGREWYIHTIYTVRSKDNANRGIGKRSVEYHSLVSQGKPQSTTKSRKKREIRSTPSLAWEIGAENSRGTNIQHIALDRTKRQIPHGRAPPDGILPWELNSPSSAVSLVTVVGGTTVGLLTICLTVIAVLMCRGKESFRGKDAPKGSSSSEPMVPPQSHHNDSSEV | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
57 | Phosphorylation | AFGRALLSPGLAGAA HHHHHHCCCCCCCCC | 20.12 | - | |
108 | Phosphorylation | PGDRCAVSVLDNDAL CCCCEEEEEECCHHH | 9.84 | - | |
123 | Phosphorylation | AQRPGRLSPKRFPCD HCCCCCCCCCCCCCC | 27.32 | 26091039 | |
125 | Acetylation | RPGRLSPKRFPCDFG CCCCCCCCCCCCCCC | 64.39 | 30588857 | |
295 | Phosphorylation | SRGAPVGSPALKREH HCCCCCCCHHHCHHC | 13.77 | - | |
358 | N-linked_Glycosylation | PSDLLIFNLTSPFQP CCCEEEEECCCCCCC | 35.10 | UniProtKB CARBOHYD | |
498 | Phosphorylation | HLVILGASSGSSAPK EEEEEECCCCCCCCC | 33.17 | 28857561 | |
499 | Phosphorylation | LVILGASSGSSAPKS EEEEECCCCCCCCCC | 42.00 | 28857561 | |
501 | Phosphorylation | ILGASSGSSAPKSFT EEECCCCCCCCCCEE | 25.85 | 28857561 | |
502 | Phosphorylation | LGASSGSSAPKSFTV EECCCCCCCCCCEEH | 52.71 | 28857561 | |
786 | Phosphorylation | INHHKIAYRPPGQEL CCCCCEEECCCCCCC | 27.42 | - | |
797 | Phosphorylation | GQELGVATRVAQFQF CCCCCEEEEEEEEEE | 24.22 | - | |
880 | Phosphorylation | KHGHMRVSGQILHVG CCCCEEECCEEEEEC | 18.02 | - | |
982 | Phosphorylation | ETDDLMLTFLLEDPP CCCCEEEEEECCCCC | 9.77 | 24275569 | |
1134 | Phosphorylation | SRAGIAISAFNLKDL HCCCEEEEECCHHHH | 20.13 | 21964256 | |
1244 | N-linked_Glycosylation | HIMNQLINGTVLVES HHHHHHHCCEEEEEE | 48.99 | UniProtKB CARBOHYD | |
1291 | Phosphorylation | GKHSVEKTVLIIVIP CCCCEEEEEEEEEEE | 13.67 | - | |
1303 | Phosphorylation | VIPVDDETPRMTINN EEECCCCCCCEEECC | 24.16 | - | |
1319 | Phosphorylation | LEIEIGDTKIINNKI EEEEECCEEEECCEE | 20.94 | - | |
1369 | N-linked_Glycosylation | ENITLGMNFTQDEVD CCEEECCCCCHHHHH | 34.71 | UniProtKB CARBOHYD | |
1440 | Phosphorylation | EGGKVTLTTDLLSTS CCCEEEEEECCCCCC | 14.65 | 24719451 | |
1445 | Phosphorylation | TLTTDLLSTSDLNSP EEEECCCCCCCCCCC | 32.91 | 24719451 | |
1459 | Phosphorylation | PDENLVFTITRAPMR CCCCEEEEEECCCCC | 17.60 | 24719451 | |
1525 | Phosphorylation | VFRTFRISISDVDNK EEEEEEEEHHHCCCC | 16.28 | - | |
1527 | Phosphorylation | RTFRISISDVDNKKP EEEEEEHHHCCCCCC | 25.45 | - | |
1537 | Phosphorylation | DNKKPVVTIHKLVVS CCCCCEEEEEEEEEE | 20.00 | - | |
1584 | N-linked_Glycosylation | IHGHLLFNNTRPVMV ECCEEECCCCCCEEE | 49.27 | UniProtKB CARBOHYD | |
1695 | Phosphorylation | DRDSLHISLRFIVTE CCCCCEEEEEEEEEE | 11.62 | 24719451 | |
1741 | N-linked_Glycosylation | YVLREGANATSDMFY EEECCCCCCCCCEEE | 55.39 | 16335952 | |
1796 | Phosphorylation | VVLKRRGYLGETSFI HHHHHCCCCCCCEEE | 15.10 | - | |
1800 | Phosphorylation | RRGYLGETSFISIGT HCCCCCCCEEEEEEC | 27.43 | - | |
1804 | Phosphorylation | LGETSFISIGTRDRT CCCCEEEEEECCCCC | 16.98 | - | |
1947 | Phosphorylation | ISRPEDHTSVVRFDK CCCCCCCCCEEECCH | 35.22 | 22210691 | |
2035 | Phosphorylation | VQVWRTGTDLSKSSS EEEEECCCCCCCCCC | 32.90 | 21712546 | |
2044 | Phosphorylation | LSKSSSVTVRSRKTD CCCCCCEEEEECCCC | 16.49 | 21712546 | |
2047 | Phosphorylation | SSSVTVRSRKTDPPS CCCEEEEECCCCCCC | 33.52 | 21712546 | |
2050 | Phosphorylation | VTVRSRKTDPPSADA EEEEECCCCCCCCCC | 53.26 | - | |
2059 | Phosphorylation | PPSADAGTDYVGISR CCCCCCCCCCEEECC | 26.36 | - | |
