CSPP1_HUMAN
ID CSPP1_HUMAN Reviewed; 1256 AA.
AC Q1MSJ5; A6ND63; Q70F00; Q8TBC1;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 4.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Centrosome and spindle pole-associated protein 1;
GN Name=CSPP1; Synonyms=CSPP;
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 2), SUBCELLULAR LOCATION,
RP PHOSPHORYLATION, AND TISSUE SPECIFICITY.
RC TISSUE=Testis;
RX PubMed=15580290; DOI=10.1038/sj.onc.1208267;
RA Patzke S., Hauge H., Sioud M., Finne E.F., Sivertsen E.A., Delabie J.,
RA Stokke T., Aasheim H.-C.;
RT "Identification of a novel centrosome/microtubule-associated coiled-coil
RT protein involved in cell-cycle progression and spindle organization.";
RL Oncogene 24:1159-1173(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, DEVELOPMENTAL STAGE, AND
RP SUBCELLULAR LOCATION.
RC TISSUE=Testis;
RX PubMed=16826565; DOI=10.1002/jcp.20725;
RA Patzke S., Stokke T., Aasheim H.-C.;
RT "CSPP and CSPP-L associate with centrosomes and microtubules and
RT differently affect microtubule organization.";
RL J. Cell. Physiol. 209:199-210(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16421571; DOI=10.1038/nature04406;
RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M.,
RA Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L.,
RA Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S.,
RA Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A.,
RA Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III,
RA Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K.,
RA Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B.,
RA O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K.,
RA Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L.,
RA Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G.,
RA Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W.,
RA Platzer M., Shimizu N., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 8.";
RL Nature 439:331-335(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 11-440 (ISOFORM 3).
RC TISSUE=Brain;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS HIS-907
RP AND ARG-1135.
RC TISSUE=Bone marrow;
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 [6]
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-527 AND SER-966, 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-966, AND IDENTIFICATION BY
RP 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 SER-244; SER-459; SER-527;
RP SER-901; SER-920 AND SER-966, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [10]
RP INVOLVEMENT IN JBTS21.
RX PubMed=24360808; DOI=10.1016/j.ajhg.2013.11.019;
RA Tuz K., Bachmann-Gagescu R., O'Day D.R., Hua K., Isabella C.R.,
RA Phelps I.G., Stolarski A.E., O'Roak B.J., Dempsey J.C., Lourenco C.,
RA Alswaid A., Bonnemann C.G., Medne L., Nampoothiri S., Stark Z.,
RA Leventer R.J., Topcu M., Cansu A., Jagadeesh S., Done S., Ishak G.E.,
RA Glass I.A., Shendure J., Neuhauss S.C., Haldeman-Englert C.R., Doherty D.,
RA Ferland R.J.;
RT "Mutations in CSPP1 cause primary cilia abnormalities and Joubert syndrome
RT with or without Jeune asphyxiating thoracic dystrophy.";
RL Am. J. Hum. Genet. 94:62-72(2014).
RN [11]
RP INVOLVEMENT IN JBTS21.
RX PubMed=24360803; DOI=10.1016/j.ajhg.2013.11.010;
RA Shaheen R., Shamseldin H.E., Loucks C.M., Seidahmed M.Z., Ansari S.,
RA Ibrahim Khalil M., Al-Yacoub N., Davis E.E., Mola N.A., Szymanska K.,
RA Herridge W., Chudley A.E., Chodirker B.N., Schwartzentruber J.,
RA Majewski J., Katsanis N., Poizat C., Johnson C.A., Parboosingh J.,
RA Boycott K.M., Innes A.M., Alkuraya F.S.;
RT "Mutations in CSPP1, encoding a core centrosomal protein, cause a range of
RT ciliopathy phenotypes in humans.";
RL Am. J. Hum. Genet. 94:73-79(2014).
RN [12]
RP TISSUE SPECIFICITY, AND INVOLVEMENT IN JBTS21.
