PR40A_HUMAN
ID PR40A_HUMAN Reviewed; 957 AA.
AC O75400; O43856; O75404; Q8TBQ1; Q9H782; Q9NWU9; Q9P0Q2; Q9Y5A8;
DT 22-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2003, sequence version 2.
DT 03-AUG-2022, entry version 206.
DE RecName: Full=Pre-mRNA-processing factor 40 homolog A;
DE AltName: Full=Fas ligand-associated factor 1;
DE AltName: Full=Formin-binding protein 11;
DE AltName: Full=Formin-binding protein 3;
DE AltName: Full=Huntingtin yeast partner A;
DE AltName: Full=Huntingtin-interacting protein 10;
DE Short=HIP-10;
DE AltName: Full=Huntingtin-interacting protein A;
DE AltName: Full=Renal carcinoma antigen NY-REN-6;
GN Name=PRPF40A; Synonyms=FBP11, FLAF1, FNBP3, HIP10, HYPA; ORFNames=HSPC225;
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 [LARGE SCALE MRNA] (ISOFORM 5), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 710-957 (ISOFORM 1).
RC TISSUE=Smooth muscle;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-448 (ISOFORM 1), NUCLEOTIDE SEQUENCE [MRNA]
RP OF 1-423 (ISOFORM 2), INTERACTION WITH HTT, AND TISSUE SPECIFICITY.
RC TISSUE=Frontal cortex;
RX PubMed=9700202; DOI=10.1093/hmg/7.9.1463;
RA Faber P.W., Barnes G.T., Srinidhi J., Chen J., Gusella J.F.,
RA MacDonald M.E.;
RT "Huntingtin interacts with a family of WW domain proteins.";
RL Hum. Mol. Genet. 7:1463-1474(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-449 AND 743-957 (ISOFORM 2).
RC TISSUE=Lymphoma;
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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 8-374 (ISOFORM 3).
RC TISSUE=Placenta;
RA Hachiya T., Kobayasi A., Touji S., Tamai K.;
RT "A Fas-ligand associated factor 1, FLAF1, potentiates Fas-ligand
RT stability.";
RL Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 542-957, AND IDENTIFICATION AS A RENAL CANCER
RP ANTIGEN.
RX PubMed=10508479;
RX DOI=10.1002/(sici)1097-0215(19991112)83:4<456::aid-ijc4>3.0.co;2-5;
RA Scanlan M.J., Gordan J.D., Williamson B., Stockert E., Bander N.H.,
RA Jongeneel C.V., Gure A.O., Jaeger D., Jaeger E., Knuth A., Chen Y.-T.,
RA Old L.J.;
RT "Antigens recognized by autologous antibody in patients with renal-cell
RT carcinoma.";
RL Int. J. Cancer 83:456-464(1999).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 646-957.
RC TISSUE=Umbilical cord blood;
RX PubMed=11042152; DOI=10.1101/gr.140200;
RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
RT "Cloning and functional analysis of cDNAs with open reading frames for 300
RT previously undefined genes expressed in CD34+ hematopoietic stem/progenitor
RT cells.";
RL Genome Res. 10:1546-1560(2000).
RN [8]
RP INTERACTION WITH POLR2A, AND STRUCTURE BY NMR OF 381-450.
RX PubMed=12381297; DOI=10.1016/s0022-2836(02)00968-3;
RA Allen M., Friedler A., Schon O., Bycroft M.;
RT "The structure of an FF domain from human HYPA/FBP11.";
RL J. Mol. Biol. 323:411-416(2002).
RN [9]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=16391387; DOI=10.1385/nmm:7:4:297;
RA Sayer J.A., Manczak M., Akileswaran L., Reddy P.H., Coghlan V.M.;
RT "Interaction of the nuclear matrix protein NAKAP with HypA and huntingtin:
RT implications for nuclear toxicity in Huntington's disease pathogenesis.";
RL NeuroMolecular Med. 7:297-310(2005).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-373; SER-883; SER-885;
RP SER-888 AND SER-938, 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 [11]
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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-932; SER-933; SER-935 AND
RP SER-938, AND 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 [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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 ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-196, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-151; THR-373; SER-933 AND
RP SER-938, AND IDENTIFICATION BY MASS SPECTROMETRY [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 [16]
RP FUNCTION.
RX PubMed=21834987; DOI=10.1186/1741-7007-9-54;
RA Bai S.W., Herrera-Abreu M.T., Rohn J.L., Racine V., Tajadura V.,
RA Suryavanshi N., Bechtel S., Wiemann S., Baum B., Ridley A.J.;
RT "Identification and characterization of a set of conserved and new
RT regulators of cytoskeletal organisation, cell morphology and migration.";
RL BMC Biol. 9:54-54(2011).
