ID   CSKI2_HUMAN             Reviewed;        1202 AA.
AC   Q8WXE0; B4DTT3; B7Z9H1; Q7LG69; Q9ULT1;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 2.
DT   27-MAR-2024, entry version 177.
DE   RecName: Full=Caskin-2;
DE   AltName: Full=CASK-interacting protein 2;
GN   Name=CASKIN2; Synonyms=KIAA1139;
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), AND VARIANT GLY-891.
RX   PubMed=12040031; DOI=10.1523/jneurosci.22-11-04264.2002;
RA   Tabuchi K., Biederer T., Butz S., Suedhof T.C.;
RT   "CASK participates in alternative tripartite complexes in which Mint 1
RT   competes for binding with Caskin 1, a novel CASK-binding protein.";
RL   J. Neurosci. 22:4264-4273(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT GLY-891.
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16625196; DOI=10.1038/nature04689;
RA   Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA   Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA   Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA   Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA   DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA   Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA   Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA   LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA   Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA   Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA   Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA   Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA   Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT   "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT   human lineage.";
RL   Nature 440:1045-1049(2006).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT GLY-891.
RC   TISSUE=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 project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 79-1202 (ISOFORM 1), AND VARIANT
RP   GLY-891.
RC   TISSUE=Brain;
RX   PubMed=10574461; DOI=10.1093/dnares/6.5.329;
RA   Hirosawa M., Nagase T., Ishikawa K., Kikuno R., Nomura N., Ohara O.;
RT   "Characterization of cDNA clones selected by the GeneMark analysis from
RT   size-fractionated cDNA libraries from human brain.";
RL   DNA Res. 6:329-336(1999).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-393; SER-396; SER-471;
RP   SER-858 AND SER-892, VARIANT [LARGE SCALE ANALYSIS] GLY-891, 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   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-396 AND SER-471, 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   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-393 AND SER-396, 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   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-253; SER-358; SER-393;
RP   SER-396; SER-471; SER-725; SER-858; SER-878 AND SER-892, VARIANT [LARGE
RP   SCALE ANALYSIS] GLY-891, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
RP   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   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-403 AND SER-406, 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   [11]
RP   STRUCTURE BY NMR OF 284-348.
RX   PubMed=21328705; DOI=10.1142/s0219720011005276;
RA   Alipanahi B., Gao X., Karakoc E., Li S.C., Balbach F., Feng G.,
RA   Donaldson L., Li M.;
RT   "Error tolerant NMR backbone resonance assignment and automated structure
RT   generation.";
RL   J. Bioinform. Comput. Biol. 9:15-41(2011).
CC   -!- SUBUNIT: May not bind CASK.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8WXE0-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8WXE0-2; Sequence=VSP_040568;
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DR   EMBL; AF451976; AAL49757.1; -; mRNA.
DR   EMBL; AK300354; BAG62095.1; -; mRNA.
DR   EMBL; AK315936; BAH14307.1; -; mRNA.
DR   EMBL; AC100787; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC066643; AAH66643.1; -; mRNA.
DR   EMBL; AB032965; BAA86453.1; -; mRNA.
DR   CCDS; CCDS11723.1; -. [Q8WXE0-1]
DR   CCDS; CCDS45775.1; -. [Q8WXE0-2]
DR   RefSeq; NP_001136115.1; NM_001142643.2. [Q8WXE0-2]
DR   RefSeq; NP_065804.2; NM_020753.4. [Q8WXE0-1]
DR   PDB; 2KE9; NMR; -; A=284-348.
DR   PDB; 4IS7; X-ray; 2.75 A; A=483-633.
DR   PDB; 5L1M; X-ray; 2.75 A; A=483-633.
DR   PDB; 7ZW4; X-ray; 2.72 A; B=1178-1202.
DR   PDBsum; 2KE9; -.
DR   PDBsum; 4IS7; -.
DR   PDBsum; 5L1M; -.
DR   PDBsum; 7ZW4; -.
DR   AlphaFoldDB; Q8WXE0; -.
DR   BMRB; Q8WXE0; -.
DR   SMR; Q8WXE0; -.
DR   BioGRID; 121577; 52.
DR   IntAct; Q8WXE0; 13.
DR   MINT; Q8WXE0; -.
