Full text data of SERBP1
SERBP1
(PAIRBP1)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Plasminogen activator inhibitor 1 RNA-binding protein (PAI1 RNA-binding protein 1; PAI-RBP1; SERPINE1 mRNA-binding protein 1)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Plasminogen activator inhibitor 1 RNA-binding protein (PAI1 RNA-binding protein 1; PAI-RBP1; SERPINE1 mRNA-binding protein 1)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q8NC51
ID PAIRB_HUMAN Reviewed; 408 AA.
AC Q8NC51; Q5VU19; Q5VU20; Q5VU22; Q8WUH0; Q96SE2; Q9BTY3; Q9BUM4;
read moreAC Q9Y367; Q9Y4S3;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2004, sequence version 2.
DT 22-JAN-2014, entry version 116.
DE RecName: Full=Plasminogen activator inhibitor 1 RNA-binding protein;
DE AltName: Full=PAI1 RNA-binding protein 1;
DE Short=PAI-RBP1;
DE AltName: Full=SERPINE1 mRNA-binding protein 1;
GN Name=SERBP1; Synonyms=PAIRBP1; ORFNames=CGI-55;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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.,
RA Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N.,
RA Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D.,
RA Wambutt R., Korn B., Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and
RT analysis of 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA 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.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA 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.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA 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
RT project: 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 MASS
RP 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
RP AND 328-364, CLEAVAGE OF INITIATOR METHIONINE, LACK OF N-TERMINAL
RP ACETYLATION, AND MASS 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
RT C-terminal region of the chromatin-remodeling factor CHD-3.";
RL FEBS Lett. 533:14-20(2003).
RN [11]
RP INTERACTION WITH SERPINE1 MRNA.
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-237 (ISOFORM 3),
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-231 (ISOFORM 4), AND
RP MASS SPECTROMETRY.
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.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [13]
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
RT cells and high confident phosphopeptide identification by cross-
RT validation of MS/MS and MS/MS/MS spectra.";
RL J. Proteome Res. 6:4150-4162(2007).
RN [14]
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
RT cytoplasmic stress granules.";
RL Hum. Mol. Genet. 17:3055-3074(2008).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-234; SER-330 AND
RP SER-394, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-237 AND THR-240
RP (ISOFORM 3), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-231 AND
RP THR-234 (ISOFORM 4), AND MASS SPECTROMETRY.
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 [16]
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.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25; SER-234; SER-392 AND
RP SER-394, AND MASS SPECTROMETRY.
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 [18]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-68; LYS-122; LYS-140 AND
RP LYS-211, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., 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 [19]
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.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: May play a role in the regulation of mRNA stability.
CC Binds to the 3'-most 134 nt of the SERPINE1/PAI1 mRNA, a region
CC which confers cyclic nucleotide regulation of message decay.
CC -!- SUBUNIT: Interacts with CHD3 and TDRD3.
CC -!- INTERACTION:
CC Q12873:CHD3; NbExp=5; IntAct=EBI-523558, EBI-523590;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cytoplasm, perinuclear
CC region. Note=Also found in perinuclear regions.
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 Note=May be due to a competing acceptor splice site;
CC Name=3;
CC IsoId=Q8NC51-3; Sequence=VSP_011631;
CC Note=May be due to a competing acceptor splice site. Contains a
CC phosphoserine at position 237. Contains a phosphothreonine at
CC position 240;
CC Name=4;
CC IsoId=Q8NC51-4; Sequence=VSP_011630, VSP_011631;
CC Note=Contains a phosphoserine at position 231. Contains a
CC phosphothreonine at position 234;
CC -!- TISSUE SPECIFICITY: Expressed at high level in the heart, skeletal
CC muscle and kidney, and at low levels in placenta, liver and brain.
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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; CAH73323.1; -; Genomic_DNA.
DR EMBL; AL590559; CAH73324.1; -; Genomic_DNA.
DR EMBL; AL590559; CAH73326.1; -; 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 PIR; T12456; T12456.
