PAIRB_HUMAN
ID PAIRB_HUMAN Reviewed; 408 AA.
AC Q8NC51; Q5VU19; Q5VU20; Q5VU22; Q8WUH0; Q96SE2; Q9BTY3; Q9BUM4; Q9Y367;
AC Q9Y4S3;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2004, sequence version 2.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=Plasminogen activator inhibitor 1 RNA-binding protein {ECO:0000305};
DE AltName: Full=PAI1 RNA-binding protein 1;
DE Short=PAI-RBP1;
DE AltName: Full=SERPINE1 mRNA-binding protein 1;
GN Name=SERBP1 {ECO:0000312|HGNC:HGNC:17860}; Synonyms=PAIRBP1;
GN ORFNames=CGI-55 {ECO:0000303|PubMed:28695742};
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 3).
RX PubMed=10810093; DOI=10.1101/gr.10.5.703;
RA Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.;
RT "Identification of novel human genes evolutionarily conserved in
RT Caenorhabditis elegans by comparative proteomics.";
RL Genome Res. 10:703-713(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC TISSUE=Brain;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Teratocarcinoma;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 4).
RC TISSUE=Colon, Lung, Placenta, Prostate, and Skin;
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 [7]
RP PROTEIN SEQUENCE OF 40-52; 137-145; 287-294 AND 304-309, AND IDENTIFICATION
RP BY MASS SPECTROMETRY.
RC TISSUE=B-cell lymphoma;
RA Bienvenut W.V.;
RL Submitted (JAN-2004) to UniProtKB.
RN [8]
RP PROTEIN SEQUENCE OF 2-32; 93-103; 146-160; 217-236; 274-286; 304-309 AND
RP 328-364, CLEAVAGE OF INITIATOR METHIONINE, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RA Bienvenut W.V., Waridel P., Quadroni M.;
RL Submitted (MAR-2009) to UniProtKB.
RN [9]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 85-408 (ISOFORM 3).
RA Spiridonov N.A., Wong L., Johnson G.R.;
RT "Homo sapiens CGI-55 protein mRNA.";
RL Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND INTERACTION WITH CHD3.
RX PubMed=12505151; DOI=10.1016/s0014-5793(02)03737-7;
RA Lemos T.A., Passos D.O., Nery F.C., Kobarg J.;
RT "Characterization of a new family of proteins that interact with the C-
RT terminal region of the chromatin-remodeling factor CHD-3.";
RL FEBS Lett. 533:14-20(2003).
RN [11]
RP INTERACTION WITH SERPINE1 MRNA, AND FUNCTION.
RX PubMed=11001948; DOI=10.1074/jbc.m006538200;
RA Heaton J.H., Dlakic W.M., Dlakic M., Gelehrter T.D.;
RT "Identification and cDNA cloning of a novel RNA-binding protein that
RT interacts with the cyclic nucleotide-responsive sequence in the type-1
RT plasminogen activator inhibitor mRNA.";
RL J. Biol. Chem. 276:3341-3347(2001).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Lymphoblast;
RX PubMed=14654843; DOI=10.1038/nature02166;
RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.;
RT "Proteomic characterization of the human centrosome by protein correlation
RT profiling.";
RL Nature 426:570-574(2003).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-237 (ISOFORM 3),
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-231 (ISOFORM 4), AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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 [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17924679; DOI=10.1021/pr070152u;
RA Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
RT "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells
RT and high confident phosphopeptide identification by cross-validation of
RT MS/MS and MS/MS/MS spectra.";
RL J. Proteome Res. 6:4150-4162(2007).
RN [15]
RP INTERACTION WITH TDRD3.