DR   STRING; 9606.ENSP00000325355; -.
DR   GlyCosmos; Q8WXE0; 1 site, 1 glycan.
DR   GlyGen; Q8WXE0; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q8WXE0; -.
DR   PhosphoSitePlus; Q8WXE0; -.
DR   SwissPalm; Q8WXE0; -.
DR   BioMuta; CASKIN2; -.
DR   DMDM; 296434467; -.
DR   EPD; Q8WXE0; -.
DR   jPOST; Q8WXE0; -.
DR   MassIVE; Q8WXE0; -.
DR   MaxQB; Q8WXE0; -.
DR   PaxDb; 9606-ENSP00000325355; -.
DR   PeptideAtlas; Q8WXE0; -.
DR   ProteomicsDB; 75016; -. [Q8WXE0-1]
DR   ProteomicsDB; 75017; -. [Q8WXE0-2]
DR   Pumba; Q8WXE0; -.
DR   Antibodypedia; 53193; 199 antibodies from 26 providers.
DR   DNASU; 57513; -.
DR   Ensembl; ENST00000321617.8; ENSP00000325355.3; ENSG00000177303.10. [Q8WXE0-1]
DR   Ensembl; ENST00000433559.6; ENSP00000406963.2; ENSG00000177303.10. [Q8WXE0-2]
DR   GeneID; 57513; -.
DR   KEGG; hsa:57513; -.
DR   MANE-Select; ENST00000321617.8; ENSP00000325355.3; NM_020753.5; NP_065804.2.
DR   UCSC; uc002joc.5; human. [Q8WXE0-1]
DR   AGR; HGNC:18200; -.
DR   CTD; 57513; -.
DR   DisGeNET; 57513; -.
DR   GeneCards; CASKIN2; -.
DR   HGNC; HGNC:18200; CASKIN2.
DR   HPA; ENSG00000177303; Low tissue specificity.
DR   MIM; 612185; gene.
DR   neXtProt; NX_Q8WXE0; -.
DR   OpenTargets; ENSG00000177303; -.
DR   PharmGKB; PA134944093; -.
DR   VEuPathDB; HostDB:ENSG00000177303; -.
DR   eggNOG; KOG0507; Eukaryota.
DR   eggNOG; KOG4384; Eukaryota.
DR   GeneTree; ENSGT00940000158256; -.
DR   HOGENOM; CLU_003619_2_0_1; -.
DR   InParanoid; Q8WXE0; -.
DR   OrthoDB; 25046at2759; -.
DR   PhylomeDB; Q8WXE0; -.
DR   TreeFam; TF320582; -.
DR   PathwayCommons; Q8WXE0; -.
DR   SignaLink; Q8WXE0; -.
DR   BioGRID-ORCS; 57513; 14 hits in 1154 CRISPR screens.
DR   ChiTaRS; CASKIN2; human.
DR   GenomeRNAi; 57513; -.
DR   Pharos; Q8WXE0; Tdark.
DR   PRO; PR:Q8WXE0; -.
DR   Proteomes; UP000005640; Chromosome 17.
DR   RNAct; Q8WXE0; Protein.
DR   Bgee; ENSG00000177303; Expressed in olfactory bulb and 180 other cell types or tissues.
DR   ExpressionAtlas; Q8WXE0; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   CDD; cd09497; SAM_caskin1_2_repeat1; 1.
DR   CDD; cd09498; SAM_caskin1_2_repeat2; 1.
DR   CDD; cd12063; SH3_Caskin2; 1.
DR   Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 3.
DR   Gene3D; 2.30.30.40; SH3 Domains; 1.
DR   Gene3D; 1.10.150.50; Transcription Factor, Ets-1; 2.
DR   InterPro; IPR033635; ANKS1/Caskin.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   InterPro; IPR032232; Caskin1-CID.
DR   InterPro; IPR035497; Caskin1/2_SAM_1.
DR   InterPro; IPR035498; Caskin1/2_SAM_2.
DR   InterPro; IPR035499; Caskin2_SH3.
DR   InterPro; IPR032117; Caskin_C.
DR   InterPro; IPR001660; SAM.
DR   InterPro; IPR013761; SAM/pointed_sf.
DR   InterPro; IPR036028; SH3-like_dom_sf.
