ID PR38B_HUMAN Reviewed; 546 AA. AC Q5VTL8; Q05DD6; Q32Q58; Q5VTL9; Q6PK39; Q7Z6E2; Q86WF3; Q8IWG9; AC Q9NW40; DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot. DT 07-DEC-2004, sequence version 1. DT 05-OCT-2010, entry version 54. DE RecName: Full=Pre-mRNA-splicing factor 38B; DE AltName: Full=Sarcoma antigen NY-SAR-27; GN Name=PRPF38B; 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 1). 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 [2] 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Lung, Muscle, Skin, and Testis; 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 [4] RP NUCLEOTIDE SEQUENCE [MRNA] OF 402-546 (ISOFORM 1). RX MEDLINE=22506365; PubMed=12601173; DOI=10.1073/pnas.0437972100; RA Lee S.-Y., Obata Y., Yoshida M., Stockert E., Williamson B., RA Jungbluth A.A., Chen Y.-T., Old L.J., Scanlan M.J.; RT "Immunomic analysis of human sarcoma."; RL Proc. Natl. Acad. Sci. U.S.A. 100:2651-2656(2003). RN [5] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-527 AND SER-529, AND RP MASS SPECTROMETRY. RC TISSUE=Colon adenocarcinoma; RX PubMed=16083285; DOI=10.1021/pr050048h; RA Kim J.-E., Tannenbaum S.R., White F.M.; RT "Global phosphoproteome of HT-29 human colon adenocarcinoma cells."; RL J. Proteome Res. 4:1339-1346(2005). RN [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-266; SER-268; SER-272; RP SER-290; SER-318; SER-320; SER-385; SER-527 AND SER-529, AND MASS RP 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 [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-527 AND SER-529, AND RP MASS SPECTROMETRY. RC TISSUE=Cervix carcinoma; RX PubMed=16964243; DOI=10.1038/nbt1240; RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; RT "A probability-based approach for high-throughput protein RT phosphorylation analysis and site localization."; RL Nat. Biotechnol. 24:1285-1292(2006). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-268, AND MASS RP SPECTROMETRY. 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 [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-527 AND SER-534, AND RP MASS SPECTROMETRY. RC TISSUE=Embryonic kidney; RX PubMed=17525332; DOI=10.1126/science.1140321; RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, RA Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., RA Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.; RT "ATM and ATR substrate analysis reveals extensive protein networks RT responsive to DNA damage."; RL Science 316:1160-1166(2007). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-527; SER-529 AND RP SER-534, 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 [11] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE RP SCALE ANALYSIS] AT SER-5, AND MASS SPECTROMETRY. RC TISSUE=Embryonic kidney; 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 [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-529, AND MASS RP 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 [13] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-227, AND MASS SPECTROMETRY. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., 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). CC -!- FUNCTION: May be required for pre-mRNA splicing (Potential). CC -!- SUBCELLULAR LOCATION: Nucleus (Potential). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q5VTL8-1; Sequence=Displayed; CC Name=2; CC IsoId=Q5VTL8-2; Sequence=VSP_025408, VSP_025409; CC -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR. CC -!- SIMILARITY: Belongs to the PRP38 family. CC -!