RN [17]
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 [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-883; SER-888; SER-933 AND
RP SER-938, AND IDENTIFICATION BY MASS SPECTROMETRY [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 [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-34; SER-151; THR-373;
RP SER-723; SER-787; SER-883; SER-885; SER-888 AND SER-938, 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 THR-345; THR-373 AND SER-938, AND
RP 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 METHYLATION [LARGE SCALE ANALYSIS] AT ARG-17; ARG-24 AND ARG-47 (ISOFORMS 2
RP AND 5), AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [22]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-241, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [23]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-191; LYS-241; LYS-375 AND
RP LYS-376, AND IDENTIFICATION BY MASS SPECTROMETRY [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]
RP STRUCTURE BY NMR OF 743-806.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the FF domain of human formin-binding protein 3.";
RL Submitted (NOV-2005) to the PDB data bank.
CC -!- FUNCTION: Binds to WASL/N-WASP and suppresses its translocation from
CC the nucleus to the cytoplasm, thereby inhibiting its cytoplasmic
CC function (By similarity). Plays a role in the regulation of cell
CC morphology and cytoskeletal organization. Required in the control of
CC cell shape and migration. May play a role in cytokinesis. May be
CC involved in pre-mRNA splicing. {ECO:0000250,
CC ECO:0000269|PubMed:21834987}.
CC -!- SUBUNIT: Interacts with the N-terminus of HTT. Interacts with the
CC phosphorylated C-terminal domain of POLR2A. Interacts with AKAP8L, SF1,
CC SRPK1, ENAH, ATBF1 and MECP2 (By similarity). Interacts through the WW
CC domains with formin proline-rich regions and with WASL/N-WASP (By
CC similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC O75400; Q12873: CHD3; NbExp=2; IntAct=EBI-473291, EBI-523590;
CC O75400; P42858: HTT; NbExp=15; IntAct=EBI-473291, EBI-466029;
CC O75400; Q8N5F7: NKAP; NbExp=2; IntAct=EBI-473291, EBI-721539;
CC O75400; Q15637: SF1; NbExp=3; IntAct=EBI-473291, EBI-744603;
CC O75400; Q15459: SF3A1; NbExp=2; IntAct=EBI-473291, EBI-1054743;
CC O75400-2; P45844-6: ABCG1; NbExp=3; IntAct=EBI-5280197, EBI-25873349;
CC O75400-2; Q6DHV7-2: ADAL; NbExp=3; IntAct=EBI-5280197, EBI-18899653;
CC O75400-2; Q5T2L2: AKR1C8P; NbExp=3; IntAct=EBI-5280197, EBI-22006248;
CC O75400-2; Q96Q83-2: ALKBH3; NbExp=3; IntAct=EBI-5280197, EBI-9089544;
CC O75400-2; Q9NU02: ANKEF1; NbExp=3; IntAct=EBI-5280197, EBI-8464238;
CC O75400-2; Q6LES2: ANXA4; NbExp=3; IntAct=EBI-5280197, EBI-10250835;
CC O75400-2; P53365: ARFIP2; NbExp=3; IntAct=EBI-5280197, EBI-638194;
CC O75400-2; Q66PJ3-4: ARL6IP4; NbExp=3; IntAct=EBI-5280197, EBI-5280499;
CC O75400-2; P18848: ATF4; NbExp=3; IntAct=EBI-5280197, EBI-492498;
CC O75400-2; Q9H0Y0: ATG10; NbExp=3; IntAct=EBI-5280197, EBI-1048913;
CC O75400-2; Q14032: BAAT; NbExp=3; IntAct=EBI-5280197, EBI-8994378;
CC O75400-2; P54687-4: BCAT1; NbExp=3; IntAct=EBI-5280197, EBI-25834445;
