PR38A_HUMAN
ID PR38A_HUMAN Reviewed; 312 AA.
AC Q8NAV1; Q96JW1; Q9BVZ8;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Pre-mRNA-splicing factor 38A;
GN Name=PRPF38A;
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 1).
RC TISSUE=Placenta;
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=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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, and Cervix;
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-209, AND IDENTIFICATION BY
RP 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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-193; SER-194 AND SER-209, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [7]
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-193 AND SER-194, AND
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-193; SER-194 AND SER-209, AND
RP 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 [10]
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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-193; SER-194 AND SER-209, AND
RP 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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11; SER-193; SER-194; SER-209
RP AND SER-226, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-209, AND IDENTIFICATION BY
RP 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 [14] {ECO:0007744|PDB:4RZ9, ECO:0007744|PDB:4RZA}
RP X-RAY CRYSTALLOGRAPHY (1.28 ANGSTROMS) OF 1-179, INTERACTION WITH MFAP1 AND
RP ZMAT2, SUBUNIT, MUTAGENESIS OF ASP-145, AND FUNCTION.
RX PubMed=26673105; DOI=10.1261/rna.054296.115;
RA Schuetze T., Ulrich A.K., Apelt L., Will C.L., Bartlick N., Seeger M.,
RA Weber G., Luehrmann R., Stelzl U., Wahl M.C.;
RT "Multiple protein-protein interactions converging on the Prp38 protein
RT during activation of the human spliceosome.";
RL RNA 22:265-277(2016).
RN [15] {ECO:0007744|PDB:5F5S}
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 1-179 IN COMPLEX WITH MFAP1, AND
RP INTERACTION WITH MFAP1.
RX PubMed=27773687; DOI=10.1016/j.str.2016.09.007;
RA Ulrich A.K.C., Seeger M., Schutze T., Bartlick N., Wahl M.C.;
RT "Scaffolding in the Spliceosome via Single alpha Helices.";
RL Structure 24:1972-1983(2016).
RN [16] {ECO:0007744|PDB:5O9Z}
RP STRUCTURE BY ELECTRON MICROSCOPY (4.50 ANGSTROMS), FUNCTION, SUBCELLULAR
RP LOCATION, AND SUBUNIT.
RX PubMed=28781166; DOI=10.1016/j.cell.2017.07.011;
RA Bertram K., Agafonov D.E., Dybkov O., Haselbach D., Leelaram M.N.,
RA Will C.L., Urlaub H., Kastner B., Luhrmann R., Stark H.;
RT "Cryo-EM Structure of a Pre-catalytic Human Spliceosome Primed for
RT Activation.";
RL Cell 170:701-713(2017).
CC -!- FUNCTION: Involved in pre-mRNA splicing as a component of the
CC spliceosome. {ECO:0000269|PubMed:26673105,
CC ECO:0000269|PubMed:28781166}.
CC -!- SUBUNIT: Component of the spliceosome B complex (Probable)
CC (PubMed:28781166). Interacts (via N-terminal interaction domain) with
CC ZMAT2 AND MFAP1 (Probable) (PubMed:27773687).
CC {ECO:0000269|PubMed:27773687, ECO:0000269|PubMed:28781166,
CC ECO:0000305|PubMed:26673105}.
CC -!- INTERACTION:
CC Q8NAV1; Q96CW1: AP2M1; NbExp=5; IntAct=EBI-715374, EBI-297683;
CC Q8NAV1; P49760: CLK2; NbExp=3; IntAct=EBI-715374, EBI-750020;
CC Q8NAV1; Q92997: DVL3; NbExp=3; IntAct=EBI-715374, EBI-739789;
CC Q8NAV1; Q6NYC1: JMJD6; NbExp=2; IntAct=EBI-715374, EBI-8464037;
CC Q8NAV1; O00560: SDCBP; NbExp=3; IntAct=EBI-715374, EBI-727004;
CC Q8NAV1; Q9H190: SDCBP2; NbExp=7; IntAct=EBI-715374, EBI-742426;
CC Q8NAV1; Q96SB4: SRPK1; NbExp=3; IntAct=EBI-715374, EBI-539478;
CC Q8NAV1; P78362: SRPK2; NbExp=6; IntAct=EBI-715374, EBI-593303;
CC Q8NAV1; Q16629: SRSF7; NbExp=3; IntAct=EBI-715374, EBI-398885;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:28781166}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8NAV1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8NAV1-2; Sequence=VSP_025424;
CC -!- SIMILARITY: Belongs to the PRP38 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB55405.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK027842; BAB55405.1; ALT_INIT; mRNA.
