MFAP1_HUMAN
ID MFAP1_HUMAN Reviewed; 439 AA.
AC P55081; Q86TG6;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 2.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Microfibrillar-associated protein 1 {ECO:0000312|HGNC:HGNC:7032};
DE AltName: Full=Spliceosome B complex protein MFAP1 {ECO:0000303|PubMed:28781166};
GN Name=MFAP1 {ECO:0000312|HGNC:HGNC:7032};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Skin;
RX PubMed=7835894; DOI=10.1006/geno.1994.1521;
RA Yeh H., Chow M., Abrams W.R., Fan J., Foster J., Mitchell H., Muenke M.,
RA Rosenbloom J.;
RT "Structure of the human gene encoding the associated microfibrillar protein
RT (MFAP1) and localization to chromosome 15q15-q21.";
RL Genomics 23:443-449(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Trachea;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16572171; DOI=10.1038/nature04601;
RA Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J.,
RA Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E.,
RA Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B.,
RA Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R.,
RA O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B.,
RA Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S.,
RA Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.;
RT "Analysis of the DNA sequence and duplication history of human chromosome
RT 15.";
RL Nature 440:671-675(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Muscle, and PNS;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-116; SER-118; SER-132;
RP SER-133 AND THR-267, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-116; SER-118 AND THR-267, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Prostate cancer;
RX PubMed=17487921; DOI=10.1002/elps.200600782;
RA Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.;
RT "Toward a global characterization of the phosphoproteome in prostate cancer
RT cells: identification of phosphoproteins in the LNCaP cell line.";
RL Electrophoresis 28:2027-2034(2007).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-116; SER-118 AND THR-267, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52; SER-53 AND THR-267, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-116; SER-118 AND THR-267, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18318008; DOI=10.1002/pmic.200700884;
RA Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
RA Zou H., Gu J.;
RT "Large-scale phosphoproteome analysis of human liver tissue by enrichment
RT and fractionation of phosphopeptides with strong anion exchange
RT chromatography.";
RL Proteomics 8:1346-1361(2008).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52; SER-53; SER-116; SER-132
RP AND THR-267, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52; SER-53; SER-116; SER-118;
RP SER-132; SER-133 AND THR-267, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52; SER-53; SER-116; SER-118;
RP SER-132; SER-133 AND THR-267, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [17]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [18]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52; SER-53; SER-94; SER-116;
RP SER-118; SER-132; SER-133; THR-267; SER-361 AND SER-432, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-53; SER-116; SER-118 AND
RP THR-267, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [21]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-249, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25755297; DOI=10.1074/mcp.o114.044792;
RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
RA Vertegaal A.C.;
RT "System-wide analysis of SUMOylation dynamics in response to replication
RT stress reveals novel small ubiquitin-like modified target proteins and
RT acceptor lysines relevant for genome stability.";
RL Mol. Cell. Proteomics 14:1419-1434(2015).
RN [22]
RP INTERACTION WITH PRPF38A.
RX PubMed=26673105; DOI=10.1261/rna.054296.115;
RA Schuetze T., Ulrich A.K., Apelt L., Will C.L., Bartlick N., Seeger M.,
RA Weber G., Luehrmann R., Stelzl U., Wahl M.C.;
RT "Multiple protein-protein interactions converging on the Prp38 protein
RT during activation of the human spliceosome.";
RL RNA 22:265-277(2016).
RN [23]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-67; LYS-249; LYS-357; LYS-371;
RP LYS-381; LYS-415 AND LYS-418, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [24] {ECO:0007744|PDB:5F5S}
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 267-344 IN COMPLEX WITH PRPF38A,
RP AND INTERACTION WITH PRPF38A.
RX PubMed=27773687; DOI=10.1016/j.str.2016.09.007;
RA Ulrich A.K.C., Seeger M., Schutze T., Bartlick N., Wahl M.C.;
RT "Scaffolding in the Spliceosome via Single alpha Helices.";
RL Structure 24:1972-1983(2016).