CC O75400-2; P06276: BCHE; NbExp=3; IntAct=EBI-5280197, EBI-7936069;
CC O75400-2; Q8N7W2-2: BEND7; NbExp=3; IntAct=EBI-5280197, EBI-10181188;
CC O75400-2; Q9NQ89: C12orf4; NbExp=3; IntAct=EBI-5280197, EBI-11090973;
CC O75400-2; Q3SXR2: C3orf36; NbExp=3; IntAct=EBI-5280197, EBI-18036948;
CC O75400-2; Q96LM5: C4orf45; NbExp=3; IntAct=EBI-5280197, EBI-12020542;
CC O75400-2; P17655: CAPN2; NbExp=3; IntAct=EBI-5280197, EBI-1028956;
CC O75400-2; P20807-4: CAPN3; NbExp=3; IntAct=EBI-5280197, EBI-11532021;
CC O75400-2; O00257-3: CBX4; NbExp=3; IntAct=EBI-5280197, EBI-4392727;
CC O75400-2; P24863: CCNC; NbExp=3; IntAct=EBI-5280197, EBI-395261;
CC O75400-2; Q9UK58: CCNL1; NbExp=3; IntAct=EBI-5280197, EBI-2836773;
CC O75400-2; Q9UK58-5: CCNL1; NbExp=3; IntAct=EBI-5280197, EBI-25873837;
CC O75400-2; Q9NNX6-10: CD209; NbExp=3; IntAct=EBI-5280197, EBI-12300031;
CC O75400-2; Q9UJX2: CDC23; NbExp=3; IntAct=EBI-5280197, EBI-396137;
CC O75400-2; P42773: CDKN2C; NbExp=3; IntAct=EBI-5280197, EBI-711290;
CC O75400-2; O95674: CDS2; NbExp=3; IntAct=EBI-5280197, EBI-3913685;
CC O75400-2; Q494V2-2: CFAP100; NbExp=3; IntAct=EBI-5280197, EBI-11953200;
CC O75400-2; Q9Y3D0: CIAO2B; NbExp=3; IntAct=EBI-5280197, EBI-744045;
CC O75400-2; P09496-2: CLTA; NbExp=3; IntAct=EBI-5280197, EBI-4401010;
CC O75400-2; Q96BR5: COA7; NbExp=3; IntAct=EBI-5280197, EBI-6269632;
CC O75400-2; P02458-1: COL2A1; NbExp=3; IntAct=EBI-5280197, EBI-12375799;
CC O75400-2; Q9UGL9: CRCT1; NbExp=3; IntAct=EBI-5280197, EBI-713677;
CC O75400-2; Q9UKG9-2: CROT; NbExp=3; IntAct=EBI-5280197, EBI-25835363;
CC O75400-2; P26998: CRYBB3; NbExp=3; IntAct=EBI-5280197, EBI-1965681;
CC O75400-2; P68400: CSNK2A1; NbExp=2; IntAct=EBI-5280197, EBI-347804;
CC O75400-2; Q5HYN5: CT45A1; NbExp=3; IntAct=EBI-5280197, EBI-12051833;
CC O75400-2; P35222: CTNNB1; NbExp=3; IntAct=EBI-5280197, EBI-491549;
CC O75400-2; Q53TN4: CYBRD1; NbExp=3; IntAct=EBI-5280197, EBI-8637742;
CC O75400-2; P10632: CYP2C8; NbExp=3; IntAct=EBI-5280197, EBI-2951522;
CC O75400-2; Q96D03: DDIT4L; NbExp=3; IntAct=EBI-5280197, EBI-742054;
CC O75400-2; Q96LJ7: DHRS1; NbExp=3; IntAct=EBI-5280197, EBI-746300;
CC O75400-2; O60479: DLX3; NbExp=3; IntAct=EBI-5280197, EBI-3908248;
CC O75400-2; Q96EY1-3: DNAJA3; NbExp=3; IntAct=EBI-5280197, EBI-11526226;
CC O75400-2; Q96BY6: DOCK10; NbExp=3; IntAct=EBI-5280197, EBI-748520;
CC O75400-2; Q92782-2: DPF1; NbExp=3; IntAct=EBI-5280197, EBI-23669343;
CC O75400-2; Q9BPU6: DPYSL5; NbExp=3; IntAct=EBI-5280197, EBI-724653;
CC O75400-2; Q86YF9: DZIP1; NbExp=3; IntAct=EBI-5280197, EBI-998108;
CC O75400-2; Q8IYY4: DZIP1L; NbExp=3; IntAct=EBI-5280197, EBI-10264440;
CC O75400-2; O00303: EIF3F; NbExp=3; IntAct=EBI-5280197, EBI-711990;
CC O75400-2; O00472: ELL2; NbExp=3; IntAct=EBI-5280197, EBI-395274;
CC O75400-2; Q49AJ0-4: FAM135B; NbExp=3; IntAct=EBI-5280197, EBI-25835236;
CC O75400-2; Q96KS9: FAM167A; NbExp=3; IntAct=EBI-5280197, EBI-10290462;
CC O75400-2; Q8IZU1: FAM9A; NbExp=3; IntAct=EBI-5280197, EBI-8468186;
CC O75400-2; Q6ZNL6: FGD5; NbExp=3; IntAct=EBI-5280197, EBI-7962481;
CC O75400-2; Q49A26-4: GLYR1; NbExp=3; IntAct=EBI-5280197, EBI-12143817;