RX PubMed=18632687; DOI=10.1093/hmg/ddn203;
RA Goulet I., Boisvenue S., Mokas S., Mazroui R., Cote J.;
RT "TDRD3, a novel Tudor domain-containing protein, localizes to cytoplasmic
RT stress granules.";
RL Hum. Mol. Genet. 17:3055-3074(2008).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-234; SER-330 AND SER-394,
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-237 AND THR-240 (ISOFORM 3),
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-231 AND THR-234 (ISOFORM 4),
RP 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 [17]
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 [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25; SER-234; SER-392 AND
RP SER-394, AND 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 [19]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-68; LYS-122; LYS-140 AND LYS-211,
RP AND IDENTIFICATION BY MASS 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 [20]
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 [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25; SER-203; SER-205;
RP SER-208; SER-221; SER-234; SER-330 AND SER-392, AND IDENTIFICATION BY MASS
RP 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 [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25; SER-330 AND SER-394, 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 [23]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-216; ARG-364; ARG-367 AND
RP ARG-370, 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 [24]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-102 AND LYS-281, AND
RP IDENTIFICATION BY MASS 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 [25]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-52 AND LYS-228, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25114211; DOI=10.1073/pnas.1413825111;
RA Impens F., Radoshevich L., Cossart P., Ribet D.;
RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by
RT external stimuli.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
RN [26]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-102 AND LYS-228, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
RA Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
RA Vertegaal A.C.;
RT "SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
RL Cell Rep. 10:1778-1791(2015).
RN [27]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-102 AND LYS-228, AND
RP IDENTIFICATION BY MASS 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 [28]
RP CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [29]
RP INTERACTION WITH ZDHHC17.
RX PubMed=28882895; DOI=10.1074/jbc.m117.799650;
RA Lemonidis K., MacLeod R., Baillie G.S., Chamberlain L.H.;
RT "Peptide array based screening reveals a large number of proteins
RT interacting with the ankyrin repeat domain of the zDHHC17 S-
RT acyltransferase.";
RL J. Biol. Chem. 292:17190-17202(2017).
RN [30]
RP SUMOYLATION AT LYS-102; LYS-228 AND LYS-281, MUTAGENESIS OF LYS-102;
RP LYS-228 AND LYS-281, AND SUBCELLULAR LOCATION.
RX PubMed=28695742; DOI=10.1021/acs.jproteome.7b00001;
RA Saito A., Souza E.E., Costa F.C., Meirelles G.V., Goncalves K.A.,
RA Santos M.T., Bressan G.C., McComb M.E., Costello C.E., Whelan S.A.,
RA Kobarg J.;
RT "Human Regulatory Protein Ki-1/57 Is a Target of SUMOylation and Affects
RT PML Nuclear Body Formation.";
RL J. Proteome Res. 16:3147-3157(2017).
RN [31]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-102; LYS-211; LYS-228 AND
RP LYS-281, SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-228 (ISOFORM 3),
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-222 (ISOFORM 4), AND
RP 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).
CC -!- FUNCTION: May play a role in the regulation of mRNA stability. Binds to
CC the 3'-most 134 nt of the SERPINE1/PAI1 mRNA, a region which confers
CC cyclic nucleotide regulation of message decay. Seems to play a role in
CC PML-nuclear bodies formation (PubMed:28695742).
CC {ECO:0000269|PubMed:11001948, ECO:0000269|PubMed:28695742}.
CC -!- SUBUNIT: Interacts with SPIN1 (By similarity). Interacts with CHD3 and
CC TDRD3 (PubMed:12505151, PubMed:18632687). Interacts with ZDHHC17 (via
CC ANK repeats) (PubMed:28882895). {ECO:0000250|UniProtKB:Q9CY58,
CC ECO:0000269|PubMed:12505151, ECO:0000269|PubMed:18632687,
CC ECO:0000269|PubMed:28882895}.