RN [25] {ECO:0007744|PDB:5O9Z}
RP STRUCTURE BY ELECTRON MICROSCOPY (4.50 ANGSTROMS), IDENTIFICATION BY MASS
RP SPECTROMETRY, FUNCTION, SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=28781166; DOI=10.1016/j.cell.2017.07.011;
RA Bertram K., Agafonov D.E., Dybkov O., Haselbach D., Leelaram M.N.,
RA Will C.L., Urlaub H., Kastner B., Luhrmann R., Stark H.;
RT "Cryo-EM Structure of a Pre-catalytic Human Spliceosome Primed for
RT Activation.";
RL Cell 170:701-713(2017).
CC -!- FUNCTION: Involved in pre-mRNA splicing as a component of the
CC spliceosome. {ECO:0000269|PubMed:28781166}.
CC -!- SUBUNIT: Component of the spliceosome B complex (PubMed:28781166).
CC Interacts with PRPF38A (via N-terminal interaction domain)
CC (PubMed:26673105, PubMed:27773687). {ECO:0000269|PubMed:26673105,
CC ECO:0000269|PubMed:27773687, ECO:0000269|PubMed:28781166}.
CC -!- INTERACTION:
CC P55081; Q96BT7-2: ALKBH8; NbExp=3; IntAct=EBI-1048159, EBI-13329511;
CC P55081; Q9Y2J4: AMOTL2; NbExp=3; IntAct=EBI-1048159, EBI-746752;
CC P55081; Q9Y2J4-4: AMOTL2; NbExp=3; IntAct=EBI-1048159, EBI-10187270;
CC P55081; Q96CW1: AP2M1; NbExp=3; IntAct=EBI-1048159, EBI-297683;
CC P55081; Q8N7W2-2: BEND7; NbExp=6; IntAct=EBI-1048159, EBI-10181188;
CC P55081; Q6PI77: BHLHB9; NbExp=3; IntAct=EBI-1048159, EBI-11519926;
CC P55081; Q8TD16-2: BICD2; NbExp=3; IntAct=EBI-1048159, EBI-11975051;
CC P55081; Q9H2G9: BLZF1; NbExp=3; IntAct=EBI-1048159, EBI-2548012;
CC P55081; Q9H257: CARD9; NbExp=3; IntAct=EBI-1048159, EBI-751319;
CC P55081; Q9H257-2: CARD9; NbExp=3; IntAct=EBI-1048159, EBI-11530605;
CC P55081; Q68D86: CCDC102B; NbExp=3; IntAct=EBI-1048159, EBI-10171570;
CC P55081; Q2TAC2: CCDC57; NbExp=3; IntAct=EBI-1048159, EBI-2808286;
CC P55081; O60729: CDC14B; NbExp=3; IntAct=EBI-1048159, EBI-970231;
CC P55081; Q96GN5: CDCA7L; NbExp=3; IntAct=EBI-1048159, EBI-5278764;
CC P55081; Q53EZ4: CEP55; NbExp=6; IntAct=EBI-1048159, EBI-747776;
CC P55081; Q8IYX8: CEP57L1; NbExp=3; IntAct=EBI-1048159, EBI-1104570;
CC P55081; Q8IYX8-2: CEP57L1; NbExp=3; IntAct=EBI-1048159, EBI-10181988;
CC P55081; Q8NHQ1: CEP70; NbExp=6; IntAct=EBI-1048159, EBI-739624;
CC P55081; Q8TAP6: CEP76; NbExp=3; IntAct=EBI-1048159, EBI-742887;
CC P55081; Q9Y2V7: COG6; NbExp=3; IntAct=EBI-1048159, EBI-3866319;
CC P55081; P38432: COIL; NbExp=3; IntAct=EBI-1048159, EBI-945751;
CC P55081; Q9H147: DNTTIP1; NbExp=3; IntAct=EBI-1048159, EBI-2795449;
CC P55081; Q8IZU0: FAM9B; NbExp=3; IntAct=EBI-1048159, EBI-10175124;
