UniProt ID | FINC_HUMAN | |
---|---|---|
UniProt AC | P02751 | |
Protein Name | Fibronectin | |
Gene Name | FN1 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 2386 | |
Subcellular Localization | Secreted, extracellular space, extracellular matrix. | |
Protein Description | Fibronectins bind cell surfaces and various compounds including collagen, fibrin, heparin, DNA, and actin. Fibronectins are involved in cell adhesion, cell motility, opsonization, wound healing, and maintenance of cell shape. Involved in osteoblast compaction through the fibronectin fibrillogenesis cell-mediated matrix assembly process, essential for osteoblast mineralization. Participates in the regulation of type I collagen deposition by osteoblasts.; Anastellin binds fibronectin and induces fibril formation. This fibronectin polymer, named superfibronectin, exhibits enhanced adhesive properties. Both anastellin and superfibronectin inhibit tumor growth, angiogenesis and metastasis. Anastellin activates p38 MAPK and inhibits lysophospholipid signaling.. | |
Protein Sequence | MLRGPGPGLLLLAVQCLGTAVPSTGASKSKRQAQQMVQPQSPVAVSQSKPGCYDNGKHYQINQQWERTYLGNALVCTCYGGSRGFNCESKPEAEETCFDKYTGNTYRVGDTYERPKDSMIWDCTCIGAGRGRISCTIANRCHEGGQSYKIGDTWRRPHETGGYMLECVCLGNGKGEWTCKPIAEKCFDHAAGTSYVVGETWEKPYQGWMMVDCTCLGEGSGRITCTSRNRCNDQDTRTSYRIGDTWSKKDNRGNLLQCICTGNGRGEWKCERHTSVQTTSSGSGPFTDVRAAVYQPQPHPQPPPYGHCVTDSGVVYSVGMQWLKTQGNKQMLCTCLGNGVSCQETAVTQTYGGNSNGEPCVLPFTYNGRTFYSCTTEGRQDGHLWCSTTSNYEQDQKYSFCTDHTVLVQTRGGNSNGALCHFPFLYNNHNYTDCTSEGRRDNMKWCGTTQNYDADQKFGFCPMAAHEEICTTNEGVMYRIGDQWDKQHDMGHMMRCTCVGNGRGEWTCIAYSQLRDQCIVDDITYNVNDTFHKRHEEGHMLNCTCFGQGRGRWKCDPVDQCQDSETGTFYQIGDSWEKYVHGVRYQCYCYGRGIGEWHCQPLQTYPSSSGPVEVFITETPSQPNSHPIQWNAPQPSHISKYILRWRPKNSVGRWKEATIPGHLNSYTIKGLKPGVVYEGQLISIQQYGHQEVTRFDFTTTSTSTPVTSNTVTGETTPFSPLVATSESVTEITASSFVVSWVSASDTVSGFRVEYELSEEGDEPQYLDLPSTATSVNIPDLLPGRKYIVNVYQISEDGEQSLILSTSQTTAPDAPPDTTVDQVDDTSIVVRWSRPQAPITGYRIVYSPSVEGSSTELNLPETANSVTLSDLQPGVQYNITIYAVEENQESTPVVIQQETTGTPRSDTVPSPRDLQFVEVTDVKVTIMWTPPESAVTGYRVDVIPVNLPGEHGQRLPISRNTFAEVTGLSPGVTYYFKVFAVSHGRESKPLTAQQTTKLDAPTNLQFVNETDSTVLVRWTPPRAQITGYRLTVGLTRRGQPRQYNVGPSVSKYPLRNLQPASEYTVSLVAIKGNQESPKATGVFTTLQPGSSIPPYNTEVTETTIVITWTPAPRIGFKLGVRPSQGGEAPREVTSDSGSIVVSGLTPGVEYVYTIQVLRDGQERDAPIVNKVVTPLSPPTNLHLEANPDTGVLTVSWERSTTPDITGYRITTTPTNGQQGNSLEEVVHADQSSCTFDNLSPGLEYNVSVYTVKDDKESVPISDTIIPAVPPPTDLRFTNIGPDTMRVTWAPPPSIDLTNFLVRYSPVKNEEDVAELSISPSDNAVVLTNLLPGTEYVVSVSSVYEQHESTPLRGRQKTGLDSPTGIDFSDITANSFTVHWIAPRATITGYRIRHHPEHFSGRPREDRVPHSRNSITLTNLTPGTEYVVSIVALNGREESPLLIGQQSTVSDVPRDLEVVAATPTSLLISWDAPAVTVRYYRITYGETGGNSPVQEFTVPGSKSTATISGLKPGVDYTITVYAVTGRGDSPASSKPISINYRTEIDKPSQMQVTDVQDNSISVKWLPSSSPVTGYRVTTTPKNGPGPTKTKTAGPDQTEMTIEGLQPTVEYVVSVYAQNPSGESQPLVQTAVTNIDRPKGLAFTDVDVDSIKIAWESPQGQVSRYRVTYSSPEDGIHELFPAPDGEEDTAELQGLRPGSEYTVSVVALHDDMESQPLIGTQSTAIPAPTDLKFTQVTPTSLSAQWTPPNVQLTGYRVRVTPKEKTGPMKEINLAPDSSSVVVSGLMVATKYEVSVYALKDTLTSRPAQGVVTTLENVSPPRRARVTDATETTITISWRTKTETITGFQVDAVPANGQTPIQRTIKPDVRSYTITGLQPGTDYKIYLYTLNDNARSSPVVIDASTAIDAPSNLRFLATTPNSLLVSWQPPRARITGYIIKYEKPGSPPREVVPRPRPGVTEATITGLEPGTEYTIYVIALKNNQKSEPLIGRKKTDELPQLVTLPHPNLHGPEILDVPSTVQKTPFVTHPGYDTGNGIQLPGTSGQQPSVGQQMIFEEHGFRRTTPPTTATPIRHRPRPYPPNVGEEIQIGHIPREDVDYHLYPHGPGLNPNASTGQEALSQTTISWAPFQDTSEYIISCHPVGTDEEPLQFRVPGTSTSATLTGLTRGATYNVIVEALKDQQRHKVREEVVTVGNSVNEGLNQPTDDSCFDPYTVSHYAVGDEWERMSESGFKLLCQCLGFGSGHFRCDSSRWCHDNGVNYKIGEKWDRQGENGQMMSCTCLGNGKGEFKCDPHEATCYDDGKTYHVGEQWQKEYLGAICSCTCFGGQRGWRCDNCRRPGGEPSPEGTTGQSYNQYSQRYHQRTNTNVNCPIECFMPLDVQADREDSRE | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
32 | Pyrrolidone_carboxylic_acid | GASKSKRQAQQMVQP CCCHHHHHHHHHCCC | 47.46 | - | |
32 | Pyrrolidone_carboxylic_acid | GASKSKRQAQQMVQP CCCHHHHHHHHHCCC | 47.46 | 6630202 | |