CC O75400-2; P32780: GTF2H1; NbExp=3; IntAct=EBI-5280197, EBI-715539;
CC O75400-2; Q9NRZ9-6: HELLS; NbExp=3; IntAct=EBI-5280197, EBI-12003732;
CC O75400-2; Q96EW2-2: HSPBAP1; NbExp=3; IntAct=EBI-5280197, EBI-25835621;
CC O75400-2; P42858: HTT; NbExp=9; IntAct=EBI-5280197, EBI-466029;
CC O75400-2; P0C870: JMJD7; NbExp=3; IntAct=EBI-5280197, EBI-9090173;
CC O75400-2; Q8N5Z5: KCTD17; NbExp=3; IntAct=EBI-5280197, EBI-743960;
CC O75400-2; Q8TBB5-2: KLHDC4; NbExp=3; IntAct=EBI-5280197, EBI-21838933;
CC O75400-2; Q8N4N3-2: KLHL36; NbExp=3; IntAct=EBI-5280197, EBI-10973851;
CC O75400-2; Q5JUW0-3: KRBOX4; NbExp=3; IntAct=EBI-5280197, EBI-12893625;
CC O75400-2; Q6DKI2: LGALS9C; NbExp=3; IntAct=EBI-5280197, EBI-9088829;
CC O75400-2; Q9H2C1: LHX5; NbExp=3; IntAct=EBI-5280197, EBI-25835523;
CC O75400-2; Q1L5Z9: LONRF2; NbExp=3; IntAct=EBI-5280197, EBI-2510853;
CC O75400-2; P27338: MAOB; NbExp=3; IntAct=EBI-5280197, EBI-3911344;
CC O75400-2; A0A0A0MR05: MLST8; NbExp=3; IntAct=EBI-5280197, EBI-25835557;
CC O75400-2; P34949-2: MPI; NbExp=3; IntAct=EBI-5280197, EBI-21823432;
CC O75400-2; Q9BV20: MRI1; NbExp=3; IntAct=EBI-5280197, EBI-747381;
CC O75400-2; Q6IN84-2: MRM1; NbExp=3; IntAct=EBI-5280197, EBI-25835707;
CC O75400-2; P01106: MYC; NbExp=3; IntAct=EBI-5280197, EBI-447544;
CC O75400-2; Q9H7X0: NAA60; NbExp=3; IntAct=EBI-5280197, EBI-12260336;
CC O75400-2; Q6ZUT1: NKAPD1; NbExp=3; IntAct=EBI-5280197, EBI-3920396;
CC O75400-2; Q8NFH3: NUP43; NbExp=3; IntAct=EBI-5280197, EBI-1059321;
CC O75400-2; Q6N063-2: OGFOD2; NbExp=3; IntAct=EBI-5280197, EBI-22006224;
CC O75400-2; Q6GQQ9-2: OTUD7B; NbExp=3; IntAct=EBI-5280197, EBI-25830200;
CC O75400-2; Q99447: PCYT2; NbExp=3; IntAct=EBI-5280197, EBI-750317;
CC O75400-2; P27815-4: PDE4A; NbExp=3; IntAct=EBI-5280197, EBI-12080840;
CC O75400-2; O15534: PER1; NbExp=3; IntAct=EBI-5280197, EBI-2557276;
CC O75400-2; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-5280197, EBI-79165;
CC O75400-2; P48739: PITPNB; NbExp=3; IntAct=EBI-5280197, EBI-1047143;
CC O75400-2; O60664: PLIN3; NbExp=3; IntAct=EBI-5280197, EBI-725795;
CC O75400-2; Q14181: POLA2; NbExp=3; IntAct=EBI-5280197, EBI-712752;
CC O75400-2; P36954: POLR2I; NbExp=3; IntAct=EBI-5280197, EBI-395202;
CC O75400-2; P02775: PPBP; NbExp=3; IntAct=EBI-5280197, EBI-718973;
CC O75400-2; Q6ZMI0-5: PPP1R21; NbExp=3; IntAct=EBI-5280197, EBI-25835994;
CC O75400-2; P54619: PRKAG1; NbExp=3; IntAct=EBI-5280197, EBI-1181439;
CC O75400-2; P23942: PRPH2; NbExp=3; IntAct=EBI-5280197, EBI-25836834;
CC O75400-2; P29074: PTPN4; NbExp=3; IntAct=EBI-5280197, EBI-710431;
CC O75400-2; Q5R372-9: RABGAP1L; NbExp=3; IntAct=EBI-5280197, EBI-10699389;
CC O75400-2; Q14498: RBM39; NbExp=6; IntAct=EBI-5280197, EBI-395290;
CC O75400-2; Q04206: RELA; NbExp=3; IntAct=EBI-5280197, EBI-73886;
CC O75400-2; Q15382: RHEB; NbExp=3; IntAct=EBI-5280197, EBI-1055287;
CC O75400-2; Q8N5U6: RNF10; NbExp=3; IntAct=EBI-5280197, EBI-714023;
CC O75400-2; Q96IZ7: RSRC1; NbExp=3; IntAct=EBI-5280197, EBI-712189;
CC O75400-2; O15126: SCAMP1; NbExp=3; IntAct=EBI-5280197, EBI-954338;
CC O75400-2; P22307-3: SCP2; NbExp=3; IntAct=EBI-5280197, EBI-25834804;