CC P55081; O94868-3: FCHSD2; NbExp=3; IntAct=EBI-1048159, EBI-11958845;
CC P55081; P51114-2: FXR1; NbExp=3; IntAct=EBI-1048159, EBI-11022345;
CC P55081; P51116: FXR2; NbExp=6; IntAct=EBI-1048159, EBI-740459;
CC P55081; O95995: GAS8; NbExp=3; IntAct=EBI-1048159, EBI-1052570;
CC P55081; Q5VSY0: GKAP1; NbExp=3; IntAct=EBI-1048159, EBI-743722;
CC P55081; Q96IK5: GMCL1; NbExp=3; IntAct=EBI-1048159, EBI-2548508;
CC P55081; Q08379: GOLGA2; NbExp=6; IntAct=EBI-1048159, EBI-618309;
CC P55081; A6NEM1: GOLGA6L9; NbExp=3; IntAct=EBI-1048159, EBI-5916454;
CC P55081; Q4V328: GRIPAP1; NbExp=3; IntAct=EBI-1048159, EBI-717919;
CC P55081; Q6NT76: HMBOX1; NbExp=6; IntAct=EBI-1048159, EBI-2549423;
CC P55081; Q9NSC5: HOMER3; NbExp=3; IntAct=EBI-1048159, EBI-748420;
CC P55081; Q96ED9-2: HOOK2; NbExp=3; IntAct=EBI-1048159, EBI-10961706;
CC P55081; O75031: HSF2BP; NbExp=3; IntAct=EBI-1048159, EBI-7116203;
CC P55081; Q13123: IK; NbExp=2; IntAct=EBI-1048159, EBI-713456;
CC P55081; Q9H079: KATNBL1; NbExp=7; IntAct=EBI-1048159, EBI-715394;
CC P55081; Q9BVG8: KIFC3; NbExp=3; IntAct=EBI-1048159, EBI-2125614;
CC P55081; Q9BVG8-5: KIFC3; NbExp=3; IntAct=EBI-1048159, EBI-14069005;
CC P55081; O95198: KLHL2; NbExp=3; IntAct=EBI-1048159, EBI-746999;
CC P55081; Q6A162: KRT40; NbExp=3; IntAct=EBI-1048159, EBI-10171697;
CC P55081; Q96JM7-2: L3MBTL3; NbExp=3; IntAct=EBI-1048159, EBI-11985629;
CC P55081; O95751: LDOC1; NbExp=6; IntAct=EBI-1048159, EBI-740738;
CC P55081; Q03252: LMNB2; NbExp=3; IntAct=EBI-1048159, EBI-2830427;
CC P55081; Q9Y250: LZTS1; NbExp=3; IntAct=EBI-1048159, EBI-1216080;
CC P55081; Q9Y6D9: MAD1L1; NbExp=6; IntAct=EBI-1048159, EBI-742610;
CC P55081; Q96EZ8: MCRS1; NbExp=3; IntAct=EBI-1048159, EBI-348259;
CC P55081; Q9UJV3-2: MID2; NbExp=6; IntAct=EBI-1048159, EBI-10172526;
CC P55081; Q8TD10: MIPOL1; NbExp=3; IntAct=EBI-1048159, EBI-2548751;
CC P55081; Q5JR59: MTUS2; NbExp=3; IntAct=EBI-1048159, EBI-742948;
CC P55081; O14777: NDC80; NbExp=3; IntAct=EBI-1048159, EBI-715849;
CC P55081; Q8NEJ9: NGDN; NbExp=3; IntAct=EBI-1048159, EBI-9995414;
CC P55081; Q7RTU3: OLIG3; NbExp=3; IntAct=EBI-1048159, EBI-10225049;
CC P55081; P26367: PAX6; NbExp=3; IntAct=EBI-1048159, EBI-747278;
CC P55081; Q8IXK0: PHC2; NbExp=3; IntAct=EBI-1048159, EBI-713786;
CC P55081; Q4G0R1: PIBF1; NbExp=3; IntAct=EBI-1048159, EBI-14066006;
CC P55081; Q9NWS0: PIH1D1; NbExp=3; IntAct=EBI-1048159, EBI-357318;
CC P55081; Q96BK5: PINX1; NbExp=3; IntAct=EBI-1048159, EBI-721782;
CC P55081; Q9H8W4: PLEKHF2; NbExp=3; IntAct=EBI-1048159, EBI-742388;
