AK17A_HUMAN
ID AK17A_HUMAN Reviewed; 695 AA.
AC Q02040; Q02832; Q2TB98; Q5JQ74; Q5JQ76; Q8N6U9;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=A-kinase anchor protein 17A;
DE Short=AKAP-17A;
DE AltName: Full=721P;
DE AltName: Full=B-lymphocyte antigen;
DE AltName: Full=Protein XE7;
DE AltName: Full=Protein kinase A-anchoring protein 17A;
DE Short=PRKA17A;
DE AltName: Full=Splicing factor, arginine/serine-rich 17A;
GN Name=AKAP17A; Synonyms=CXYorf3, DXYS155E, SFRS17A, XE7;
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 [MRNA] (ISOFORM 1).
RX PubMed=1302606; DOI=10.1093/hmg/1.9.782-a;
RA Ellison J.W., Ramos C., Yen P.H., Shapiro L.J.;
RT "Structure and expression of the human pseudoautosomal gene XE7.";
RL Hum. Mol. Genet. 1:691-696(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
RX PubMed=1438229; DOI=10.1073/pnas.89.21.10425;
RA Voland J.R., Wyzykowski R.J., Huang M., Dutton R.W.;
RT "Cloning and sequencing of a trophoblast-endothelial-activated lymphocyte
RT surface protein: cDNA sequence and genomic structure.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:10425-10429(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3), AND VARIANT
RP SER-194.
RC TISSUE=Blood;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP IDENTIFICATION IN A COMPLEX WITH THE SPLICEOSOME, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=12176931; DOI=10.1101/gr.473902;
RA Rappsilber J., Ryder U., Lamond A.I., Mann M.;
RT "Large-scale proteomic analysis of the human spliceosome.";
RL Genome Res. 12:1231-1245(2002).
RN [6]
RP SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
RX PubMed=14759258; DOI=10.1186/gb-2004-5-2-r8;
RA Hillman R.T., Green R.E., Brenner S.E.;
RT "An unappreciated role for RNA surveillance.";
RL Genome Biol. 5:R8.1-R8.16(2004).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-537, 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 [8]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH ZRANB2 AND SFRS1.
RX PubMed=16982639; DOI=10.1093/nar/gkl660;
RA Mangs A.H., Speirs H.J.L., Goy C., Adams D.J., Markus M.A., Morris B.J.;
RT "XE7: a novel splicing factor that interacts with ASF/SF2 and ZNF265.";
RL Nucleic Acids Res. 34:4976-4986(2006).
RN [9]
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 [10]
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DOMAIN, AND
RP MUTAGENESIS OF 438-LEU-LEU-439 AND 445-LYS-LYS-446.
RX PubMed=19840947; DOI=10.1074/jbc.m109.056465;
RA Jarnaess E., Stokka A.J., Kvissel A.K., Skalhegg B.S., Torgersen K.M.,
RA Scott J.D., Carlson C.R., Tasken K.;
RT "Splicing factor arginine/serine-rich 17A (SFRS17A) is an A-kinase
RT anchoring protein that targets protein kinase A to splicing factor
RT compartments.";
RL J. Biol. Chem. 284:35154-35164(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-537 AND SER-633, 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-537, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-537, 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]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-118, AND IDENTIFICATION BY MASS
RP 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 [15]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-118, AND IDENTIFICATION BY MASS
RP 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: Splice factor regulating alternative splice site selection
CC for certain mRNA precursors. Mediates regulation of pre-mRNA splicing
CC in a PKA-dependent manner. {ECO:0000269|PubMed:16982639,
CC ECO:0000269|PubMed:19840947}.
CC -!- SUBUNIT: Monomer. Component of the spliceosome. Interacts with ZRANB2
CC and SFRS1/ASF through its Arg/Ser-rich domain. Interacts with RI and
CC RII subunits of PKA. {ECO:0000269|PubMed:12176931,
CC ECO:0000269|PubMed:16982639, ECO:0000269|PubMed:19840947}.