CC -!- INTERACTION:
CC Q8NC51; Q12873: CHD3; NbExp=5; IntAct=EBI-523558, EBI-523590;
CC Q8NC51; P16284: PECAM1; NbExp=3; IntAct=EBI-523558, EBI-716404;
CC Q8NC51; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-523558, EBI-79165;
CC Q8NC51; P50454: SERPINH1; NbExp=3; IntAct=EBI-523558, EBI-350723;
CC Q8NC51; P37173: TGFBR2; NbExp=3; IntAct=EBI-523558, EBI-296151;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12505151,
CC ECO:0000269|PubMed:28695742}. Nucleus {ECO:0000269|PubMed:12505151,
CC ECO:0000269|PubMed:28695742}. Cytoplasm, perinuclear region
CC {ECO:0000269|PubMed:12505151}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q8NC51-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8NC51-2; Sequence=VSP_011630;
CC Name=3;
CC IsoId=Q8NC51-3; Sequence=VSP_011631;
CC Name=4;
CC IsoId=Q8NC51-4; Sequence=VSP_011630, VSP_011631;
CC -!- TISSUE SPECIFICITY: Expressed at high level in the heart, skeletal
CC muscle and kidney, and at low levels in placenta, liver and brain.
CC {ECO:0000269|PubMed:12505151}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to a competing acceptor splice
CC site. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 3]: May be due to a competing acceptor splice
CC site. {ECO:0000305}.
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DR EMBL; AF151813; AAD34050.1; -; mRNA.
DR EMBL; AL080119; CAB45718.1; -; mRNA.
DR EMBL; AK074970; BAC11324.1; -; mRNA.
DR EMBL; CR457383; CAG33664.1; -; mRNA.
DR EMBL; AL590559; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC003049; AAH03049.1; -; mRNA.
DR EMBL; BC008045; AAH08045.1; -; mRNA.
DR EMBL; BC017449; AAH17449.1; -; mRNA.
DR EMBL; BC019273; AAH19273.1; -; mRNA.
DR EMBL; BC020555; AAH20555.1; -; mRNA.
DR EMBL; BC002488; AAH02488.1; -; mRNA.
DR EMBL; BC026916; AAH26916.1; -; mRNA.
DR EMBL; AY032853; AAK51130.1; -; mRNA.
DR CCDS; CCDS30746.1; -. [Q8NC51-1]
DR CCDS; CCDS30747.1; -. [Q8NC51-3]
DR CCDS; CCDS30748.1; -. [Q8NC51-2]
DR CCDS; CCDS639.1; -. [Q8NC51-4]
DR PIR; T12456; T12456.
DR RefSeq; NP_001018077.1; NM_001018067.1. [Q8NC51-1]
DR RefSeq; NP_001018078.1; NM_001018068.1. [Q8NC51-2]
DR RefSeq; NP_001018079.1; NM_001018069.1. [Q8NC51-3]
DR RefSeq; NP_056455.3; NM_015640.3. [Q8NC51-4]
DR PDB; 4V6X; EM; 5.00 A; Ah=1-408.
DR PDB; 6Z6M; EM; 3.10 A; CD=1-408.
DR PDB; 6Z6N; EM; 2.90 A; CD=1-408.
DR PDBsum; 4V6X; -.
DR PDBsum; 6Z6M; -.
DR PDBsum; 6Z6N; -.
DR AlphaFoldDB; Q8NC51; -.
DR BioGRID; 117571; 545.
DR DIP; DIP-33819N; -.
DR IntAct; Q8NC51; 96.
DR MINT; Q8NC51; -.
DR STRING; 9606.ENSP00000360034; -.
DR CarbonylDB; Q8NC51; -.
DR GlyGen; Q8NC51; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q8NC51; -.
DR MetOSite; Q8NC51; -.
DR PhosphoSitePlus; Q8NC51; -.
DR SwissPalm; Q8NC51; -.
DR BioMuta; SERBP1; -.
DR DMDM; 52783206; -.
DR EPD; Q8NC51; -.
DR jPOST; Q8NC51; -.
DR MassIVE; Q8NC51; -.
DR MaxQB; Q8NC51; -.
DR PaxDb; Q8NC51; -.
DR PeptideAtlas; Q8NC51; -.
DR PRIDE; Q8NC51; -.