32 | Pyrrolidone_carboxylic_acid | GASKSKRQAQQMVQP CCCHHHHHHHHHCCC | 47.46 | 6630202 | |
41 | O-linked_Glycosylation | QQMVQPQSPVAVSQS HHHCCCCCCCEECCC | 28.20 | OGP | |
41 | Phosphorylation | QQMVQPQSPVAVSQS HHHCCCCCCCEECCC | 28.20 | 27251275 | |
46 | O-linked_Glycosylation | PQSPVAVSQSKPGCY CCCCCEECCCCCCCC | 20.99 | OGP | |
46 | Phosphorylation | PQSPVAVSQSKPGCY CCCCCEECCCCCCCC | 20.99 | 22210691 | |
90 | Malonylation | RGFNCESKPEAEETC CCCCCCCCCCCCHHC | 25.28 | 32601280 | |
100 | Acetylation | AEETCFDKYTGNTYR CCHHCCCCCCCCEEE | 25.18 | 25038526 | |
100 | Malonylation | AEETCFDKYTGNTYR CCHHCCCCCCCCEEE | 25.18 | 26320211 | |
101 | Phosphorylation | EETCFDKYTGNTYRV CHHCCCCCCCCEEEE | 23.02 | - | |
106 | Phosphorylation | DKYTGNTYRVGDTYE CCCCCCEEEECCCCC | 13.80 | - | |
112 | Phosphorylation | TYRVGDTYERPKDSM EEEECCCCCCCCCCE | 18.06 | 23911959 | |
118 | Phosphorylation | TYERPKDSMIWDCTC CCCCCCCCEEEEEEE | 20.49 | 24719451 | |
136 | Phosphorylation | GRGRISCTIANRCHE CCCEEEEEEECCCCC | 19.14 | 24719451 | |
226 | Phosphorylation | GSGRITCTSRNRCND CCCEEEECCCCCCCC | 23.28 | 24719451 | |
245 | Phosphorylation | TSYRIGDTWSKKDNR CEEECCCCCCCCCCC | 26.82 | 23403867 | |
247 | Phosphorylation | YRIGDTWSKKDNRGN EECCCCCCCCCCCCC | 31.74 | 23403867 | |
274 | Phosphorylation | EWKCERHTSVQTTSS EEEEEEECCEEEECC | 36.49 | 23312004 | |
275 | Phosphorylation | WKCERHTSVQTTSSG EEEEEECCEEEECCC | 13.20 | 23312004 | |
278 | O-linked_Glycosylation | ERHTSVQTTSSGSGP EEECCEEEECCCCCC | 26.87 | OGP | |
278 | Phosphorylation | ERHTSVQTTSSGSGP EEECCEEEECCCCCC | 26.87 | 24505115 | |
279 | O-linked_Glycosylation | RHTSVQTTSSGSGPF EECCEEEECCCCCCC | 12.10 | 55828963 | |
279 | Phosphorylation | RHTSVQTTSSGSGPF EECCEEEECCCCCCC | 12.10 | 24505115 | |
280 | O-linked_Glycosylation | HTSVQTTSSGSGPFT ECCEEEECCCCCCCC | 35.77 | OGP | |
280 | Phosphorylation | HTSVQTTSSGSGPFT ECCEEEECCCCCCCC | 35.77 | 30576742 | |
281 | O-linked_Glycosylation | TSVQTTSSGSGPFTD CCEEEECCCCCCCCC | 34.58 | OGP | |
281 | Phosphorylation | TSVQTTSSGSGPFTD CCEEEECCCCCCCCC | 34.58 | 24505115 | |
283 | O-linked_Glycosylation | VQTTSSGSGPFTDVR EEEECCCCCCCCCEE | 45.28 | OGP | |
283 | Phosphorylation | VQTTSSGSGPFTDVR EEEECCCCCCCCCEE | 45.28 | 24505115 | |
287 | O-linked_Glycosylation | SSGSGPFTDVRAAVY CCCCCCCCCEEEEEE | 36.40 | OGP | |
372 | Phosphorylation | TYNGRTFYSCTTEGR EECCEEEEEEECCCC | 11.39 | - | |
389 | O-linked_Glycosylation | GHLWCSTTSNYEQDQ CEEEEECCCCCCCCC | 9.93 | OGP | |
402 | O-linked_Glycosylation | DQKYSFCTDHTVLVQ CCCEEEECCCEEEEE | 28.89 | OGP | |
410 | O-linked_Glycosylation | DHTVLVQTRGGNSNG CCEEEEEECCCCCCC | 24.65 | OGP | |
430 | N-linked_Glycosylation | PFLYNNHNYTDCTSE EEEECCCCCCCCCCC | 43.45 | 11285216 | |
443 | Sulfoxidation | SEGRRDNMKWCGTTQ CCCCCCCCCCCCCCC | 4.12 | 8347617 | |
448 | O-linked_Glycosylation | DNMKWCGTTQNYDAD CCCCCCCCCCCCCCC | 23.28 | OGP | |
449 | O-linked_Glycosylation | NMKWCGTTQNYDADQ CCCCCCCCCCCCCCC | 10.49 | OGP | |
463 | Sulfoxidation | QKFGFCPMAAHEEIC CCCCCCCCCCCCHHE | 5.60 | 8347617 | |
477 | Sulfoxidation | CTTNEGVMYRIGDQW EECCCCEEEEECCCC | 2.47 | 8347617 | |
486 | Methylation | RIGDQWDKQHDMGHM EECCCCHHHCCCCEE | 46.72 | - | |
528 | N-linked_Glycosylation | DDITYNVNDTFHKRH EEEEEECCCHHHHHC | 38.68 | 18638581 | |
528 | N-linked_Glycosylation | DDITYNVNDTFHKRH EEEEEECCCHHHHHC | 38.68 | 17623646 | |
542 | N-linked_Glycosylation | HEEGHMLNCTCFGQG CCCCCEEEEEEECCC | 16.10 | 18638581 | |
542 | N-linked_Glycosylation | HEEGHMLNCTCFGQG CCCCCEEEEEEECCC | 16.10 | 16335952 | |
588 | Phosphorylation | HGVRYQCYCYGRGIG CCEEEEEEEECCCCC | 3.53 | - | |
617 | O-linked_Glycosylation | GPVEVFITETPSQPN CCEEEEEECCCCCCC | 23.49 | OGP | |