CC -!- INTERACTION:
CC Q02040; Q8N2N9-4: ANKRD36B; NbExp=3; IntAct=EBI-1042725, EBI-12170453;
CC Q02040; Q8NHQ1: CEP70; NbExp=7; IntAct=EBI-1042725, EBI-739624;
CC Q02040; Q92997: DVL3; NbExp=3; IntAct=EBI-1042725, EBI-739789;
CC Q02040; Q9UGU5: HMGXB4; NbExp=3; IntAct=EBI-1042725, EBI-7261162;
CC Q02040; P78317: RNF4; NbExp=5; IntAct=EBI-1042725, EBI-2340927;
CC Q02040; Q9H190: SDCBP2; NbExp=3; IntAct=EBI-1042725, EBI-742426;
CC Q02040; A7MD48: SRRM4; NbExp=3; IntAct=EBI-1042725, EBI-3867173;
CC Q02040; Q9NVV9: THAP1; NbExp=5; IntAct=EBI-1042725, EBI-741515;
CC Q02040; Q7KZS0: UBE2I; NbExp=3; IntAct=EBI-1042725, EBI-10180829;
CC Q02040; O95218: ZRANB2; NbExp=4; IntAct=EBI-1042725, EBI-1051583;
CC Q02040-3; Q13137: CALCOCO2; NbExp=3; IntAct=EBI-10222656, EBI-739580;
CC Q02040-3; Q8NHQ1: CEP70; NbExp=3; IntAct=EBI-10222656, EBI-739624;
CC Q02040-3; Q6A162: KRT40; NbExp=3; IntAct=EBI-10222656, EBI-10171697;
CC Q02040-3; Q99750: MDFI; NbExp=3; IntAct=EBI-10222656, EBI-724076;
CC Q02040-3; Q9NVV9: THAP1; NbExp=3; IntAct=EBI-10222656, EBI-741515;
CC Q02040-3; Q13077: TRAF1; NbExp=3; IntAct=EBI-10222656, EBI-359224;
CC -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000269|PubMed:16982639,
CC ECO:0000269|PubMed:19840947}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q02040-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q02040-2; Sequence=VSP_004490, VSP_004491;
CC Name=3;
CC IsoId=Q02040-3; Sequence=VSP_024947, VSP_024948;
CC -!- TISSUE SPECIFICITY: Widely expressed. Found in heart, brain, lung,
CC liver, skeletal muscle, kidney and pancreas. Expressed in activated B-
CC cells and placenta. Expressed in all cell lines tested including
CC Jurkat-TAg, U-937 and HEK293 cells. {ECO:0000269|PubMed:19840947}.
CC -!- DOMAIN: RI-alpha binding site, predicted to form an amphipathic helix,
CC could participate in protein-protein interactions with a complementary
CC surface on the R-subunit dimer. {ECO:0000269|PubMed:19840947}.
CC -!- MISCELLANEOUS: The gene coding for this protein is located in the
CC pseudoautosomal region 1 (PAR1) of X and Y chromosomes.
CC -!- MISCELLANEOUS: [Isoform 2]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- CAUTION: Was originally thought to be a cell surface protein involved
CC in B-cell activation. {ECO:0000305|PubMed:1438229}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA36187.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; L03426; AAA61303.1; -; mRNA.
DR EMBL; L03426; AAA61304.1; -; mRNA.
DR EMBL; M99578; AAA36187.1; ALT_FRAME; mRNA.
DR EMBL; AL683807; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC028151; AAH28151.1; -; mRNA.
DR EMBL; BC110496; AAI10497.1; -; mRNA.
DR EMBL; BC110497; AAI10498.1; -; mRNA.
DR CCDS; CCDS14116.1; -. [Q02040-1]
DR PIR; A46419; A46419.
DR PIR; I54325; I54325.
DR RefSeq; NP_005079.2; NM_005088.2. [Q02040-1]
DR AlphaFoldDB; Q02040; -.
DR BioGRID; 113860; 92.
DR IntAct; Q02040; 44.
DR STRING; 9606.ENSP00000324827; -.
DR iPTMnet; Q02040; -.
DR PhosphoSitePlus; Q02040; -.
DR BioMuta; AKAP17A; -.
DR DMDM; 146291102; -.
DR EPD; Q02040; -.
DR jPOST; Q02040; -.
DR MassIVE; Q02040; -.
DR MaxQB; Q02040; -.
DR PaxDb; Q02040; -.
DR PeptideAtlas; Q02040; -.
DR PRIDE; Q02040; -.
DR ProteomicsDB; 58030; -. [Q02040-1]
DR ProteomicsDB; 58031; -. [Q02040-2]
DR ProteomicsDB; 58032; -. [Q02040-3]
DR Antibodypedia; 23427; 229 antibodies from 30 providers.
DR DNASU; 8227; -.
DR Ensembl; ENST00000313871.9; ENSP00000324827.3; ENSG00000197976.12. [Q02040-1]
DR Ensembl; ENST00000474361.6; ENSP00000435479.1; ENSG00000197976.12. [Q02040-2]
DR GeneID; 8227; -.
DR KEGG; hsa:8227; -.
DR MANE-Select; ENST00000313871.9; ENSP00000324827.3; NM_005088.3; NP_005079.2.
DR UCSC; uc004cqa.4; human. [Q02040-1]
DR CTD; 8227; -.
DR DisGeNET; 8227; -.
DR GeneCards; AKAP17A; -.
DR HGNC; HGNC:18783; AKAP17A.
DR HPA; ENSG00000197976; Low tissue specificity.
DR MIM; 312095; gene.
DR MIM; 465000; gene.
DR neXtProt; NX_Q02040; -.
DR OpenTargets; ENSG00000197976; -.
DR PharmGKB; PA162402969; -.
DR VEuPathDB; HostDB:ENSG00000197976; -.
DR eggNOG; KOG2891; Eukaryota.
DR GeneTree; ENSGT00440000039314; -.
DR HOGENOM; CLU_011589_3_0_1; -.
DR InParanoid; Q02040; -.
DR OMA; AEEAPCK; -.