DR   InterPro; IPR001452; SH3_domain.
DR   PANTHER; PTHR24174; ANKYRIN REPEAT AND STERILE ALPHA MOTIF DOMAIN-CONTAINING PROTEIN 1; 1.
DR   PANTHER; PTHR24174:SF18; CASKIN-2; 1.
DR   Pfam; PF12796; Ank_2; 3.
DR   Pfam; PF16907; Caskin-Pro-rich; 1.
DR   Pfam; PF16632; Caskin-tail; 1.
DR   Pfam; PF16600; Caskin1-CID; 1.
DR   Pfam; PF00536; SAM_1; 2.
DR   Pfam; PF07653; SH3_2; 1.
DR   PRINTS; PR01415; ANKYRIN.
DR   SMART; SM00248; ANK; 6.
DR   SMART; SM00454; SAM; 2.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF48403; Ankyrin repeat; 1.
DR   SUPFAM; SSF47769; SAM/Pointed domain; 2.
DR   SUPFAM; SSF50044; SH3-domain; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 5.
DR   PROSITE; PS50105; SAM_DOMAIN; 2.
DR   PROSITE; PS50002; SH3; 1.
DR   Genevisible; Q8WXE0; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; ANK repeat; Cytoplasm; Phosphoprotein;
KW   Reference proteome; Repeat; SH3 domain.
FT   CHAIN           1..1202
FT                   /note="Caskin-2"
FT                   /id="PRO_0000066983"
FT   REPEAT          48..77
FT                   /note="ANK 1"
FT   REPEAT          81..110
FT                   /note="ANK 2"
FT   REPEAT          114..143
FT                   /note="ANK 3"
FT   REPEAT          147..176
FT                   /note="ANK 4"
FT   REPEAT          188..217
FT                   /note="ANK 5"
FT   REPEAT          220..249
FT                   /note="ANK 6"
FT   DOMAIN          281..347
FT                   /note="SH3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT   DOMAIN          489..552
FT                   /note="SAM 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT   DOMAIN          558..622
FT                   /note="SAM 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT   REGION          355..460
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          676..1104
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1116..1181
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        364..381
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        399..427
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        698..718
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        752..791
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        823..855
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        865..893
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        986..1000
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1018..1069
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1122..1136
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1138..1158
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         253
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         358
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         393
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT   MOD_RES         396
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         403
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:24275569"
FT   MOD_RES         406
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:24275569"
FT   MOD_RES         409
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8VHK1"
FT   MOD_RES         471
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"
FT   MOD_RES         725
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         858
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         877
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8VHK1"
FT   MOD_RES         878
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         892
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:23186163"
FT   VAR_SEQ         1..82
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_040568"
FT   VARIANT         891
FT                   /note="E -> G (in dbSNP:rs7503373)"