DR RefSeq; NP_001018077.1; NM_001018067.1.
DR RefSeq; NP_001018078.1; NM_001018068.1.
DR RefSeq; NP_001018079.1; NM_001018069.1.
DR RefSeq; NP_056455.3; NM_015640.3.
DR UniGene; Hs.530412; -.
DR PDB; 3J3A; EM; 5.00 A; h=1-408.
DR PDBsum; 3J3A; -.
DR ProteinModelPortal; Q8NC51; -.
DR DIP; DIP-33819N; -.
DR IntAct; Q8NC51; 31.
DR MINT; MINT-1373976; -.
DR PhosphoSite; Q8NC51; -.
DR DMDM; 52783206; -.
DR PaxDb; Q8NC51; -.
DR PRIDE; Q8NC51; -.
DR DNASU; 26135; -.
DR Ensembl; ENST00000361219; ENSP00000354591; ENSG00000142864.
DR Ensembl; ENST00000370990; ENSP00000360029; ENSG00000142864.
DR Ensembl; ENST00000370994; ENSP00000360033; ENSG00000142864.
DR Ensembl; ENST00000370995; ENSP00000360034; ENSG00000142864.
DR GeneID; 26135; -.
DR KEGG; hsa:26135; -.
DR UCSC; uc001ddv.3; human.
DR CTD; 26135; -.
DR GeneCards; GC01M067873; -.
DR HGNC; HGNC:17860; SERBP1.
DR HPA; CAB026297; -.
DR HPA; HPA020559; -.
DR MIM; 607378; gene.
DR neXtProt; NX_Q8NC51; -.
DR PharmGKB; PA413; -.
DR eggNOG; NOG321910; -.
DR HOVERGEN; HBG056357; -.
DR InParanoid; Q8NC51; -.
DR KO; K13199; -.
DR OMA; PNRGIRT; -.
DR OrthoDB; EOG71P2BG; -.
DR PhylomeDB; Q8NC51; -.
DR ChiTaRS; SERBP1; human.
DR GeneWiki; SERBP1; -.
DR GenomeRNAi; 26135; -.
DR NextBio; 48165; -.
DR PRO; PR:Q8NC51; -.
DR ArrayExpress; Q8NC51; -.
DR Bgee; Q8NC51; -.
DR CleanEx; HS_SERBP1; -.
DR Genevestigator; Q8NC51; -.
DR GO; GO:0005737; C:cytoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; IDA:HGNC.
DR GO; GO:0043488; P:regulation of mRNA stability; NAS:HGNC.
DR InterPro; IPR006861; HABP4_PAIRBP1-bd.
DR InterPro; IPR027205; SERBP1.
DR PANTHER; PTHR12299:SF8; PTHR12299:SF8; 1.
DR Pfam; PF04774; HABP4_PAI-RBP1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Complete proteome;
KW Cytoplasm; Direct protein sequencing; Nucleus; Phosphoprotein;
KW Reference proteome; RNA-binding.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 408 Plasminogen activator inhibitor 1 RNA-
FT binding protein.
FT /FTId=PRO_0000058182.
FT MOD_RES 25 25 Phosphoserine.
FT MOD_RES 68 68 N6-acetyllysine.
FT MOD_RES 122 122 N6-acetyllysine.
FT MOD_RES 140 140 N6-acetyllysine.
FT MOD_RES 211 211 N6-acetyllysine.
FT MOD_RES 234 234 Phosphoserine.
FT MOD_RES 330 330 Phosphoserine.
FT MOD_RES 392 392 Phosphoserine.
FT MOD_RES 394 394 Phosphoserine.
FT VAR_SEQ 203 208 Missing (in isoform 2 and isoform 4).
FT /FTId=VSP_011630.
FT VAR_SEQ 233 247 Missing (in isoform 3 and isoform 4).
FT /FTId=VSP_011631.
FT CONFLICT 55 55 A -> T (in Ref. 1; AAD34050).