DR EMBL; AK092038; BAC03796.1; -; mRNA.
DR EMBL; AL513218; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC000777; AAH00777.2; -; mRNA.
DR EMBL; BC063655; AAH63655.1; -; mRNA.
DR EMBL; BC105004; AAI05005.1; -; mRNA.
DR EMBL; BC105006; AAI05007.1; -; mRNA.
DR CCDS; CCDS567.1; -. [Q8NAV1-1]
DR RefSeq; NP_116253.2; NM_032864.3. [Q8NAV1-1]
DR PDB; 4RZ9; X-ray; 1.28 A; A=1-179.
DR PDB; 4RZA; X-ray; 1.90 A; A=1-205.
DR PDB; 5F5S; X-ray; 2.40 A; A=1-179.
DR PDB; 5O9Z; EM; 4.50 A; I=1-312.
DR PDB; 6AHD; EM; 3.80 A; Z=1-312.
DR PDB; 7AAV; EM; 4.20 A; I=1-312.
DR PDB; 7ABF; EM; 3.90 A; I=1-312.
DR PDB; 7ABG; EM; 7.80 A; I=1-312.
DR PDB; 7ABI; EM; 8.00 A; I=1-312.
DR PDBsum; 4RZ9; -.
DR PDBsum; 4RZA; -.
DR PDBsum; 5F5S; -.
DR PDBsum; 5O9Z; -.
DR PDBsum; 6AHD; -.
DR PDBsum; 7AAV; -.
DR PDBsum; 7ABF; -.
DR PDBsum; 7ABG; -.
DR PDBsum; 7ABI; -.
DR AlphaFoldDB; Q8NAV1; -.
DR SMR; Q8NAV1; -.
DR BioGRID; 124382; 154.
DR IntAct; Q8NAV1; 51.
DR MINT; Q8NAV1; -.
DR STRING; 9606.ENSP00000257181; -.
DR iPTMnet; Q8NAV1; -.
DR PhosphoSitePlus; Q8NAV1; -.
DR BioMuta; PRPF38A; -.
DR DMDM; 74760086; -.
DR EPD; Q8NAV1; -.
DR jPOST; Q8NAV1; -.
DR MassIVE; Q8NAV1; -.
DR MaxQB; Q8NAV1; -.
DR PaxDb; Q8NAV1; -.
DR PeptideAtlas; Q8NAV1; -.
DR PRIDE; Q8NAV1; -.
DR ProteomicsDB; 72706; -. [Q8NAV1-1]
DR ProteomicsDB; 72707; -. [Q8NAV1-2]
DR Antibodypedia; 53332; 116 antibodies from 23 providers.
DR DNASU; 84950; -.
DR Ensembl; ENST00000257181.10; ENSP00000257181.8; ENSG00000134748.13. [Q8NAV1-1]
DR GeneID; 84950; -.
DR KEGG; hsa:84950; -.
DR MANE-Select; ENST00000257181.10; ENSP00000257181.8; NM_032864.4; NP_116253.2.
DR UCSC; uc001ctv.5; human. [Q8NAV1-1]
DR CTD; 84950; -.
DR GeneCards; PRPF38A; -.
DR HGNC; HGNC:25930; PRPF38A.
DR HPA; ENSG00000134748; Low tissue specificity.
DR neXtProt; NX_Q8NAV1; -.
DR OpenTargets; ENSG00000134748; -.
DR PharmGKB; PA142671125; -.
DR VEuPathDB; HostDB:ENSG00000134748; -.
DR eggNOG; KOG2889; Eukaryota.
DR GeneTree; ENSGT00730000111085; -.
DR HOGENOM; CLU_039466_1_0_1; -.
DR InParanoid; Q8NAV1; -.
DR OMA; FYMRLVG; -.
DR OrthoDB; 1182767at2759; -.
DR PhylomeDB; Q8NAV1; -.
DR TreeFam; TF105910; -.
DR PathwayCommons; Q8NAV1; -.
DR Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
DR SignaLink; Q8NAV1; -.