CC P55081; O43395: PRPF3; NbExp=2; IntAct=EBI-1048159, EBI-744322;
CC P55081; Q8TAD8: SNIP1; NbExp=4; IntAct=EBI-1048159, EBI-749336;
CC P55081; Q9Y2D8: SSX2IP; NbExp=3; IntAct=EBI-1048159, EBI-2212028;
CC P55081; Q96MF2: STAC3; NbExp=3; IntAct=EBI-1048159, EBI-745680;
CC P55081; O75558: STX11; NbExp=3; IntAct=EBI-1048159, EBI-714135;
CC P55081; O75478: TADA2A; NbExp=3; IntAct=EBI-1048159, EBI-742268;
CC P55081; Q8TDR4: TCP10L; NbExp=3; IntAct=EBI-1048159, EBI-3923210;
CC P55081; Q96N21: TEPSIN; NbExp=3; IntAct=EBI-1048159, EBI-11139477;
CC P55081; Q9UBB9: TFIP11; NbExp=3; IntAct=EBI-1048159, EBI-1105213;
CC P55081; Q9NVV9: THAP1; NbExp=3; IntAct=EBI-1048159, EBI-741515;
CC P55081; Q08117: TLE5; NbExp=3; IntAct=EBI-1048159, EBI-717810;
CC P55081; Q08117-2: TLE5; NbExp=5; IntAct=EBI-1048159, EBI-11741437;
CC P55081; P19237: TNNI1; NbExp=3; IntAct=EBI-1048159, EBI-746692;
CC P55081; Q12933: TRAF2; NbExp=3; IntAct=EBI-1048159, EBI-355744;
CC P55081; Q8WV44: TRIM41; NbExp=3; IntAct=EBI-1048159, EBI-725997;
CC P55081; Q8IWZ5: TRIM42; NbExp=3; IntAct=EBI-1048159, EBI-5235829;
CC P55081; Q9BYV2: TRIM54; NbExp=6; IntAct=EBI-1048159, EBI-2130429;
CC P55081; Q5W5X9-3: TTC23; NbExp=3; IntAct=EBI-1048159, EBI-9090990;
CC P55081; Q8N1B4: VPS52; NbExp=6; IntAct=EBI-1048159, EBI-2799833;
CC P55081; Q9Y2K1: ZBTB1; NbExp=3; IntAct=EBI-1048159, EBI-2682961;
CC P55081; O43829: ZBTB14; NbExp=3; IntAct=EBI-1048159, EBI-10176632;
CC P55081; Q96BR9: ZBTB8A; NbExp=3; IntAct=EBI-1048159, EBI-742740;
CC P55081; Q6P2D0: ZFP1; NbExp=3; IntAct=EBI-1048159, EBI-2555749;
CC P55081; Q8N8Y5: ZFP41; NbExp=3; IntAct=EBI-1048159, EBI-12224489;
CC P55081; Q9NTW7: ZFP64; NbExp=3; IntAct=EBI-1048159, EBI-711679;
CC P55081; P52741: ZNF134; NbExp=3; IntAct=EBI-1048159, EBI-18054945;
CC P55081; Q9UDV6: ZNF212; NbExp=3; IntAct=EBI-1048159, EBI-1640204;
CC P55081; Q8TD17: ZNF398; NbExp=7; IntAct=EBI-1048159, EBI-8643207;
CC P55081; P51814-6: ZNF41; NbExp=3; IntAct=EBI-1048159, EBI-12700258;
CC P55081; Q96NG5: ZNF558; NbExp=3; IntAct=EBI-1048159, EBI-373363;
CC P55081; Q6ZNG0: ZNF620; NbExp=3; IntAct=EBI-1048159, EBI-4395669;
CC P55081; Q9NQZ8: ZNF71; NbExp=3; IntAct=EBI-1048159, EBI-7138235;
CC P55081; P36508: ZNF76; NbExp=3; IntAct=EBI-1048159, EBI-7254550;
CC P55081; Q9UGI0: ZRANB1; NbExp=3; IntAct=EBI-1048159, EBI-527853;
CC P55081; Q15695: ZRSR2P1; NbExp=3; IntAct=EBI-1048159, EBI-12270264;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:28781166}.