FT                   /evidence="ECO:0000269|PubMed:10574461,
FT                   ECO:0000269|PubMed:12040031, ECO:0000269|PubMed:14702039,
FT                   ECO:0000269|PubMed:15489334, ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:23186163"
FT                   /id="VAR_060244"
FT   CONFLICT        640
FT                   /note="A -> G (in Ref. 2; BAH14307)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1093
FT                   /note="L -> P (in Ref. 2; BAH14307)"
FT                   /evidence="ECO:0000305"
FT   STRAND          284..290
FT                   /evidence="ECO:0007829|PDB:2KE9"
FT   STRAND          308..312
FT                   /evidence="ECO:0007829|PDB:2KE9"
FT   STRAND          320..324
FT                   /evidence="ECO:0007829|PDB:2KE9"
FT   STRAND          335..337
FT                   /evidence="ECO:0007829|PDB:2KE9"
FT   HELIX           339..341
FT                   /evidence="ECO:0007829|PDB:2KE9"
FT   STRAND          342..345
FT                   /evidence="ECO:0007829|PDB:2KE9"
FT   HELIX           490..499
FT                   /evidence="ECO:0007829|PDB:4IS7"
FT   TURN            500..502
FT                   /evidence="ECO:0007829|PDB:4IS7"
FT   HELIX           504..506
FT                   /evidence="ECO:0007829|PDB:5L1M"
FT   HELIX           507..512
FT                   /evidence="ECO:0007829|PDB:4IS7"
FT   HELIX           517..520
FT                   /evidence="ECO:0007829|PDB:4IS7"
FT   HELIX           525..530
FT                   /evidence="ECO:0007829|PDB:4IS7"
FT   HELIX           536..547
FT                   /evidence="ECO:0007829|PDB:4IS7"
FT   TURN            555..558
FT                   /evidence="ECO:0007829|PDB:4IS7"
FT   HELIX           563..569
FT                   /evidence="ECO:0007829|PDB:4IS7"
FT   HELIX           573..575
FT                   /evidence="ECO:0007829|PDB:4IS7"
FT   HELIX           576..581
FT                   /evidence="ECO:0007829|PDB:4IS7"
FT   HELIX           587..590
FT                   /evidence="ECO:0007829|PDB:4IS7"
FT   HELIX           595..597
FT                   /evidence="ECO:0007829|PDB:4IS7"
FT   HELIX           598..601
FT                   /evidence="ECO:0007829|PDB:4IS7"
FT   HELIX           606..624
FT                   /evidence="ECO:0007829|PDB:4IS7"
SQ   SEQUENCE   1202 AA;  126783 MW;  881E6BAEEBDF3DC5 CRC64;
     MGREQDLILA VKNGDVTGVQ KLVAKVKATK TKLLGSTKRL NVNYQDADGF SALHHAALGG
     SLELIALLLE AQATVDIKDS NGMRPLHYAA WQGRLEPVRL LLRASAAVNA ASLDGQIPLH
     LAAQYGHYEV SEMLLQHQSN PCLVNKAKKT PLDLACEFGR LKVAQLLLNS HLCVALLEGE
     AKDPCDPNYT TPLHLAAKNG HREVIRQLLR AGIEINRQTK TGTALHEAAL YGKTEVVRLL
     LEGGVDVNIR NTYNQTALDI VNQFTTSQAS REIKQLLREA SGILKVRALK DFWNLHDPTA
     LNVRAGDVIT VLEQHPDGRW KGHIHESQRG TDRIGYFPPG IVEVVSKRVG IPAARLPSAP
     TPLRPGFSRT PQPPAEEPPH PLTYSQLPRV GLSPDSPAGD RNSVGSEGSV GSIRSAGSGQ
     SSEGTNGHGP GLLIENAQPL PSAGEDQVLP GLHPPSLADN LSHRPLANCR SGEQIFTQDV
     RPEQLLEGKD AQAIHNWLSE FQLEGYTAHF LQAGYDVPTI SRMTPEDLTA IGVTKPGHRK
     KIASEIAQLS IAEWLPSYIP TDLLEWLCAL GLPQYHKQLV SSGYDSMGLV ADLTWEELQE
     IGVNKLGHQK KLMLGVKRLA ELRRGLLQGE ALSEGGRRLA KGPELMAIEG LENGEGPATA
     GPRLLTFQGS ELSPELQAAM AGGGPEPLPL PPARSPSQES IGARSRGSGH SQEQPAPQPS
     GGDPSPPQER NLPEGTERPP KLCSSLPGQG PPPYVFMYPQ GSPSSPAPGP PPGAPWAFSY
     LAGPPATPPD PPRPKRRSHS LSRPGPTEGD AEGEAEGPVG STLGSYATLT RRPGRSALVR
     TSPSVTPTPA RGTPRSQSFA LRARRKGPPP PPPKRLSSVS GPSPEPPPLD ESPGPKEGAT
     GPRRRTLSEP AGPSEPPGPP APAGPASDTE EEEPGPEGTP PSRGSSGEGL PFAEEGNLTI
     KQRPKPAGPP PRETPVPPGL DFNLTESDTV KRRPKCRERE PLQTALLAFG VASATPGPAA
     PLPSPTPGES PPASSLPQPE PSSLPAQGVP TPLAPSPAMQ PPVPPCPGPG LESSAASRWN
     GETEPPAAPA ALLKVPGAGT APKPVSVACT QLAFSGPKLA PRLGPRPVPP PRPESTGTVG
     PGQAQQRLEQ TSSSLAAALR AAEKSIGTKE QEGTPSASTK HILDDISTMF DALADQLDAM
     LD
//