DR BioGRID-ORCS; 84950; 789 hits in 1081 CRISPR screens.
DR ChiTaRS; PRPF38A; human.
DR GenomeRNAi; 84950; -.
DR Pharos; Q8NAV1; Tbio.
DR PRO; PR:Q8NAV1; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q8NAV1; protein.
DR Bgee; ENSG00000134748; Expressed in tendon of biceps brachii and 192 other tissues.
DR Genevisible; Q8NAV1; HS.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0071011; C:precatalytic spliceosome; IDA:UniProtKB.
DR GO; GO:0071005; C:U2-type precatalytic spliceosome; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IDA:UniProtKB.
DR InterPro; IPR005037; PRP38.
DR InterPro; IPR024767; PRP38_C.
DR PANTHER; PTHR23142; PTHR23142; 1.
DR Pfam; PF03371; PRP38; 1.
DR Pfam; PF12871; PRP38_assoc; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Coiled coil; mRNA processing;
KW mRNA splicing; Nucleus; Phosphoprotein; Reference proteome; Spliceosome.
FT CHAIN 1..312
FT /note="Pre-mRNA-splicing factor 38A"
FT /id="PRO_0000287272"
FT REGION 1..179
FT /note="N-terminal protein interaction domain"
FT /evidence="ECO:0000269|PubMed:26673105"
FT REGION 181..312
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 170..204
FT /evidence="ECO:0000255"
FT COMPBIAS 188..204
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 205..227
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 228..312
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 11
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 193
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 194
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 209
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 MOD_RES 226
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..187
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_025424"
FT MUTAGEN 145
FT /note="D->A: Loss of interaction with MFAP1."
FT /evidence="ECO:0000269|PubMed:26673105"
FT CONFLICT 94
FT /note="E -> G (in Ref. 1; BAB55405)"
FT /evidence="ECO:0000305"
FT HELIX 1..3
FT /evidence="ECO:0007829|PDB:5F5S"
FT HELIX 17..20
FT /evidence="ECO:0007829|PDB:4RZ9"
FT HELIX 23..30
FT /evidence="ECO:0007829|PDB:4RZ9"
FT HELIX 33..38
FT /evidence="ECO:0007829|PDB:4RZ9"
FT HELIX 44..46
FT /evidence="ECO:0007829|PDB:4RZ9"
FT HELIX 47..51
FT /evidence="ECO:0007829|PDB:4RZ9"
FT TURN 62..65
FT /evidence="ECO:0007829|PDB:4RZ9"
FT HELIX 69..80
FT /evidence="ECO:0007829|PDB:4RZ9"
FT HELIX 84..92
FT /evidence="ECO:0007829|PDB:4RZ9"
FT HELIX 97..110
FT /evidence="ECO:0007829|PDB:4RZ9"
FT HELIX 113..120
FT /evidence="ECO:0007829|PDB:4RZ9"
FT HELIX 121..125
FT /evidence="ECO:0007829|PDB:4RZ9"
FT STRAND 129..133
FT /evidence="ECO:0007829|PDB:4RZ9"
FT STRAND 139..143
FT /evidence="ECO:0007829|PDB:4RZ9"
FT HELIX 144..153
FT /evidence="ECO:0007829|PDB:4RZ9"
FT STRAND 155..157
FT /evidence="ECO:0007829|PDB:4RZ9"
FT HELIX 168..173
FT /evidence="ECO:0007829|PDB:4RZ9"
SQ SEQUENCE 312 AA; 37477 MW; 0AABEEC0010EBD4B CRC64;
MANRTVKDAH SIHGTNPQYL VEKIIRTRIY ESKYWKEECF GLTAELVVDK AMELRFVGGV
YGGNIKPTPF LCLTLKMLQI QPEKDIIVEF IKNEDFKYVR MLGALYMRLT GTAIDCYKYL
EPLYNDYRKI KSQNRNGEFE LMHVDEFIDE LLHSERVCDI ILPRLQKRYV LEEAEQLEPR
VSALEEDMDD VESSEEEEEE DEKLERVPSP DHRRRSYRDL DKPRRSPTLR YRRSRSRSPR
RRSRSPKRRS PSPRRERHRS KSPRRHRSRS RDRRHRSRSK SPGHHRSHRH RSHSKSPERS
KKSHKKSRRG NE