CC O75400-2; O00560: SDCBP; NbExp=3; IntAct=EBI-5280197, EBI-727004;
CC O75400-2; Q9H190: SDCBP2; NbExp=6; IntAct=EBI-5280197, EBI-742426;
CC O75400-2; Q9BRK5: SDF4; NbExp=3; IntAct=EBI-5280197, EBI-1389808;
CC O75400-2; Q9NTN9-3: SEMA4G; NbExp=3; IntAct=EBI-5280197, EBI-9089805;
CC O75400-2; Q7L8J4: SH3BP5L; NbExp=3; IntAct=EBI-5280197, EBI-747389;
CC O75400-2; Q9BZQ2: SHCBP1L; NbExp=3; IntAct=EBI-5280197, EBI-10818532;
CC O75400-2; O60902-3: SHOX2; NbExp=3; IntAct=EBI-5280197, EBI-9092164;
CC O75400-2; Q8IYM2: SLFN12; NbExp=3; IntAct=EBI-5280197, EBI-2822550;
CC O75400-2; Q86US8: SMG6; NbExp=3; IntAct=EBI-5280197, EBI-3232100;
CC O75400-2; Q96EX1: SMIM12; NbExp=3; IntAct=EBI-5280197, EBI-2874543;
CC O75400-2; P37840: SNCA; NbExp=3; IntAct=EBI-5280197, EBI-985879;
CC O75400-2; Q96H20: SNF8; NbExp=3; IntAct=EBI-5280197, EBI-747719;
CC O75400-2; Q13573: SNW1; NbExp=3; IntAct=EBI-5280197, EBI-632715;
CC O75400-2; Q496A3: SPATS1; NbExp=3; IntAct=EBI-5280197, EBI-3923692;
CC O75400-2; Q9C004: SPRY4; NbExp=3; IntAct=EBI-5280197, EBI-354861;
CC O75400-2; Q5W111-2: SPRYD7; NbExp=3; IntAct=EBI-5280197, EBI-12408727;
CC O75400-2; Q8WXA9: SREK1; NbExp=3; IntAct=EBI-5280197, EBI-1044237;
CC O75400-2; Q8N9Q2: SREK1IP1; NbExp=3; IntAct=EBI-5280197, EBI-10268630;
CC O75400-2; Q92797-2: SYMPK; NbExp=3; IntAct=EBI-5280197, EBI-21560407;
CC O75400-2; O15273: TCAP; NbExp=3; IntAct=EBI-5280197, EBI-954089;
CC O75400-2; Q86WV5: TEN1; NbExp=3; IntAct=EBI-5280197, EBI-2562799;
CC O75400-2; P22735: TGM1; NbExp=3; IntAct=EBI-5280197, EBI-2562368;
CC O75400-2; O43548: TGM5; NbExp=3; IntAct=EBI-5280197, EBI-12027348;
CC O75400-2; Q9UIK5-2: TMEFF2; NbExp=3; IntAct=EBI-5280197, EBI-25835153;
CC O75400-2; Q8WVE6-2: TMEM171; NbExp=3; IntAct=EBI-5280197, EBI-25874374;
CC O75400-2; Q12888: TP53BP1; NbExp=3; IntAct=EBI-5280197, EBI-396540;
CC O75400-2; Q9H313-4: TTYH1; NbExp=3; IntAct=EBI-5280197, EBI-17671298;
CC O75400-2; Q9BQE3: TUBA1C; NbExp=3; IntAct=EBI-5280197, EBI-1103245;
CC O75400-2; P49459: UBE2A; NbExp=3; IntAct=EBI-5280197, EBI-2339348;
CC O75400-2; P62253: UBE2G1; NbExp=3; IntAct=EBI-5280197, EBI-2340619;
CC O75400-2; Q9NX94: WBP1L; NbExp=3; IntAct=EBI-5280197, EBI-10316321;
CC O75400-2; O43829: ZBTB14; NbExp=3; IntAct=EBI-5280197, EBI-10176632;
CC O75400-2; Q8IWT0-2: ZBTB8OS; NbExp=3; IntAct=EBI-5280197, EBI-12956041;
CC O75400-2; Q96LX8: ZNF597; NbExp=3; IntAct=EBI-5280197, EBI-9091553;
CC O75400-2; Q3KNS6-3: ZNF829; NbExp=3; IntAct=EBI-5280197, EBI-18036029;
CC O75400-2; B7Z3E8; NbExp=3; IntAct=EBI-5280197, EBI-25831617;
CC O75400-2; Q86V28; NbExp=3; IntAct=EBI-5280197, EBI-10259496;
CC -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000250}. Nucleus matrix
CC {ECO:0000269|PubMed:16391387}. Note=Colocalizes with AKAP8L in the
CC nuclear matrix. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=O75400-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O75400-2; Sequence=VSP_040781, VSP_008047;
CC Name=3;
CC IsoId=O75400-3; Sequence=VSP_008048;
CC Name=5;
CC IsoId=O75400-5; Sequence=VSP_040781, VSP_008047, VSP_040782,
CC VSP_040783;
CC -!- TISSUE SPECIFICITY: Expressed in the brain cortex (at protein level).