DR PhylomeDB; Q02040; -.
DR TreeFam; TF320443; -.
DR PathwayCommons; Q02040; -.
DR SignaLink; Q02040; -.
DR BioGRID-ORCS; 8227; 18 hits in 576 CRISPR screens.
DR ChiTaRS; AKAP17A; human.
DR GeneWiki; SFRS17A; -.
DR GenomeRNAi; 8227; -.
DR Pharos; Q02040; Tbio.
DR PRO; PR:Q02040; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; Q02040; protein.
DR Bgee; ENSG00000197976; Expressed in tibia and 196 other tissues.
DR ExpressionAtlas; Q02040; baseline and differential.
DR Genevisible; Q02040; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0016607; C:nuclear speck; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
DR GO; GO:0051018; F:protein kinase A binding; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0042113; P:B cell activation; NAS:UniProtKB.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0043484; P:regulation of RNA splicing; IMP:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; NAS:UniProtKB.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; NAS:UniProtKB.
DR InterPro; IPR034355; AKAP17A.
DR InterPro; IPR035979; RBD_domain_sf.
DR PANTHER; PTHR12484:SF2; PTHR12484:SF2; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Isopeptide bond; mRNA processing; mRNA splicing;
KW Nucleus; Phosphoprotein; Reference proteome; RNA-binding; Spliceosome;
KW Ubl conjugation.
FT CHAIN 1..695
FT /note="A-kinase anchor protein 17A"
FT /id="PRO_0000022692"
FT DOMAIN 147..256
FT /note="RRM"
FT REGION 83..112
FT /note="PKA-RI and PKA-RII subunit binding domain"
FT REGION 279..337
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 425..454
FT /note="PKA-RI-alpha subunit binding domain"
FT REGION 482..695
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 568..600
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 632..647
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 648..695
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 537
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 633
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT CROSSLNK 118
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0007744|PubMed:25114211"
FT CROSSLNK 118
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 385..445
FT /note="AVKLREQEQKEEKLRLQQQEERRRLQEAELRRVEEEKERALGLQRKERELRE
FT RLLSILLSK -> VGGSLCSRQPRPGCPQCPPLKCGRRHGAVSPPAAAVATKPALMPRM
FT TAPSREGVALVCRSR (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_024947"
FT VAR_SEQ 385
FT /note="A -> L (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_004490"
FT VAR_SEQ 386..695
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_004491"
FT VAR_SEQ 446..695
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_024948"
FT VARIANT 194
FT /note="P -> S (in dbSNP:rs17852504)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_055353"
FT MUTAGEN 438..439
FT /note="LL->PP: Abolishes binding to PKA-RI; when associated
FT with 445-P-P-446."
FT /evidence="ECO:0000269|PubMed:19840947"
FT MUTAGEN 445..446
FT /note="KK->PP: Abolishes binding to PKA-RI; when associated
FT with 438-P-P-439."
FT /evidence="ECO:0000269|PubMed:19840947"
FT CONFLICT 443
FT /note="L -> Q (in Ref. 2; AAA36187)"
FT /evidence="ECO:0000305"
FT CONFLICT 500
FT /note="P -> A (in Ref. 1; AAA61303 and 4; AAI10497)"
FT /evidence="ECO:0000305"
FT CONFLICT 502
FT /note="H -> P (in Ref. 2; AAA36187)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 695 AA; 80735 MW; 639E88ECA8006CF2 CRC64;
MAAATIVHDT SEAVELCPAY GLYLKPITKM TISVALPQLK QPGKSISNWE VMERLKGMVQ
NHQFSTLRIS KSTMDFIRFE GEVENKSLVK SFLACLDGKT IKLSGFSDIL KVRAAEFKID
FPTRHDWDSF FRDAKDMNET LPGERPDTIH LEGLPCKWFA LKESGSEKPS EDVLVKVFEK
FGEIRNVDIP MLDPYREEMT GRNFHTFSFG GHLNFEAYVQ YREYMGFIQA MSALRGMKLM
YKGEDGKAVA CNIKVSFDST KHLSDASIKK RQLERQKLQE LEQQREEQKR REKEAEERQR
AEERKQKELE ELERERKREE KLRKREQKQR DRELRRNQKK LEKLQAEEQK QLQEKIKLEE
RKLLLAQRNL QSIRLIAELL SRAKAVKLRE QEQKEEKLRL QQQEERRRLQ EAELRRVEEE
KERALGLQRK ERELRERLLS ILLSKKPDDS HTHDELGVAH ADLLQPVLDI LQTVSSGCVS
ATTLHPLGGQ PPAGAPKESP AHPEADGAPK SVNGSVAEEA PCKEVQSSCR VVPEDGSPEK
RCPGGVLSCI PDNNQQPKGI PACEQNVSRK DTRSEQDKCN REPSKGRGRA TGDGLADRHK
RERSRARRAS SREDGRPRKE RRPHKKHAYK DDSPRRRSTS PDHTRSRRSH SKDRHRRERS
RERRGSASRK HSRHRRRSER SRSRSPSRHR STWNR