DR ProteomicsDB; 72850; -. [Q8NC51-1]
DR ProteomicsDB; 72851; -. [Q8NC51-2]
DR ProteomicsDB; 72852; -. [Q8NC51-3]
DR ProteomicsDB; 72853; -. [Q8NC51-4]
DR TopDownProteomics; Q8NC51-1; -. [Q8NC51-1]
DR TopDownProteomics; Q8NC51-2; -. [Q8NC51-2]
DR TopDownProteomics; Q8NC51-3; -. [Q8NC51-3]
DR TopDownProteomics; Q8NC51-4; -. [Q8NC51-4]
DR Antibodypedia; 19619; 389 antibodies from 28 providers.
DR DNASU; 26135; -.
DR Ensembl; ENST00000361219.11; ENSP00000354591.6; ENSG00000142864.15. [Q8NC51-3]
DR Ensembl; ENST00000370990.5; ENSP00000360029.5; ENSG00000142864.15. [Q8NC51-2]
DR Ensembl; ENST00000370994.8; ENSP00000360033.4; ENSG00000142864.15. [Q8NC51-4]
DR Ensembl; ENST00000370995.6; ENSP00000360034.2; ENSG00000142864.15. [Q8NC51-1]
DR GeneID; 26135; -.
DR KEGG; hsa:26135; -.
DR MANE-Select; ENST00000361219.11; ENSP00000354591.6; NM_001018069.2; NP_001018079.1. [Q8NC51-3]
DR UCSC; uc001ddv.4; human. [Q8NC51-1]
DR CTD; 26135; -.
DR DisGeNET; 26135; -.
DR GeneCards; SERBP1; -.
DR HGNC; HGNC:17860; SERBP1.
DR HPA; ENSG00000142864; Low tissue specificity.
DR MIM; 607378; gene.
DR neXtProt; NX_Q8NC51; -.
DR OpenTargets; ENSG00000142864; -.
DR PharmGKB; PA413; -.
DR VEuPathDB; HostDB:ENSG00000142864; -.
DR eggNOG; KOG2945; Eukaryota.
DR GeneTree; ENSGT00520000055591; -.
DR HOGENOM; CLU_037366_2_1_1; -.
DR InParanoid; Q8NC51; -.
DR OMA; EEMNGFQ; -.
DR OrthoDB; 1183388at2759; -.
DR PhylomeDB; Q8NC51; -.
DR TreeFam; TF318374; -.
DR PathwayCommons; Q8NC51; -.
DR SignaLink; Q8NC51; -.
DR BioGRID-ORCS; 26135; 286 hits in 1049 CRISPR screens.
DR ChiTaRS; SERBP1; human.
DR GeneWiki; SERBP1; -.
DR GenomeRNAi; 26135; -.
DR Pharos; Q8NC51; Tbio.
DR PRO; PR:Q8NC51; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q8NC51; protein.
DR Bgee; ENSG00000142864; Expressed in skeletal muscle tissue of biceps brachii and 207 other tissues.
DR ExpressionAtlas; Q8NC51; baseline and differential.
DR Genevisible; Q8NC51; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; IDA:HGNC-UCL.
DR GO; GO:0043022; F:ribosome binding; IDA:FlyBase.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0032183; F:SUMO binding; IDA:UniProtKB.
DR GO; GO:0030578; P:PML body organization; IDA:UniProtKB.
DR GO; GO:0043488; P:regulation of mRNA stability; NAS:HGNC-UCL.
DR InterPro; IPR039764; HABP4/SERBP1.
DR InterPro; IPR006861; HABP4_PAIRBP1-bd.
DR InterPro; IPR032381; IHABP4_N.
DR InterPro; IPR027205; SERBP1.
DR PANTHER; PTHR12299; PTHR12299; 1.
DR PANTHER; PTHR12299:SF29; PTHR12299:SF29; 1.
DR Pfam; PF04774; HABP4_PAI-RBP1; 1.
DR Pfam; PF16174; IHABP4_N; 1.