CC Widely expressed. {ECO:0000269|PubMed:16391387,
CC ECO:0000269|PubMed:9700202}.
CC -!- DOMAIN: The WW domains are essential for localization to nuclear
CC speckles. {ECO:0000250}.
CC -!- MISCELLANEOUS: [Isoform 5]: Probable target of nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the PRPF40 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC27501.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAC27502.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAC27506.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAD42862.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAF36145.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAH11788.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence starting in position 409.; Evidence={ECO:0000305};
CC Sequence=BAA91277.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB15016.1; Type=Miscellaneous discrepancy; Evidence={ECO:0000305};
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DR EMBL; AC012443; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC079344; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK000592; BAA91277.1; ALT_INIT; mRNA.
DR EMBL; AK024810; BAB15016.1; ALT_SEQ; mRNA.
DR EMBL; AF049523; AAC27501.1; ALT_INIT; mRNA.
DR EMBL; AF049524; AAC27502.1; ALT_INIT; mRNA.
DR EMBL; AF049528; AAC27506.1; ALT_INIT; mRNA.
DR EMBL; BC011788; AAH11788.1; ALT_SEQ; mRNA.
DR EMBL; BC027178; AAH27178.1; -; mRNA.
DR EMBL; U70667; AAB93495.1; -; mRNA.
DR EMBL; AF155096; AAD42862.1; ALT_FRAME; mRNA.
DR EMBL; AF151059; AAF36145.1; ALT_FRAME; mRNA.
DR CCDS; CCDS46430.1; -. [O75400-2]
DR RefSeq; NP_060362.3; NM_017892.3. [O75400-2]
DR PDB; 1UZC; NMR; -; A=381-450.
DR PDB; 1YWI; NMR; -; A=142-173.
DR PDB; 1YWJ; NMR; -; A=142-173.
DR PDB; 1ZR7; NMR; -; A=146-173.
DR PDB; 2CQN; NMR; -; A=743-806.
DR PDB; 2DYF; NMR; -; A=146-173.
DR PDB; 2KZG; NMR; -; A=381-450.
DR PDB; 2L5F; NMR; -; A=133-220.
DR PDB; 2L9V; NMR; -; A=381-450.
DR PDB; 2LKS; NMR; -; A=391-439.
DR PDBsum; 1UZC; -.
DR PDBsum; 1YWI; -.
DR PDBsum; 1YWJ; -.
DR PDBsum; 1ZR7; -.
DR PDBsum; 2CQN; -.
DR PDBsum; 2DYF; -.
DR PDBsum; 2KZG; -.
DR PDBsum; 2L5F; -.
DR PDBsum; 2L9V; -.
DR PDBsum; 2LKS; -.
DR AlphaFoldDB; O75400; -.
DR BMRB; O75400; -.
DR SMR; O75400; -.
DR BioGRID; 120792; 349.
DR CORUM; O75400; -.
DR IntAct; O75400; 250.
DR MINT; O75400; -.
DR STRING; 9606.ENSP00000386458; -.
DR MoonDB; O75400; Predicted.
DR GlyGen; O75400; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O75400; -.
DR PhosphoSitePlus; O75400; -.
DR SwissPalm; O75400; -.
DR BioMuta; PRPF40A; -.
DR EPD; O75400; -.
DR jPOST; O75400; -.
DR MassIVE; O75400; -.
DR MaxQB; O75400; -.
DR PaxDb; O75400; -.
DR PeptideAtlas; O75400; -.
DR PRIDE; O75400; -.
DR ProteomicsDB; 49972; -. [O75400-1]
DR ProteomicsDB; 49973; -. [O75400-2]
DR ProteomicsDB; 49974; -. [O75400-3]
DR ProteomicsDB; 49975; -. [O75400-5]
DR Antibodypedia; 33687; 93 antibodies from 17 providers.
DR DNASU; 55660; -.
DR Ensembl; ENST00000354363.11; ENSP00000346332.7; ENSG00000196504.19. [O75400-5]
DR GeneID; 55660; -.
DR KEGG; hsa:55660; -.
DR UCSC; uc002tyh.5; human. [O75400-1]
DR CTD; 55660; -.
DR DisGeNET; 55660; -.
DR GeneCards; PRPF40A; -.
DR HGNC; HGNC:16463; PRPF40A.
DR HPA; ENSG00000196504; Low tissue specificity.
DR MIM; 612941; gene.