CC -!- SIMILARITY: Belongs to the MFAP1 family. {ECO:0000305}.
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DR EMBL; U04209; AAA92786.1; -; mRNA.
DR EMBL; AK312867; BAG35719.1; -; mRNA.
DR EMBL; AC018512; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471082; EAW77247.1; -; Genomic_DNA.
DR EMBL; BC023557; AAH23557.1; -; mRNA.
DR EMBL; BC050742; AAH50742.1; -; mRNA.
DR CCDS; CCDS10105.1; -.
DR PIR; A55565; A55565.
DR RefSeq; NP_005917.2; NM_005926.2.
DR PDB; 5F5S; X-ray; 2.40 A; B=267-344.
DR PDB; 5O9Z; EM; 4.50 A; K=1-439.
DR PDB; 6AHD; EM; 3.80 A; 0=1-439.
DR PDB; 7AAV; EM; 4.20 A; K=1-439.
DR PDB; 7ABF; EM; 3.90 A; K=1-439.
DR PDB; 7ABG; EM; 7.80 A; K=1-439.
DR PDB; 7ABI; EM; 8.00 A; K=1-439.
DR PDBsum; 5F5S; -.
DR PDBsum; 5O9Z; -.
DR PDBsum; 6AHD; -.
DR PDBsum; 7AAV; -.
DR PDBsum; 7ABF; -.
DR PDBsum; 7ABG; -.
DR PDBsum; 7ABI; -.
DR AlphaFoldDB; P55081; -.
DR SMR; P55081; -.
DR BioGRID; 110394; 258.
DR CORUM; P55081; -.
DR IntAct; P55081; 129.
DR MINT; P55081; -.
DR STRING; 9606.ENSP00000267812; -.
DR GlyGen; P55081; 2 sites, 1 O-linked glycan (1 site).
DR iPTMnet; P55081; -.
DR PhosphoSitePlus; P55081; -.
DR BioMuta; MFAP1; -.
DR DMDM; 205831094; -.
DR EPD; P55081; -.
DR jPOST; P55081; -.
DR MassIVE; P55081; -.
DR MaxQB; P55081; -.
DR PaxDb; P55081; -.
DR PeptideAtlas; P55081; -.
DR PRIDE; P55081; -.
DR ProteomicsDB; 56782; -.
DR TopDownProteomics; P55081; -.
DR Antibodypedia; 24163; 134 antibodies from 23 providers.
DR DNASU; 4236; -.
DR Ensembl; ENST00000267812.4; ENSP00000267812.3; ENSG00000140259.7.
DR GeneID; 4236; -.
DR KEGG; hsa:4236; -.
DR MANE-Select; ENST00000267812.4; ENSP00000267812.3; NM_005926.3; NP_005917.2.
DR UCSC; uc001zth.2; human.
DR CTD; 4236; -.
DR DisGeNET; 4236; -.
DR GeneCards; MFAP1; -.
DR HGNC; HGNC:7032; MFAP1.
DR HPA; ENSG00000140259; Low tissue specificity.
DR MIM; 600215; gene.
DR neXtProt; NX_P55081; -.
DR OpenTargets; ENSG00000140259; -.
DR PharmGKB; PA30768; -.
DR VEuPathDB; HostDB:ENSG00000140259; -.
DR eggNOG; KOG1425; Eukaryota.