DR SMART; SM01233; HABP4_PAI-RBP1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm;
KW Direct protein sequencing; Isopeptide bond; Methylation; Nucleus;
KW Phosphoprotein; Reference proteome; RNA-binding; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.8, ECO:0007744|PubMed:25944712"
FT CHAIN 2..408
FT /note="Plasminogen activator inhibitor 1 RNA-binding
FT protein"
FT /id="PRO_0000058182"
FT REGION 33..292
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 328..408
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 55..69
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 95..161
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 176..219
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 236..254
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 257..292
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 328..349
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 25
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 52
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9CY58"
FT MOD_RES 68
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 122
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 140
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 165
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9CY58"
FT MOD_RES 188
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9CY58"
FT MOD_RES 197
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6AXS5"
FT MOD_RES 203
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 205
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 208
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 211
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 216
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 221
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 234
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"
FT MOD_RES 329
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9CY58"
FT MOD_RES 330
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 364
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 367
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 370
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 392
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 394
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:24275569"
FT CROSSLNK 52
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0007744|PubMed:25114211"
FT CROSSLNK 102
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000269|PubMed:28695742"
FT CROSSLNK 102
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:25772364,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 211
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 228
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000269|PubMed:28695742,
FT ECO:0007744|PubMed:25114211"
FT CROSSLNK 228
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:25114211,
FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:25772364,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 281
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000269|PubMed:28695742"
FT CROSSLNK 281
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:28112733"
FT VAR_SEQ 203..208
FT /note="Missing (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:11230166,
FT ECO:0000303|PubMed:15489334, ECO:0000303|Ref.4"
FT /id="VSP_011630"
FT VAR_SEQ 233..247
FT /note="Missing (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:10810093,
FT ECO:0000303|PubMed:11230166, ECO:0000303|PubMed:15489334,
FT ECO:0000303|Ref.4, ECO:0000303|Ref.9"
FT /id="VSP_011631"
FT MUTAGEN 102
FT /note="K->R: Not sumoylated; when associated with R-228 and
FT R-281."
FT /evidence="ECO:0000269|PubMed:28695742"
FT MUTAGEN 228
FT /note="K->R: Not sumoylated; when associated with R-102 and
FT R-281."
FT /evidence="ECO:0000269|PubMed:28695742"
FT MUTAGEN 281
FT /note="K->R: Not sumoylated; when associated with R-102 and
FT R-228."
FT /evidence="ECO:0000269|PubMed:28695742"
FT CONFLICT 55
FT /note="A -> T (in Ref. 1; AAD34050)"
FT /evidence="ECO:0000305"
FT CONFLICT 101
FT /note="L -> F (in Ref. 1; AAD34050)"
FT /evidence="ECO:0000305"
FT CONFLICT 312
FT /note="N -> S (in Ref. 3; BAC11324)"
FT /evidence="ECO:0000305"
FT CONFLICT 376
FT /note="R -> C (in Ref. 6; AAH02488)"
FT /evidence="ECO:0000305"
FT MOD_RES Q8NC51-3:237
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648"
FT MOD_RES Q8NC51-3:240
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT CROSSLNK Q8NC51-3:228
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT MOD_RES Q8NC51-4:231
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648"
FT MOD_RES Q8NC51-4:234
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT CROSSLNK Q8NC51-4:222
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
SQ SEQUENCE 408 AA; 44965 MW; 2289992374FA6A96 CRC64;
MPGHLQEGFG CVVTNRFDQL FDDESDPFEV LKAAENKKKE AGGGGVGGPG AKSAAQAAAQ
TNSNAAGKQL RKESQKDRKN PLPPSVGVVD KKEETQPPVA LKKEGIRRVG RRPDQQLQGE
GKIIDRRPER RPPRERRFEK PLEEKGEGGE FSVDRPIIDR PIRGRGGLGR GRGGRGRGMG
RGDGFDSRGK REFDRHSGSD RSSFSHYSGL KHEDKRGGSG SHNWGTVKDE LTESPKYIQK
QISYNYSDLD QSNVTEETPE GEEHHPVADT ENKENEVEEV KEEGPKEMTL DEWKAIQNKD
RAKVEFNIRK PNEGADGQWK KGFVLHKSKS EEAHAEDSVM DHHFRKPAND ITSQLEINFG
DLGRPGRGGR GGRGGRGRGG RPNRGSRTDK SSASAPDVDD PEAFPALA