FT CONFLICT 101 101 L -> F (in Ref. 1; AAD34050).
FT CONFLICT 312 312 N -> S (in Ref. 3; BAC11324).
FT CONFLICT 376 376 R -> C (in Ref. 6; AAH02488).
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
//
ID PAIRB_HUMAN Reviewed; 408 AA.
AC Q8NC51; Q5VU19; Q5VU20; Q5VU22; Q8WUH0; Q96SE2; Q9BTY3; Q9BUM4;
read moreAC Q9Y367; Q9Y4S3;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2004, sequence version 2.
DT 22-JAN-2014, entry version 116.
DE RecName: Full=Plasminogen activator inhibitor 1 RNA-binding protein;
DE AltName: Full=PAI1 RNA-binding protein 1;
DE Short=PAI-RBP1;
DE AltName: Full=SERPINE1 mRNA-binding protein 1;
GN Name=SERBP1; Synonyms=PAIRBP1; ORFNames=CGI-55;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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.,
RA Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N.,
RA Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D.,
RA Wambutt R., Korn B., Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and
RT analysis of 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA 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.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA 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.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA 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
RT project: 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 MASS
RP 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
RP AND 328-364, CLEAVAGE OF INITIATOR METHIONINE, LACK OF N-TERMINAL
RP ACETYLATION, AND MASS 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
RT C-terminal region of the chromatin-remodeling factor CHD-3.";
RL FEBS Lett. 533:14-20(2003).
RN [11]
RP INTERACTION WITH SERPINE1 MRNA.
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-237 (ISOFORM 3),
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-231 (ISOFORM 4), AND
RP MASS SPECTROMETRY.
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.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [13]
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
RT cells and high confident phosphopeptide identification by cross-
RT validation of MS/MS and MS/MS/MS spectra.";
RL J. Proteome Res. 6:4150-4162(2007).
RN [14]
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
RT cytoplasmic stress granules.";
RL Hum. Mol. Genet. 17:3055-3074(2008).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-234; SER-330 AND
RP SER-394, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-237 AND THR-240
RP (ISOFORM 3), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-231 AND
RP THR-234 (ISOFORM 4), AND MASS SPECTROMETRY.
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 [16]
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.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25; SER-234; SER-392 AND
RP SER-394, AND MASS SPECTROMETRY.
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 [18]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-68; LYS-122; LYS-140 AND
RP LYS-211, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., 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 [19]
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.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: May play a role in the regulation of mRNA stability.
CC Binds to the 3'-most 134 nt of the SERPINE1/PAI1 mRNA, a region
CC which confers cyclic nucleotide regulation of message decay.
CC -!- SUBUNIT: Interacts with CHD3 and TDRD3.
CC -!- INTERACTION:
CC Q12873:CHD3; NbExp=5; IntAct=EBI-523558, EBI-523590;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cytoplasm, perinuclear
CC region. Note=Also found in perinuclear regions.
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 Note=May be due to a competing acceptor splice site;
CC Name=3;
CC IsoId=Q8NC51-3; Sequence=VSP_011631;
CC Note=May be due to a competing acceptor splice site. Contains a
CC phosphoserine at position 237. Contains a phosphothreonine at
CC position 240;
CC Name=4;
CC IsoId=Q8NC51-4; Sequence=VSP_011630, VSP_011631;
CC Note=Contains a phosphoserine at position 231. Contains a
CC phosphothreonine at position 234;
CC -!- TISSUE SPECIFICITY: Expressed at high level in the heart, skeletal
CC muscle and kidney, and at low levels in placenta, liver and brain.
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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; CAH73323.1; -; Genomic_DNA.
DR EMBL; AL590559; CAH73324.1; -; Genomic_DNA.
DR EMBL; AL590559; CAH73326.1; -; 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 PIR; T12456; T12456.
DR RefSeq; NP_001018077.1; NM_001018067.1.
DR RefSeq; NP_001018078.1; NM_001018068.1.