DR GeneTree; ENSGT00690000102225; -.
DR HOGENOM; CLU_023077_1_0_1; -.
DR InParanoid; P55081; -.
DR OMA; FHNERAG; -.
DR OrthoDB; 1535406at2759; -.
DR PhylomeDB; P55081; -.
DR TreeFam; TF314398; -.
DR PathwayCommons; P55081; -.
DR Reactome; R-HSA-2129379; Molecules associated with elastic fibres.
DR SignaLink; P55081; -.
DR BioGRID-ORCS; 4236; 793 hits in 1092 CRISPR screens.
DR ChiTaRS; MFAP1; human.
DR GeneWiki; MFAP1; -.
DR GenomeRNAi; 4236; -.
DR Pharos; P55081; Tbio.
DR PRO; PR:P55081; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; P55081; protein.
DR Bgee; ENSG00000140259; Expressed in secondary oocyte and 205 other tissues.
DR Genevisible; P55081; HS.
DR GO; GO:0005813; C:centrosome; IDA:HPA.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0001527; C:microfibril; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0071005; C:U2-type precatalytic spliceosome; IDA:UniProtKB.
DR GO; GO:0005684; C:U2-type spliceosomal complex; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IDA:UniProtKB.
DR InterPro; IPR033194; MFAP1.
DR InterPro; IPR009730; MFAP1_C.
DR PANTHER; PTHR15327; PTHR15327; 1.
DR Pfam; PF06991; MFAP1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Isopeptide bond; mRNA processing; mRNA splicing;
KW Nucleus; Phosphoprotein; Reference proteome; Spliceosome; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:22814378"
FT CHAIN 2..439
FT /note="Microfibrillar-associated protein 1"
FT /id="PRO_0000096458"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 39..200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 80..129
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 144..167
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 168..192
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:22814378"
FT MOD_RES 52
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 53
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 94
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 116
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:17487921, ECO:0007744|PubMed:18318008,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 118
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:17487921, ECO:0007744|PubMed:18318008,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 132
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 133
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 267
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:17487921, ECO:0007744|PubMed:18318008,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 361
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 432
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CROSSLNK 67
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 249
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25755297,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 357
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 371
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 381
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 415
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 418
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CONFLICT 238
FT /note="K -> Q (in Ref. 1; AAA92786)"
FT /evidence="ECO:0000305"
FT CONFLICT 242
FT /note="K -> Q (in Ref. 1; AAA92786)"
FT /evidence="ECO:0000305"
FT CONFLICT 245
FT /note="E -> G (in Ref. 1; AAA92786)"
FT /evidence="ECO:0000305"
FT CONFLICT 249
FT /note="K -> P (in Ref. 1; AAA92786)"
FT /evidence="ECO:0000305"
FT HELIX 273..321
FT /evidence="ECO:0007829|PDB:5F5S"
SQ SEQUENCE 439 AA; 51958 MW; 0EF6F4F091C05A88 CRC64;
MSVPSALMKQ PPIQSTAGAV PVRNEKGEIS MEKVKVKRYV SGKRPDYAPM ESSDEEDEEF
QFIKKAKEQE AEPEEQEEDS SSDPRLRRLQ NRISEDVEER LARHRKIVEP EVVGESDSEV
EGDAWRMERE DSSEEEEEEI DDEEIERRRG MMRQRAQERK NEEMEVMEVE DEGRSGEESE
SESEYEEYTD SEDEMEPRLK PVFIRKKDRV TVQEREAEAL KQKELEQEAK RMAEERRKYT
LKIVEEETKK ELEENKRSLA ALDALNTDDE NDEEEYEAWK VRELKRIKRD REDREALEKE
KAEIERMRNL TEEERRAELR ANGKVITNKA VKGKYKFLQK YYHRGAFFMD EDEEVYKRDF
SAPTLEDHFN KTILPKVMQV KNFGRSGRTK YTHLVDQDTT SFDSAWGQES AQNTKFFKQK
AAGVRDVFER PSAKKRKTT