641 | Phosphorylation | QPSHISKYILRWRPK CCCCCHHHHHHCCCC | 9.82 | - | |
658 | O-linked_Glycosylation | VGRWKEATIPGHLNS CCCCEECCCCCCCCE | 28.88 | OGP | |
667 | O-linked_Glycosylation | PGHLNSYTIKGLKPG CCCCCEEEECCCCCC | 18.94 | OGP | |
677 | Phosphorylation | GLKPGVVYEGQLISI CCCCCEEEEEEEEEE | 16.37 | 24043423 | |
683 | Phosphorylation | VYEGQLISIQQYGHQ EEEEEEEEEEEECCC | 23.96 | 24043423 | |
687 | Phosphorylation | QLISIQQYGHQEVTR EEEEEEEECCCEEEE | 10.53 | 24043423 | |
693 | Phosphorylation | QYGHQEVTRFDFTTT EECCCEEEEEEEEEC | 25.51 | 24043423 | |
715 | Phosphorylation | SNTVTGETTPFSPLV ECCCCCCCCCCCCCC | 40.91 | 24275569 | |
771 | O-linked_Glycosylation | QYLDLPSTATSVNIP CEECCCCCCCCCCCC | 31.82 | OGP | |
818 | O-linked_Glycosylation | PDAPPDTTVDQVDDT CCCCCCCCCCCCCCC | 29.48 | OGP | |
876 | Sulfation | DLQPGVQYNITIYAV HCCCCCEEEEEEEEE | 13.21 | - | |
876 | Sulfation | DLQPGVQYNITIYAV HCCCCCEEEEEEEEE | 13.21 | - | |
877 | N-linked_Glycosylation | LQPGVQYNITIYAVE CCCCCEEEEEEEEEE | 14.08 | 17614963 | |
881 | Sulfation | VQYNITIYAVEENQE CEEEEEEEEEECCCC | 8.92 | - | |
881 | Sulfation | VQYNITIYAVEENQE CEEEEEEEEEECCCC | 8.92 | - | |
904 | Phosphorylation | ETTGTPRSDTVPSPR ECCCCCCCCCCCCCC | 38.55 | 17192257 | |
909 | Phosphorylation | PRSDTVPSPRDLQFV CCCCCCCCCCCCEEE | 28.38 | 17322306 | |
926 | Sulfoxidation | TDVKVTIMWTPPESA EEEEEEEEECCCHHH | 2.08 | 27541571 | |
935 | O-linked_Glycosylation | TPPESAVTGYRVDVI CCCHHHCCCEEEEEE | 28.36 | OGP | |
937 | Phosphorylation | PESAVTGYRVDVIPV CHHHCCCEEEEEEEC | 9.71 | - | |
960 | Phosphorylation | RLPISRNTFAEVTGL CCCCCCCCCCHHHCC | 24.10 | - | |
968 | Phosphorylation | FAEVTGLSPGVTYYF CCHHHCCCCCCEEEE | 22.43 | - | |
972 | Phosphorylation | TGLSPGVTYYFKVFA HCCCCCCEEEEEEEE | 20.58 | - | |
974 | Nitration | LSPGVTYYFKVFAVS CCCCCEEEEEEEEEC | 6.38 | - | |
986 | Phosphorylation | AVSHGRESKPLTAQQ EECCCCCCCCCCCCC | 37.91 | 24719451 | |
987 | Acetylation | VSHGRESKPLTAQQT ECCCCCCCCCCCCCC | 39.01 | 30586037 | |
1007 | N-linked_Glycosylation | PTNLQFVNETDSTVL CCCEEEECCCCCEEE | 47.98 | 18638581 | |
1007 | N-linked_Glycosylation | PTNLQFVNETDSTVL CCCEEEECCCCCEEE | 47.98 | 17623646 | |
1034 | Phosphorylation | YRLTVGLTRRGQPRQ EEEEEEECCCCCCCC | 16.64 | 24961811 | |
1042 | Phosphorylation | RRGQPRQYNVGPSVS CCCCCCCEECCCCCC | 17.07 | 21406692 | |
1047 | Phosphorylation | RQYNVGPSVSKYPLR CCEECCCCCCCCCCC | 32.85 | 21406692 | |
1050 | Ubiquitination | NVGPSVSKYPLRNLQ ECCCCCCCCCCCCCC | 49.05 | 21890473 | |
1050 | Ubiquitination | NVGPSVSKYPLRNLQ ECCCCCCCCCCCCCC | 49.05 | 2189047 | |
1050 (in isoform 1) | Ubiquitination | - | 49.05 | 21890473 | |
1050 (in isoform 10) | Ubiquitination | - | 49.05 | 21890473 | |
1050 (in isoform 11) | Ubiquitination | - | 49.05 | 21890473 | |
1050 (in isoform 12) | Ubiquitination | - | 49.05 | 21890473 | |
1050 (in isoform 13) | Ubiquitination | - | 49.05 | 21890473 | |
1050 (in isoform 14) | Ubiquitination | - | 49.05 | 21890473 | |
1050 (in isoform 15) | Ubiquitination | - | 49.05 | 21890473 | |
1050 (in isoform 3) | Ubiquitination | - | 49.05 | 21890473 | |
1050 (in isoform 4) | Ubiquitination | - | 49.05 | 21890473 | |
1050 (in isoform 5) | Ubiquitination | - | 49.05 | 21890473 | |
1050 (in isoform 6) | Ubiquitination | - | 49.05 | 21890473 | |
1050 (in isoform 7) | Ubiquitination | - | 49.05 | 21890473 | |
1050 (in isoform 8) | Ubiquitination | - | 49.05 | 21890473 | |
1050 (in isoform 9) | Ubiquitination | - | 49.05 | 21890473 | |
1122 | O-linked_Glycosylation | FKLGVRPSQGGEAPR EEEECCCCCCCCCCC | 30.78 | OGP | |
1132 | Phosphorylation | GEAPREVTSDSGSIV CCCCCEEECCCCCEE | 23.28 | 26074081 | |
1133 | Phosphorylation | EAPREVTSDSGSIVV CCCCEEECCCCCEEE | 34.65 | 26074081 | |