DR RefSeq; NP_001018079.1; NM_001018069.1.
DR RefSeq; NP_056455.3; NM_015640.3.
DR UniGene; Hs.530412; -.
DR PDB; 3J3A; EM; 5.00 A; h=1-408.
DR PDBsum; 3J3A; -.
DR ProteinModelPortal; Q8NC51; -.
DR DIP; DIP-33819N; -.
DR IntAct; Q8NC51; 31.
DR MINT; MINT-1373976; -.
DR PhosphoSite; Q8NC51; -.
DR DMDM; 52783206; -.
DR PaxDb; Q8NC51; -.
DR PRIDE; Q8NC51; -.
DR DNASU; 26135; -.
DR Ensembl; ENST00000361219; ENSP00000354591; ENSG00000142864.
DR Ensembl; ENST00000370990; ENSP00000360029; ENSG00000142864.
DR Ensembl; ENST00000370994; ENSP00000360033; ENSG00000142864.
DR Ensembl; ENST00000370995; ENSP00000360034; ENSG00000142864.
DR GeneID; 26135; -.
DR KEGG; hsa:26135; -.
DR UCSC; uc001ddv.3; human.
DR CTD; 26135; -.
DR GeneCards; GC01M067873; -.
DR HGNC; HGNC:17860; SERBP1.
DR HPA; CAB026297; -.
DR HPA; HPA020559; -.
DR MIM; 607378; gene.
DR neXtProt; NX_Q8NC51; -.
DR PharmGKB; PA413; -.
DR eggNOG; NOG321910; -.
DR HOVERGEN; HBG056357; -.
DR InParanoid; Q8NC51; -.
DR KO; K13199; -.
DR OMA; PNRGIRT; -.
DR OrthoDB; EOG71P2BG; -.
DR PhylomeDB; Q8NC51; -.
DR ChiTaRS; SERBP1; human.
DR GeneWiki; SERBP1; -.
DR GenomeRNAi; 26135; -.
DR NextBio; 48165; -.
DR PRO; PR:Q8NC51; -.
DR ArrayExpress; Q8NC51; -.
DR Bgee; Q8NC51; -.
DR CleanEx; HS_SERBP1; -.
DR Genevestigator; Q8NC51; -.
DR GO; GO:0005737; C:cytoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; IDA:HGNC.
DR GO; GO:0043488; P:regulation of mRNA stability; NAS:HGNC.
DR InterPro; IPR006861; HABP4_PAIRBP1-bd.
DR InterPro; IPR027205; SERBP1.
DR PANTHER; PTHR12299:SF8; PTHR12299:SF8; 1.
DR Pfam; PF04774; HABP4_PAI-RBP1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Complete proteome;
KW Cytoplasm; Direct protein sequencing; Nucleus; Phosphoprotein;
KW Reference proteome; RNA-binding.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 408 Plasminogen activator inhibitor 1 RNA-
FT binding protein.
FT /FTId=PRO_0000058182.
FT MOD_RES 25 25 Phosphoserine.
FT MOD_RES 68 68 N6-acetyllysine.
FT MOD_RES 122 122 N6-acetyllysine.
FT MOD_RES 140 140 N6-acetyllysine.
FT MOD_RES 211 211 N6-acetyllysine.
FT MOD_RES 234 234 Phosphoserine.
FT MOD_RES 330 330 Phosphoserine.
FT MOD_RES 392 392 Phosphoserine.
FT MOD_RES 394 394 Phosphoserine.
FT VAR_SEQ 203 208 Missing (in isoform 2 and isoform 4).
FT /FTId=VSP_011630.
FT VAR_SEQ 233 247 Missing (in isoform 3 and isoform 4).
FT /FTId=VSP_011631.
FT CONFLICT 55 55 A -> T (in Ref. 1; AAD34050).
FT CONFLICT 101 101 L -> F (in Ref. 1; AAD34050).
FT CONFLICT 312 312 N -> S (in Ref. 3; BAC11324).