- SEQUENCE CAUTION: CC Sequence=AAO65168.1; Type=Erroneous initiation; CC Sequence=CAH72070.1; Type=Erroneous gene model prediction; CC Sequence=CAI12934.1; Type=Erroneous gene model prediction; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK001192; BAA91546.1; -; mRNA. DR EMBL; AL591719; CAH72068.1; -; Genomic_DNA. DR EMBL; AL160171; CAH72068.1; JOINED; Genomic_DNA. DR EMBL; AL591719; CAH72069.1; -; Genomic_DNA. DR EMBL; AL160171; CAH72069.1; JOINED; Genomic_DNA. DR EMBL; AL591719; CAH72070.1; ALT_SEQ; Genomic_DNA. DR EMBL; AL160171; CAH72070.1; JOINED; Genomic_DNA. DR EMBL; AL160171; CAI12932.1; -; Genomic_DNA. DR EMBL; AL591719; CAI12932.1; JOINED; Genomic_DNA. DR EMBL; AL160171; CAI12933.1; -; Genomic_DNA. DR EMBL; AL591719; CAI12933.1; JOINED; Genomic_DNA. DR EMBL; AL160171; CAI12934.1; ALT_SEQ; Genomic_DNA. DR EMBL; AL591719; CAI12934.1; JOINED; Genomic_DNA. DR EMBL; BC007757; AAH07757.1; ALT_TERM; mRNA. DR EMBL; BC016296; AAH16296.1; ALT_TERM; mRNA. DR EMBL; BC024275; AAH24275.1; ALT_TERM; mRNA. DR EMBL; BC040127; AAH40127.1; ALT_TERM; mRNA. DR EMBL; BC053838; AAH53838.1; -; mRNA. DR EMBL; BC107801; AAI07802.1; ALT_TERM; mRNA. DR EMBL; BC130346; AAI30347.1; -; mRNA. DR EMBL; BC132963; AAI32964.1; -; mRNA. DR EMBL; AY211915; AAO65168.1; ALT_INIT; mRNA. DR IPI; IPI00018098; -. DR IPI; IPI00647851; -. DR RefSeq; NP_060531.2; -. DR UniGene; Hs.342307; -. DR ProteinModelPortal; Q5VTL8; -. DR IntAct; Q5VTL8; 5. DR PhosphoSite; Q5VTL8; -. DR PRIDE; Q5VTL8; -. DR Ensembl; ENST00000370025; ENSP00000359042; ENSG00000134186. DR GeneID; 55119; -. DR KEGG; hsa:55119; -. DR NMPDR; fig|9606.3.peg.1611; -. DR UCSC; uc001dvv.2; human. DR CTD; 55119; -. DR GeneCards; GC01P109234; -. DR H-InvDB; HIX0020919; -. DR HGNC; HGNC:25512; PRPF38B. DR PharmGKB; PA142671126; -. DR HOVERGEN; HBG101033; -. DR InParanoid; Q5VTL8; -. DR OMA; DRGLDRR; -. DR OrthoDB; EOG98WFMN; -. DR PhylomeDB; Q5VTL8; -. DR NextBio; 58764; -. DR ArrayExpress; Q5VTL8; -. DR Bgee; Q5VTL8; -. DR CleanEx; HS_PRPF38B; -. DR Genevestigator; Q5VTL8; -. DR GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW. DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW. DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW. DR InterPro; IPR005037; PRP38. DR PANTHER; PTHR23142; PRP38; 1. DR Pfam; PF03371; PRP38; 1. PE 1: Evidence at protein level; KW Acetylation; Alternative splicing; Coiled coil; Complete proteome; KW mRNA processing; mRNA splicing; Nucleus; Phosphoprotein; Spliceosome. FT INIT_MET 1 1 Removed. FT CHAIN 2 546 Pre-mRNA-splicing factor 38B. FT /FTId=PRO_0000287235. FT COILED 292 321 Potential. FT COMPBIAS 253 451 Arg-rich. FT MOD_RES 2 2 N-acetylalanine. FT MOD_RES 5 5 Phosphoserine. FT MOD_RES 35 35 Phosphothreonine (By similarity). FT MOD_RES 227 227 N6-acetyllysine. FT MOD_RES 266 266 Phosphoserine. FT MOD_RES 268 268 Phosphoserine. FT MOD_RES 272 272 Phosphoserine. FT MOD_RES 290 290 Phosphoserine. FT MOD_RES 318 318 Phosphoserine. FT MOD_RES 320 320 Phosphoserine. FT MOD_RES 385 385 Phosphoserine. FT MOD_RES 527 527 Phosphoserine. FT MOD_RES 529 529 Phosphoserine. FT MOD_RES 534 534 Phosphoserine. FT VAR_SEQ 187 190 DLDV -> FFTL (in isoform 2). FT /FTId=VSP_025408. FT VAR_SEQ 191 546 Missing (in isoform 2). FT /FTId=VSP_025409. FT CONFLICT 52 52 N -> S (in Ref. 1; BAA91546). FT CONFLICT 294 295 EL -> DR (in Ref. 3; AAH40127). SQ SEQUENCE 546 AA; 64468 MW; A3082DCF491F88F8 CRC64; MANNSPALTG NSQPQHQAAA AAAQQQQQCG GGGATKPAVS GKQGNVLPLW GNEKTMNLNP MILTNILSSP YFKVQLYELK TYHEVVDEIY FKVTHVEPWE KGSRKTAGQT GMCGGVRGVG TGGIVSTAFC LLYKLFTLKL TRKQVMGLIT HTDSPYIRAL GFMYIRYTQP PTDLWDWFES FLDDEEDLDV KAGGGCVMTI GEMLRSFLTK LEWFSTLFPR IPVPVQKNID QQIKTRPRKI KKDGKEGAEE IDRHVERRRS RSPRRSLSPR RSPRRSRSRS HHREGHGSSS FDRELEREKE RQRLEREAKE REKERRRSRS IDRGLERRRS RSRERHRSRS RSRDRKGDRR DRDREREKEN ERGRRRDRDY DKERGNEREK ERERSRERSK EQRSRGEVEE KKHKEDKDDR RHRDDKRDSK KEKKHSRSRS RERKHRSRSR SRNAGKRSRS RSKEKSSKHK NESKEKSNKR SRSGSQGRTD SVEKSKKREH SPSKEKSRKR SRSKERSHKR DHSDSKDQSD KHDRRRSQSI EQESQEKQHK NKDETV //