1135 | Phosphorylation | PREVTSDSGSIVVSG CCEEECCCCCEEEEC | 33.92 | 26074081 | |
1137 | Phosphorylation | EVTSDSGSIVVSGLT EEECCCCCEEEECCC | 19.03 | 26074081 | |
1141 | Phosphorylation | DSGSIVVSGLTPGVE CCCCEEEECCCCCEE | 19.72 | 26074081 | |
1144 | Phosphorylation | SIVVSGLTPGVEYVY CEEEECCCCCEEEEE | 22.86 | 26074081 | |
1149 | Phosphorylation | GLTPGVEYVYTIQVL CCCCCEEEEEEEEEE | 9.06 | 26074081 | |
1151 | Phosphorylation | TPGVEYVYTIQVLRD CCCEEEEEEEEEECC | 9.38 | 26074081 | |
1152 | Phosphorylation | PGVEYVYTIQVLRDG CCEEEEEEEEEECCC | 8.55 | 26074081 | |
1198 | O-linked_Glycosylation | LTVSWERSTTPDITG EEEEEEECCCCCCCC | 25.72 | OGP | |
1199 | O-linked_Glycosylation | TVSWERSTTPDITGY EEEEEECCCCCCCCE | 48.87 | OGP | |
1200 | O-linked_Glycosylation | VSWERSTTPDITGYR EEEEECCCCCCCCEE | 21.88 | OGP | |
1200 | Phosphorylation | VSWERSTTPDITGYR EEEEECCCCCCCCEE | 21.88 | 25690035 | |
1204 | O-linked_Glycosylation | RSTTPDITGYRITTT ECCCCCCCCEEEEEC | 35.22 | OGP | |
1204 | Phosphorylation | RSTTPDITGYRITTT ECCCCCCCCEEEEEC | 35.22 | 25690035 | |
1206 | Phosphorylation | TTPDITGYRITTTPT CCCCCCCEEEEECCC | 7.09 | - | |
1244 | N-linked_Glycosylation | LSPGLEYNVSVYTVK CCCCCEEEEEEEEEC | 15.37 | 16335952 | |
1271 | Phosphorylation | IPAVPPPTDLRFTNI EECCCCCCCCCCCCC | 54.14 | - | |
1276 | O-linked_Glycosylation | PPTDLRFTNIGPDTM CCCCCCCCCCCCCCE | 21.35 | OGP | |
1276 | Phosphorylation | PPTDLRFTNIGPDTM CCCCCCCCCCCCCCE | 21.35 | 24114839 | |
1282 | O-linked_Glycosylation | FTNIGPDTMRVTWAP CCCCCCCCEEEEECC | 15.26 | OGP | |
1282 | Phosphorylation | FTNIGPDTMRVTWAP CCCCCCCCEEEEECC | 15.26 | 24114839 | |
1347 | Phosphorylation | SVYEQHESTPLRGRQ HHHCCCCCCCCCCCC | 32.95 | 24719451 | |
1373 (in isoform 12) | Phosphorylation | - | 21.60 | 27251275 | |
1376 (in isoform 12) | Phosphorylation | - | 3.12 | 27251275 | |
1379 (in isoform 12) | Phosphorylation | - | 1.98 | 27251275 | |
1381 (in isoform 12) | Phosphorylation | - | 19.80 | 27251275 | |
1386 (in isoform 12) | Phosphorylation | - | 24.65 | 27251275 | |
1389 (in isoform 12) | Phosphorylation | - | 22.32 | 27251275 | |
1395 (in isoform 12) | Phosphorylation | - | 53.89 | 27251275 | |
1481 | O-linked_Glycosylation | TVRYYRITYGETGGN EEEEEEEEECCCCCC | 19.24 | OGP | |
1530 | O-linked_Glycosylation | GRGDSPASSKPISIN CCCCCCCCCCCEEEE | 42.13 | OGP | |
1531 | O-linked_Glycosylation | RGDSPASSKPISINY CCCCCCCCCCEEEEE | 44.55 | OGP | |
1535 | O-linked_Glycosylation | PASSKPISINYRTEI CCCCCCEEEEEECCC | 17.20 | OGP | |
1546 | O-linked_Glycosylation | RTEIDKPSQMQVTDV ECCCCCCCCCEEEEC | 43.98 | OGP | |
1551 | O-linked_Glycosylation | KPSQMQVTDVQDNSI CCCCCEEEECCCCEE | 17.35 | OGP | |
1557 | O-linked_Glycosylation | VTDVQDNSISVKWLP EEECCCCEEEEEECC | 25.24 | OGP | |
1557 | Phosphorylation | VTDVQDNSISVKWLP EEECCCCEEEEEECC | 25.24 | 24719451 | |
1565 | O-linked_Glycosylation | ISVKWLPSSSPVTGY EEEEECCCCCCCCCE | 41.08 | OGP | |
1566 | O-linked_Glycosylation | SVKWLPSSSPVTGYR EEEECCCCCCCCCEE | 36.40 | OGP | |
1567 | O-linked_Glycosylation | VKWLPSSSPVTGYRV EEECCCCCCCCCEEE | 27.94 | OGP | |
1570 | O-linked_Glycosylation | LPSSSPVTGYRVTTT CCCCCCCCCEEEEEC | 31.70 | OGP | |
1605 | O-linked_Glycosylation | TIEGLQPTVEYVVSV EEECCCCEEEEEEEE | 17.01 | OGP | |
1605 (in isoform 10) | Phosphorylation | - | 17.01 | 27251275 | |
1605 (in isoform 14) | Phosphorylation | - | 17.01 | 27251275 | |
1605 (in isoform 8) | Phosphorylation | - | 17.01 | 27251275 | |
1605 (in isoform 9) | Phosphorylation | - | 17.01 | 27251275 | |
1608 (in isoform 10) | Phosphorylation | - | 11.21 | 27251275 | |
1608 (in isoform 14) | Phosphorylation | - | 11.21 | 27251275 | |
1608 (in isoform 8) | Phosphorylation | - | 11.21 | 27251275 | |