FT CONFLICT 376 376 R -> C (in Ref. 6; AAH02488).
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
//
MIM
607378
*RECORD*
*FIELD* NO
607378
*FIELD* TI
*607378 SERPINE1 mRNA-BINDING PROTEIN 1; SERBP1
;;PAI1 RNA-BINDING PROTEIN 1;;
PAIRBP1
read more*FIELD* TX
CLONING
Heaton et al. (2001) purified Pairbp1 from rat hepatoma cells and
determined that it binds to the cyclic nucleotide-responsive element of
the rat Pai1 gene (173360). Based on homology with the N-terminal amino
acid sequence of the rat protein, they identified a human PAIRBP1 cDNA.
The deduced 387-amino acid human protein does not contain an RNA
recognition motif or a K homology domain, but it has other motifs
frequently found in RNA-binding proteins, notably an RGG box, an RG-rich
region, and an arg-rich region. It also contains a putative protein
kinase A (see 601639) phosphorylation site at ser74. PAIRBP1 shares
several blocks of conserved sequence with proteins from Arabidopsis,
Drosophila, chicken, mouse, and rat.
GENE FUNCTION
Using RNA electrophoretic mobility shift assay and ultraviolet
cross-linking experiments, Heaton et al. (2001) determined that
recombinant PAIRBP1 binds to the cyclic nucleotide-responsive element of
rat Pai1 in a concentration-dependent manner. By mutation analysis, they
determined that PAIRBP1 interacts primarily with the adenine-rich region
of the response element.
*FIELD* RF
1. Heaton, J. H.; Dlakic, W. M.; Dlakic, M.; Gelehrter, T. D.: Identification
and cDNA cloning of a novel RNA-binding protein that interacts with
the cyclic nucleotide-responsive sequence in the type-1 plasminogen
activator inhibitor mRNA. J. Biol. Chem. 276: 3341-3347, 2001.
*FIELD* CD
Patricia A. Hartz: 11/22/2002
*FIELD* ED
wwang: 03/30/2010
mgross: 11/22/2002
*RECORD*
*FIELD* NO
607378
*FIELD* TI
*607378 SERPINE1 mRNA-BINDING PROTEIN 1; SERBP1
;;PAI1 RNA-BINDING PROTEIN 1;;
PAIRBP1
read more*FIELD* TX
CLONING
Heaton et al. (2001) purified Pairbp1 from rat hepatoma cells and
determined that it binds to the cyclic nucleotide-responsive element of
the rat Pai1 gene (173360). Based on homology with the N-terminal amino
acid sequence of the rat protein, they identified a human PAIRBP1 cDNA.
The deduced 387-amino acid human protein does not contain an RNA
recognition motif or a K homology domain, but it has other motifs
frequently found in RNA-binding proteins, notably an RGG box, an RG-rich
region, and an arg-rich region. It also contains a putative protein
kinase A (see 601639) phosphorylation site at ser74. PAIRBP1 shares
several blocks of conserved sequence with proteins from Arabidopsis,
Drosophila, chicken, mouse, and rat.
GENE FUNCTION
Using RNA electrophoretic mobility shift assay and ultraviolet
cross-linking experiments, Heaton et al. (2001) determined that
recombinant PAIRBP1 binds to the cyclic nucleotide-responsive element of
rat Pai1 in a concentration-dependent manner. By mutation analysis, they
determined that PAIRBP1 interacts primarily with the adenine-rich region
of the response element.
*FIELD* RF
1. Heaton, J. H.; Dlakic, W. M.; Dlakic, M.; Gelehrter, T. D.: Identification
and cDNA cloning of a novel RNA-binding protein that interacts with
the cyclic nucleotide-responsive sequence in the type-1 plasminogen
activator inhibitor mRNA. J. Biol. Chem. 276: 3341-3347, 2001.
*FIELD* CD
Patricia A. Hartz: 11/22/2002
*FIELD* ED
wwang: 03/30/2010
mgross: 11/22/2002