2061 | Phosphorylation | SADAGTDYVGISRNL CCCCCCCCEEECCCC | 10.62 | - | |
2065 | Phosphorylation | GTDYVGISRNLDFAP CCCCEEECCCCCCCC | 14.80 | 22210691 | |
2119 | Phosphorylation | EPSKATVSINDSVSD CCCCCEEECCCCHHH | 16.00 | 28787133 | |
2125 | Phosphorylation | VSINDSVSDLPKMQF EECCCCHHHCCCCCE | 37.06 | 25954137 | |
2137 | Phosphorylation | MQFKERIYTGSESDG CCEEEEEECCCCCCC | 15.98 | - | |
2138 | Phosphorylation | QFKERIYTGSESDGQ CEEEEEECCCCCCCC | 31.68 | - | |
2140 | Phosphorylation | KERIYTGSESDGQIV EEEEECCCCCCCCEE | 26.57 | - | |
2158 | Phosphorylation | HRTGDVQYRSSVRCY EECCCCEEEEEEEEE | 16.59 | 22817900 | |
2160 | Phosphorylation | TGDVQYRSSVRCYTR CCCCEEEEEEEEEEC | 28.40 | 22985185 | |
2256 | Phosphorylation | TVIKFGETKFSVTEP EEEEECCCEEEECCC | 37.46 | 22210691 | |
2299 | Phosphorylation | TKDGSATSGEDYHPV ECCCCCCCCCCCCCC | 39.64 | 24505115 | |
2338 | Phosphorylation | REMREAFTVHLKPDE HHHHHEEEEEECCCC | 17.67 | 29978859 | |
2370 | Phosphorylation | MSSMADVTFPSVPQI HHCCCCCCCCCHHHH | 30.31 | 19413330 | |
2433 | Phosphorylation | INDTLTRYRWLISAP CCCHHHEEEEHHCCC | 10.82 | - | |
2581 | Phosphorylation | RVGNHKCSNLLDYTE EECCCCCCCCCCCCE | 35.00 | 30206219 | |
2586 | Phosphorylation | KCSNLLDYTEVKTHY CCCCCCCCCEEEEEE | 12.55 | 30206219 | |
2587 | Phosphorylation | CSNLLDYTEVKTHYG CCCCCCCCEEEEEEC | 33.69 | 30206219 | |
2591 | Phosphorylation | LDYTEVKTHYGFLTD CCCCEEEEEECCCCC | 26.04 | 30206219 | |
2593 | Phosphorylation | YTEVKTHYGFLTDAT CCEEEEEECCCCCCC | 18.14 | 30206219 | |
2597 | Phosphorylation | KTHYGFLTDATKNPE EEEECCCCCCCCCHH | 22.71 | 30206219 | |
2600 | Phosphorylation | YGFLTDATKNPEIIG ECCCCCCCCCHHHCC | 33.88 | 30206219 | |
2614 | Phosphorylation | GETYPYQYSLSIRGS CCCCCEEEEEEECCC | 13.02 | 25884760 | |
2615 | Phosphorylation | ETYPYQYSLSIRGST CCCCEEEEEEECCCC | 10.50 | 24719451 | |
2617 | Phosphorylation | YPYQYSLSIRGSTTL CCEEEEEEECCCCEE | 12.33 | 24719451 | |
2850 | Phosphorylation | DIRFQQVSDPVAAEF EEEEEECCCCCEEEE | 31.68 | 26074081 | |
2858 | Phosphorylation | DPVAAEFSLNTQMYL CCCEEEEECHHHHHH | 16.53 | 26074081 | |
2861 | Phosphorylation | AAEFSLNTQMYLLSK EEEEECHHHHHHEEC | 21.72 | 26074081 | |
2864 | Phosphorylation | FSLNTQMYLLSKKSL EECHHHHHHEECCEE | 8.48 | 26074081 | |
2867 | Phosphorylation | NTQMYLLSKKSLWLS HHHHHHEECCEEEEC | 35.13 | 26074081 | |
3058 | Phosphorylation | KKREIRSTPSLAWEI HHHHCCCCCCHHHHH | 13.67 | - |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
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Oops, there are no upstream regulatory protein records of FREM2_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of FREM2_HUMAN !! |
* 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 FREM2_HUMAN !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
Oops, there are no PPI records of FREM2_HUMAN !! |
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N-linked Glycosylation | |
Reference | PubMed |
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,hydrazide chemistry, and mass spectrometry."; Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,Moore R.J., Smith R.D.; J. Proteome Res. 4:2070-2080(2005). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1741, AND MASSSPECTROMETRY. |