1608 (in isoform 9) | Phosphorylation | - | 11.21 | 27251275 | |
1611 | O-linked_Glycosylation | PTVEYVVSVYAQNPS CEEEEEEEEEEECCC | 10.20 | OGP | |
1611 | Phosphorylation | PTVEYVVSVYAQNPS CEEEEEEEEEEECCC | 10.20 | 27251275 | |
1611 (in isoform 10) | Phosphorylation | - | 10.20 | 27251275 | |
1611 (in isoform 14) | Phosphorylation | - | 10.20 | 27251275 | |
1611 (in isoform 8) | Phosphorylation | - | 10.20 | 27251275 | |
1611 (in isoform 9) | Phosphorylation | - | 10.20 | 27251275 | |
1613 (in isoform 10) | Phosphorylation | - | 8.58 | 27251275 | |
1613 (in isoform 14) | Phosphorylation | - | 8.58 | 27251275 | |
1613 (in isoform 8) | Phosphorylation | - | 8.58 | 27251275 | |
1613 (in isoform 9) | Phosphorylation | - | 8.58 | 27251275 | |
1618 (in isoform 10) | Phosphorylation | - | 63.84 | 27251275 | |
1618 (in isoform 14) | Phosphorylation | - | 63.84 | 27251275 | |
1618 (in isoform 8) | Phosphorylation | - | 63.84 | 27251275 | |
1618 (in isoform 9) | Phosphorylation | - | 63.84 | 27251275 | |
1621 (in isoform 10) | Phosphorylation | - | 40.39 | 27251275 | |
1621 (in isoform 14) | Phosphorylation | - | 40.39 | 27251275 | |
1621 (in isoform 8) | Phosphorylation | - | 40.39 | 27251275 | |
1621 (in isoform 9) | Phosphorylation | - | 40.39 | 27251275 | |
1627 | O-linked_Glycosylation | ESQPLVQTAVTNIDR CCCCCEEEEECCCCC | 18.67 | OGP | |
1627 (in isoform 10) | Phosphorylation | - | 18.67 | 27251275 | |
1627 (in isoform 14) | Phosphorylation | - | 18.67 | 27251275 | |
1627 (in isoform 8) | Phosphorylation | - | 18.67 | 27251275 | |
1627 (in isoform 9) | Phosphorylation | - | 18.67 | 27251275 | |
1641 | O-linked_Glycosylation | RPKGLAFTDVDVDSI CCCCCCEEEECCCEE | 29.52 | OGP | |
1654 | O-linked_Glycosylation | SIKIAWESPQGQVSR EEEEEEECCCCCEEE | 16.30 | OGP | |
1660 | O-linked_Glycosylation | ESPQGQVSRYRVTYS ECCCCCEEEEEEEEC | 18.73 | OGP | |
1696 | Phosphorylation | LQGLRPGSEYTVSVV HCCCCCCCEEEEEEE | 30.07 | 24043423 | |
1696 (in isoform 13) | Phosphorylation | - | 30.07 | 27251275 | |
1698 | Phosphorylation | GLRPGSEYTVSVVAL CCCCCCEEEEEEEEE | 17.71 | 24043423 | |
1699 | Phosphorylation | LRPGSEYTVSVVALH CCCCCEEEEEEEEEE | 11.40 | 24043423 | |
1699 (in isoform 13) | Phosphorylation | - | 11.40 | 27251275 | |
1701 | Phosphorylation | PGSEYTVSVVALHDD CCCEEEEEEEEEECC | 11.77 | 24043423 | |
1702 (in isoform 13) | Phosphorylation | - | 2.25 | 27251275 | |
1704 (in isoform 13) | Phosphorylation | - | 9.31 | 27251275 | |
1709 (in isoform 13) | Phosphorylation | - | 7.13 | 27251275 | |
1711 | Phosphorylation | ALHDDMESQPLIGTQ EEECCCCCCCCEECC | 30.38 | 24043423 | |
1712 (in isoform 13) | Phosphorylation | - | 24.42 | 27251275 | |
1717 | O-linked_Glycosylation | ESQPLIGTQSTAIPA CCCCCEECCCCCCCC | 16.62 | OGP | |
1717 | Phosphorylation | ESQPLIGTQSTAIPA CCCCCEECCCCCCCC | 16.62 | 24043423 | |
1718 (in isoform 13) | Phosphorylation | - | 33.30 | 27251275 | |
1719 | Phosphorylation | QPLIGTQSTAIPAPT CCCEECCCCCCCCCC | 21.46 | 24043423 | |
1720 | Phosphorylation | PLIGTQSTAIPAPTD CCEECCCCCCCCCCC | 20.84 | 24043423 | |
1720 (in isoform 12) | Phosphorylation | - | 20.84 | 29116813 | |
1726 | Phosphorylation | STAIPAPTDLKFTQV CCCCCCCCCCEEEEE | 56.95 | 24043423 | |
1743 | O-linked_Glycosylation | TSLSAQWTPPNVQLT CCCCCCCCCCCEEEC | 19.45 | OGP | |
1743 | Phosphorylation | TSLSAQWTPPNVQLT CCCCCCCCCCCEEEC | 19.45 | - | |
1762 | Phosphorylation | RVTPKEKTGPMKEIN EECCCCCCCCCCEEE | 47.84 | - | |
1783 | Sulfoxidation | SVVVSGLMVATKYEV CEEEECEEEEEEEEE | 1.89 | 27541571 | |
1786 | Phosphorylation | VSGLMVATKYEVSVY EECEEEEEEEEEEEE | 23.81 | 30278072 | |
1791 | O-linked_Glycosylation | VATKYEVSVYALKDT EEEEEEEEEEEEEHH | 9.47 | OGP | |