DR neXtProt; NX_O75400; -.
DR OpenTargets; ENSG00000196504; -.
DR PharmGKB; PA28195; -.
DR eggNOG; KOG0152; Eukaryota.
DR GeneTree; ENSGT00930000150980; -.
DR HOGENOM; CLU_005825_0_0_1; -.
DR InParanoid; O75400; -.
DR OrthoDB; 1112854at2759; -.
DR PhylomeDB; O75400; -.
DR TreeFam; TF318732; -.
DR PathwayCommons; O75400; -.
DR Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
DR SignaLink; O75400; -.
DR BioGRID-ORCS; 55660; 733 hits in 1084 CRISPR screens.
DR ChiTaRS; PRPF40A; human.
DR EvolutionaryTrace; O75400; -.
DR GeneWiki; PRPF40A; -.
DR GenomeRNAi; 55660; -.
DR Pharos; O75400; Tbio.
DR PRO; PR:O75400; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; O75400; protein.
DR Bgee; ENSG00000196504; Expressed in secondary oocyte and 213 other tissues.
DR ExpressionAtlas; O75400; baseline and differential.
DR Genevisible; O75400; HS.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0016363; C:nuclear matrix; IDA:UniProtKB.
DR GO; GO:0016607; C:nuclear speck; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005685; C:U1 snRNP; IBA:GO_Central.
DR GO; GO:0071004; C:U2-type prespliceosome; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0016477; P:cell migration; IMP:UniProtKB.
DR GO; GO:0007010; P:cytoskeleton organization; IMP:UniProtKB.
DR GO; GO:0045292; P:mRNA cis splicing, via spliceosome; IEA:InterPro.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central.
DR GO; GO:0008360; P:regulation of cell shape; IMP:UniProtKB.
DR GO; GO:0032465; P:regulation of cytokinesis; IMP:UniProtKB.
DR CDD; cd00201; WW; 2.
DR Gene3D; 1.10.10.440; -; 5.
DR InterPro; IPR002713; FF_domain.
DR InterPro; IPR036517; FF_domain_sf.
DR InterPro; IPR039726; Prp40-like.
DR InterPro; IPR001202; WW_dom.
DR InterPro; IPR036020; WW_dom_sf.
DR PANTHER; PTHR11864; PTHR11864; 1.
DR Pfam; PF01846; FF; 5.
DR Pfam; PF00397; WW; 2.
DR SMART; SM00441; FF; 5.
DR SMART; SM00456; WW; 2.
DR SUPFAM; SSF51045; SSF51045; 2.
DR SUPFAM; SSF81698; SSF81698; 5.
DR PROSITE; PS51676; FF; 6.
DR PROSITE; PS01159; WW_DOMAIN_1; 2.
DR PROSITE; PS50020; WW_DOMAIN_2; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cell cycle; Cell division;
KW Isopeptide bond; Methylation; mRNA processing; mRNA splicing; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Ubl conjugation.
FT CHAIN 1..957
FT /note="Pre-mRNA-processing factor 40 homolog A"
FT /id="PRO_0000076085"
FT DOMAIN 140..173
FT /note="WW 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT DOMAIN 181..214
FT /note="WW 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT DOMAIN 393..447
FT /note="FF 1"
FT DOMAIN 460..514
FT /note="FF 2"
FT DOMAIN 527..587
FT /note="FF 3"
FT DOMAIN 607..667
FT /note="FF 4"
FT DOMAIN 672..727
FT /note="FF 5"
FT DOMAIN 742..799
FT /note="FF 6"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 243..263
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 337..386
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 803..957
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 249..263
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 337..367
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 368..386
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 807..827
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 828..866
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 867..881
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 882..927
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 937..957
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 9
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9R1C7"
FT MOD_RES 34
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 151
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 196
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 345
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 373
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 723
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 787
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 883
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 885
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 888
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 932