1823 | O-linked_Glycosylation | PPRRARVTDATETTI CCCCCEECCCCCEEE | 17.86 | OGP | |
1826 | O-linked_Glycosylation | RARVTDATETTITIS CCEECCCCCEEEEEE | 36.35 | OGP | |
1828 | O-linked_Glycosylation | RVTDATETTITISWR EECCCCCEEEEEEEE | 21.10 | OGP | |
1829 | O-linked_Glycosylation | VTDATETTITISWRT ECCCCCEEEEEEEEC | 15.19 | OGP | |
1831 | O-linked_Glycosylation | DATETTITISWRTKT CCCCEEEEEEEECCC | 13.58 | OGP | |
1833 | O-linked_Glycosylation | TETTITISWRTKTET CCEEEEEEEECCCEE | 11.23 | OGP | |
1833 | Phosphorylation | TETTITISWRTKTET CCEEEEEEEECCCEE | 11.23 | 24719451 | |
1837 | Ubiquitination | ITISWRTKTETITGF EEEEEECCCEEECEE | 35.47 | - | |
1840 | Phosphorylation | SWRTKTETITGFQVD EEECCCEEECEEEEE | 29.13 | - | |
1842 | Phosphorylation | RTKTETITGFQVDAV ECCCEEECEEEEEEC | 39.09 | 22210691 | |
1855 | Phosphorylation | AVPANGQTPIQRTIK ECCCCCCCCCEEECC | 24.61 | 22210691 | |
1860 | Phosphorylation | GQTPIQRTIKPDVRS CCCCCEEECCCCCCE | 19.58 | 22210691 | |
1877 | O-linked_Glycosylation | ITGLQPGTDYKIYLY EEECCCCCEEEEEEE | 42.72 | OGP | |
1879 | Phosphorylation | GLQPGTDYKIYLYTL ECCCCCEEEEEEEEC | 10.10 | - | |
1880 | Acetylation | LQPGTDYKIYLYTLN CCCCCEEEEEEEECC | 27.90 | 15605883 | |
1884 | Phosphorylation | TDYKIYLYTLNDNAR CEEEEEEEECCCCCC | 7.69 | - | |
1885 | O-linked_Glycosylation | DYKIYLYTLNDNARS EEEEEEEECCCCCCC | 19.25 | OGP | |
1914 | O-linked_Glycosylation | SNLRFLATTPNSLLV CCEEEEEECCCCEEE | 44.95 | OGP | |
1914 | Phosphorylation | SNLRFLATTPNSLLV CCEEEEEECCCCEEE | 44.95 | 23532336 | |
1915 | O-linked_Glycosylation | NLRFLATTPNSLLVS CEEEEEECCCCEEEE | 18.18 | OGP | |
1922 | O-linked_Glycosylation | TPNSLLVSWQPPRAR CCCCEEEECCCCCCE | 21.69 | OGP | |
1922 | Phosphorylation | TPNSLLVSWQPPRAR CCCCEEEECCCCCCE | 21.69 | 23532336 | |
1931 | O-linked_Glycosylation | QPPRARITGYIIKYE CCCCCEEEEEEEEEC | 20.55 | OGP | |
1936 | Malonylation | RITGYIIKYEKPGSP EEEEEEEEECCCCCC | 37.49 | 26320211 | |
1952 (in isoform 9) | Phosphorylation | - | 41.71 | 29116813 | |
1977 (in isoform 14) | Phosphorylation | - | 44.84 | 29116813 | |
1981 | Malonylation | IALKNNQKSEPLIGR EEEECCCCCCCCCCC | 59.93 | 26320211 | |
1982 | Phosphorylation | ALKNNQKSEPLIGRK EEECCCCCCCCCCCC | 34.38 | 23911959 | |
1999 | O-linked_Glycosylation | DELPQLVTLPHPNLH CCCCCCCCCCCCCCC | 43.07 | OGP | |
2015 | Phosphorylation | PEILDVPSTVQKTPF CCCCCCCCCCCCCCC | 40.85 | 28270605 | |
2016 | Phosphorylation | EILDVPSTVQKTPFV CCCCCCCCCCCCCCC | 22.38 | 28270605 | |
2020 | O-linked_Glycosylation | VPSTVQKTPFVTHPG CCCCCCCCCCCCCCC | 12.60 | OGP | |
2024 | O-linked_Glycosylation | VQKTPFVTHPGYDTG CCCCCCCCCCCCCCC | 23.80 | OGP | |
2039 | O-linked_Glycosylation | NGIQLPGTSGQQPSV CCEECCCCCCCCCCC | 27.95 | OGP | |
2040 | O-linked_Glycosylation | GIQLPGTSGQQPSVG CEECCCCCCCCCCCC | 40.28 | OGP | |
2042 (in isoform 17) | Phosphorylation | - | 52.35 | 29116813 | |
2045 | O-linked_Glycosylation | GTSGQQPSVGQQMIF CCCCCCCCCCCEEEE | 34.24 | OGP | |
2050 | Sulfoxidation | QPSVGQQMIFEEHGF CCCCCCEEEEECCCC | 2.66 | 27541571 | |
2060 | O-linked_Glycosylation | EEHGFRRTTPPTTAT ECCCCCCCCCCCCCC | 39.12 | OGP | |
2061 | O-linked_Glycosylation | EHGFRRTTPPTTATP CCCCCCCCCCCCCCC | 26.01 | OGP | |
2064 | O-linked_Glycosylation | FRRTTPPTTATPIRH CCCCCCCCCCCCCCC | 30.21 | 55826769 | |
2064 | Phosphorylation | FRRTTPPTTATPIRH CCCCCCCCCCCCCCC | 30.21 | 22210691 | |
2065 | O-linked_Glycosylation | RRTTPPTTATPIRHR CCCCCCCCCCCCCCC | 34.02 | 55826775 | |
2065 | Phosphorylation | RRTTPPTTATPIRHR CCCCCCCCCCCCCCC | 34.02 | 29116813 | |
2067 | O-linked_Glycosylation | TTPPTTATPIRHRPR CCCCCCCCCCCCCCC | 19.70 | OGP | |
2067 | Phosphorylation | TTPPTTATPIRHRPR CCCCCCCCCCCCCCC | 19.70 | 22210691 | |
2067 (in isoform 3) | Phosphorylation | - | 19.70 | 29116813 | |
2073 (in isoform 5) | Phosphorylation | - | 35.16 | 24275569 | |
2108 | N-linked_Glycosylation | HGPGLNPNASTGQEA CCCCCCCCCCCCHHH | 45.51 | 16037490 | |
2119 | O-linked_Glycosylation | GQEALSQTTISWAPF CHHHHHCCEEEECCC | 23.79 | OGP | |
2130 | O-linked_Glycosylation | WAPFQDTSEYIISCH ECCCCCCCCEEEEEE | 36.37 | OGP | |
2153 | O-linked_Glycosylation | LQFRVPGTSTSATLT CEEECCCCCCCEECC | 23.82 | OGP | |
2154 | Phosphorylation | QFRVPGTSTSATLTG EEECCCCCCCEECCC | 26.70 | 30087585 | |
2155 | O-linked_Glycosylation | FRVPGTSTSATLTGL EECCCCCCCEECCCC | 23.40 | OGP | |
2155 | Phosphorylation | FRVPGTSTSATLTGL EECCCCCCCEECCCC | 23.40 | 30087585 | |
2158 | O-linked_Glycosylation | PGTSTSATLTGLTRG CCCCCCEECCCCCCC | 25.31 | OGP | |
2158 (in isoform 7) | Phosphorylation | - | 25.31 | 29116813 | |
2160 | O-linked_Glycosylation | TSTSATLTGLTRGAT CCCCEECCCCCCCCC | 26.28 | OGP | |
2163 | O-linked_Glycosylation | SATLTGLTRGATYNV CEECCCCCCCCCHHH | 28.53 | OGP | |
2199 | N-linked_Glycosylation | NSVNEGLNQPTDDSC CHHCCCCCCCCCCCC | 57.55 | 16037490 | |
2202 | O-linked_Glycosylation | NEGLNQPTDDSCFDP CCCCCCCCCCCCCCC | 42.55 | OGP | |
2211 | O-linked_Glycosylation | DSCFDPYTVSHYAVG CCCCCCCCCCEEECC | 22.41 | OGP | |
2258 | Phosphorylation | CHDNGVNYKIGEKWD ECCCCCCEEECCCCC | 11.11 | - | |
2275 | Phosphorylation | GENGQMMSCTCLGNG CCCCCEEEEEEECCC | 10.84 | 24505115 | |
2294 | O-linked_Glycosylation | KCDPHEATCYDDGKT EECCCCCEEECCCCE | 14.49 | OGP | |
2294 | Phosphorylation | KCDPHEATCYDDGKT EECCCCCEEECCCCE | 14.49 | 29083192 | |
2312 | Phosphorylation | GEQWQKEYLGAICSC CHHHHHHHHCHHEEC | 19.92 | - | |
2318 | Phosphorylation | EYLGAICSCTCFGGQ HHHCHHEECEECCCC | 13.32 | 19824718 | |
2341 | O-linked_Glycosylation | RRPGGEPSPEGTTGQ CCCCCCCCCCCCCCC | 31.14 | OGP | |
2341 | Phosphorylation | RRPGGEPSPEGTTGQ CCCCCCCCCCCCCCC | 31.14 | 24505115 | |
2345 | O-linked_Glycosylation | GEPSPEGTTGQSYNQ CCCCCCCCCCCCHHH | 26.54 | OGP | |
2345 | Phosphorylation | GEPSPEGTTGQSYNQ CCCCCCCCCCCCHHH | 26.54 | 28270605 | |
2346 | O-linked_Glycosylation | EPSPEGTTGQSYNQY CCCCCCCCCCCHHHH | 44.04 | OGP | |
2346 | Phosphorylation | EPSPEGTTGQSYNQY CCCCCCCCCCCHHHH | 44.04 | 28270605 | |
2349 | O-linked_Glycosylation | PEGTTGQSYNQYSQR CCCCCCCCHHHHHHH | 27.65 | OGP | |
2349 | Phosphorylation | PEGTTGQSYNQYSQR CCCCCCCCHHHHHHH | 27.65 | 19824718 | |
2350 | Phosphorylation | EGTTGQSYNQYSQRY CCCCCCCHHHHHHHH | 9.82 | 28270605 | |
2353 | Phosphorylation | TGQSYNQYSQRYHQR CCCCHHHHHHHHHHH | 11.79 | 28270605 | |
2354 | O-linked_Glycosylation | GQSYNQYSQRYHQRT CCCHHHHHHHHHHHC | 9.83 | OGP | |
2354 | Phosphorylation | GQSYNQYSQRYHQRT CCCHHHHHHHHHHHC | 9.83 | 28857561 | |
2361 | Phosphorylation | SQRYHQRTNTNVNCP HHHHHHHCCCCCCCC | 39.56 | 28060719 | |
2363 | Phosphorylation | RYHQRTNTNVNCPIE HHHHHCCCCCCCCEE | 39.67 | 28060719 | |
2384 | Phosphorylation | VQADREDSRE----- CCCCCHHHCC----- | 33.29 | 26846344 | |
2432 | Phosphorylation | ----------------------------------------------------- ----------------------------------------------------- | 24719451 | ||
2440 | Phosphorylation | ------------------------------------------------------------- ------------------------------------------------------------- | 24719451 | ||
2445 | Phosphorylation | ------------------------------------------------------------------ ------------------------------------------------------------------ | 24719451 | ||
2454 | Phosphorylation | --------------------------------------------------------------------------- --------------------------------------------------------------------------- | 24275569 | ||