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 933
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692"
FT MOD_RES 935
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 938
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT CROSSLNK 191
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 241
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 375
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 376
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1
FT /note="M -> MCSGSGRRRSSLSPTM (in isoform 2 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:9700202"
FT /id="VSP_040781"
FT VAR_SEQ 14..55
FT /note="Missing (in isoform 2 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:9700202"
FT /id="VSP_008047"
FT VAR_SEQ 127..128
FT /note="PG -> LN (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_040782"
FT VAR_SEQ 129..957
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_040783"
FT VAR_SEQ 220..237
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_008048"
FT CONFLICT 372..373
FT /note="FT -> LL (in Ref. 5; AAB93495)"
FT /evidence="ECO:0000305"
FT CONFLICT 433
FT /note="K -> N (in Ref. 3; AAC27501/AAC27506)"
FT /evidence="ECO:0000305"
FT CONFLICT 787
FT /note="S -> P (in Ref. 1; BAA91277)"
FT /evidence="ECO:0000305"
FT STRAND 136..138
FT /evidence="ECO:0007829|PDB:2L5F"
FT TURN 142..145
FT /evidence="ECO:0007829|PDB:2L5F"
FT STRAND 146..151
FT /evidence="ECO:0007829|PDB:1YWI"
FT TURN 152..154
FT /evidence="ECO:0007829|PDB:1YWI"
FT STRAND 155..160
FT /evidence="ECO:0007829|PDB:1YWI"
FT TURN 161..164
FT /evidence="ECO:0007829|PDB:1YWI"
FT STRAND 165..169
FT /evidence="ECO:0007829|PDB:1YWI"
FT HELIX 172..174
FT /evidence="ECO:0007829|PDB:2L5F"
FT HELIX 177..183
FT /evidence="ECO:0007829|PDB:2L5F"
FT STRAND 186..191
FT /evidence="ECO:0007829|PDB:2L5F"
FT STRAND 197..201
FT /evidence="ECO:0007829|PDB:2L5F"
FT TURN 202..205
FT /evidence="ECO:0007829|PDB:2L5F"
FT STRAND 206..209
FT /evidence="ECO:0007829|PDB:2L5F"
FT HELIX 213..216
FT /evidence="ECO:0007829|PDB:2L5F"
FT STRAND 218..220
FT /evidence="ECO:0007829|PDB:2L5F"
FT HELIX 393..406
FT /evidence="ECO:0007829|PDB:1UZC"
FT STRAND 411..413
FT /evidence="ECO:0007829|PDB:2LKS"
FT HELIX 415..423
FT /evidence="ECO:0007829|PDB:1UZC"
FT HELIX 426..430
FT /evidence="ECO:0007829|PDB:1UZC"
FT HELIX 434..447
FT /evidence="ECO:0007829|PDB:1UZC"
FT HELIX 743..755
FT /evidence="ECO:0007829|PDB:2CQN"
FT HELIX 767..774
FT /evidence="ECO:0007829|PDB:2CQN"
FT HELIX 778..781
FT /evidence="ECO:0007829|PDB:2CQN"
FT HELIX 786..804
FT /evidence="ECO:0007829|PDB:2CQN"
FT MOD_RES O75400-2:17
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES O75400-2:24
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES O75400-2:47
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES O75400-5:17
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES O75400-5:24
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES O75400-5:47
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
SQ SEQUENCE 957 AA; 108805 MW; 8874D0C1CE1FCDAF CRC64;
MRPGTGAERG GLMVSEMESH PPSQGPGDGE RRLSGSSLCS GSWVSADGFL RRRPSMGHPG
MHYAPMGMHP MGQRANMPPV PHGMMPQMMP PMGGPPMGQM PGMMSSVMPG MMMSHMSQAS
MQPALPPGVN SMDVAAGTAS GAKSMWTEHK SPDGRTYYYN TETKQSTWEK PDDLKTPAEQ
LLSKCPWKEY KSDSGKPYYY NSQTKESRWA KPKELEDLEG YQNTIVAGSL ITKSNLHAMI
KAEESSKQEE CTTTSTAPVP TTEIPTTMST MAAAEAAAAV VAAAAAAAAA AAAANANAST
SASNTVSGTV PVVPEPEVTS IVATVVDNEN TVTISTEEQA QLTSTPAIQD QSVEVSSNTG
EETSKQETVA DFTPKKEEEE SQPAKKTYTW NTKEEAKQAF KELLKEKRVP SNASWEQAMK
MIINDPRYSA LAKLSEKKQA FNAYKVQTEK EEKEEARSKY KEAKESFQRF LENHEKMTST
TRYKKAEQMF GEMEVWNAIS ERDRLEIYED VLFFLSKKEK EQAKQLRKRN WEALKNILDN
MANVTYSTTW SEAQQYLMDN PTFAEDEELQ NMDKEDALIC FEEHIRALEK EEEEEKQKSL
LRERRRQRKN RESFQIFLDE LHEHGQLHSM SSWMELYPTI SSDIRFTNML GQPGSTALDL
FKFYVEDLKA RYHDEKKIIK DILKDKGFVV EVNTTFEDFV AIISSTKRST TLDAGNIKLA
FNSLLEKAEA REREREKEEA RKMKRKESAF KSMLKQAAPP IELDAVWEDI RERFVKEPAF
EDITLESERK RIFKDFMHVL EHECQHHHSK NKKHSKKSKK HHRKRSRSRS GSDSDDDDSH
SKKKRQRSES RSASEHSSSA ESERSYKKSK KHKKKSKKRR HKSDSPESDA EREKDKKEKD
RESEKDRTRQ RSESKHKSPK KKTGKDSGNW DTSGSELSEG ELEKRRRTLL EQLDDDQ