2475 | Phosphorylation | ------------------------------------------------------------------------------------------------ ------------------------------------------------------------------------------------------------ | 20166139 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
2475 | S | Phosphorylation | Kinase | FAM20C | Q8IXL6 | Uniprot |
- | K | Ubiquitination | E3 ubiquitin ligase | BTRC | Q9Y297 | PMID:24658274 |
- | K | Ubiquitination | E3 ubiquitin ligase | VHL | P40337 | PMID:11024059 |
* 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 FINC_HUMAN !! |
Kegg Disease | ||||||
---|---|---|---|---|---|---|
There are no disease associations of PTM sites. | ||||||
OMIM Disease | ||||||
601894 | Glomerulopathy with fibronectin deposits 2 (GFND2) | |||||
Kegg Drug | ||||||
There are no disease associations of PTM sites. | ||||||
DrugBank | ||||||
There are no disease associations of PTM sites. |
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N-linked Glycosylation | |
Reference | PubMed |
"The hairpin structure of the (6)F1(1)F2(2)F2 fragment from humanfibronectin enhances gelatin binding."; Pickford A.R., Smith S.P., Staunton D., Boyd J., Campbell I.D.; EMBO J. 20:1519-1529(2001). Cited for: STRUCTURE BY NMR OF 305-464, AND GLYCOSYLATION AT ASN-430. | |
"Glycoproteomics analysis of human liver tissue by combination ofmultiple enzyme digestion and hydrazide chemistry."; Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.; J. Proteome Res. 8:651-661(2009). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-528 AND ASN-1007, AND MASSSPECTROMETRY. | |
"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-430; ASN-528; ASN-542;ASN-1007 AND ASN-1244, AND MASS SPECTROMETRY. | |
"Screening for N-glycosylated proteins by liquid chromatography massspectrometry."; Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R.; Proteomics 4:454-465(2004). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-528, AND MASSSPECTROMETRY. | |
"Identification of novel fibronectin fragments detected specificallyin juvenile urine."; Iida R., Yasuda T., Kishi K.; FEBS J. 274:3939-3947(2007). Cited for: PROTEIN SEQUENCE OF 723-911, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,GLYCOSYLATION AT ASN-877, AND VARIANT PRO-817. | |
O-linked Glycosylation | |
Reference | PubMed |
"Human plasma fibronectin. Demonstration of structural differencesbetween the A- and B-chains in the III CS region."; Tressel T., McCarthy J.B., Calaycay J., Lee T.D., Legesse K.,Shively J.E., Pande H.; Biochem. J. 274:731-738(1991). Cited for: PROTEIN SEQUENCE OF 1614-1623; 1730-1748; 1756-1759; 1803-1811;1860-1923; 1930-1945; 1949-1972; 1982-1989; 1991-2003; 2020-2038;2060-2131; 2150-2180; 2185-2205 AND 2231-2242, GLYCOSYLATION ATTHR-2064 AND THR-2065, LACK OF GLYCOSYLATION AT ASN-2108, MASSSPECTROMETRY, AND VARIANT ILE-2170. | |
Phosphorylation | |
Reference | PubMed |
"An initial characterization of the serum phosphoproteome."; Zhou W., Ross M.M., Tessitore A., Ornstein D., Vanmeter A.,Liotta L.A., Petricoin E.F. III; J. Proteome Res. 8:5523-5531(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2341 AND SER-2349,TISSUE SPECIFICITY, AND MASS SPECTROMETRY. | |
"Large-scale phosphoproteome analysis of human liver tissue byenrichment and fractionation of phosphopeptides with strong anionexchange chromatography."; Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,Zou H., Gu J.; Proteomics 8:1346-1361(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2384, AND MASSSPECTROMETRY. | |
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-904, AND MASSSPECTROMETRY. | |
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2384, AND MASSSPECTROMETRY. |