RX PubMed=24360807; DOI=10.1016/j.ajhg.2013.11.015;
RA Akizu N., Silhavy J.L., Rosti R.O., Scott E., Fenstermaker A.G.,
RA Schroth J., Zaki M.S., Sanchez H., Gupta N., Kabra M., Kara M.,
RA Ben-Omran T., Rosti B., Guemez-Gamboa A., Spencer E., Pan R., Cai N.,
RA Abdellateef M., Gabriel S., Halbritter J., Hildebrandt F., van Bokhoven H.,
RA Gunel M., Gleeson J.G.;
RT "Mutations in CSPP1 lead to classical Joubert syndrome.";
RL Am. J. Hum. Genet. 94:80-86(2014).
RN [13]
RP INTERACTION WITH ARMC9; TOGARAM1; CCDC66; CEP104 AND CEP290.
RX PubMed=32453716; DOI=10.1172/jci131656;
RG University of Washington Center for Mendelian Genomics;
RG Genomics England Research Consortium;
RA Latour B.L., Van De Weghe J.C., Rusterholz T.D., Letteboer S.J., Gomez A.,
RA Shaheen R., Gesemann M., Karamzade A., Asadollahi M., Barroso-Gil M.,
RA Chitre M., Grout M.E., van Reeuwijk J., van Beersum S.E., Miller C.V.,
RA Dempsey J.C., Morsy H., Bamshad M.J., Nickerson D.A., Neuhauss S.C.,
RA Boldt K., Ueffing M., Keramatipour M., Sayer J.A., Alkuraya F.S.,
RA Bachmann-Gagescu R., Roepman R., Doherty D.;
RT "Dysfunction of the ciliary ARMC9/TOGARAM1 protein module causes Joubert
RT syndrome.";
RL J. Clin. Invest. 130:4423-4439(2020).
CC -!- FUNCTION: May play a role in cell-cycle-dependent microtubule
CC organization. {ECO:0000269|PubMed:16826565}.
CC -!- SUBUNIT: Interacts with PLEKHG6. Interacts with ARMC9, TOGARAM1,
CC CCDC66, CEP104 and CEP290 (PubMed:32453716).
CC {ECO:0000250|UniProtKB:B2RX88, ECO:0000269|PubMed:32453716}.
CC -!- INTERACTION:
CC Q1MSJ5-1; Q08379: GOLGA2; NbExp=3; IntAct=EBI-10239122, EBI-618309;
CC Q1MSJ5-1; Q99471: PFDN5; NbExp=3; IntAct=EBI-10239122, EBI-357275;
CC Q1MSJ5-1; Q6NUQ1: RINT1; NbExp=3; IntAct=EBI-10239122, EBI-726876;
CC Q1MSJ5-2; Q96HT8: MRFAP1L1; NbExp=3; IntAct=EBI-10239155, EBI-748896;
CC Q1MSJ5-2; Q96KN7: RPGRIP1; NbExp=3; IntAct=EBI-10239155, EBI-1050213;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome. Cytoplasm, cytoskeleton, spindle. Cytoplasm,
CC cytoskeleton, spindle pole {ECO:0000250}. Note=Associated with mitotic
CC spindles.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=3;
CC IsoId=Q1MSJ5-3; Sequence=Displayed;
CC Name=1; Synonyms=CSPP-L;
CC IsoId=Q1MSJ5-1; Sequence=VSP_040072;
CC Name=2; Synonyms=CSPP, CSPP-S;
CC IsoId=Q1MSJ5-2; Sequence=VSP_026475, VSP_026476;
CC -!- TISSUE SPECIFICITY: Expressed in adult and fetal brain with enrichment
CC in the cerebellum. Detected in testis. {ECO:0000269|PubMed:15580290,
CC ECO:0000269|PubMed:24360807}.
CC -!- DEVELOPMENTAL STAGE: Isoform 1 expression increases throughout the cell
CC cycle and peaks in G2/M phase. Isoform 2 expression is highest in G1
CC phase and decreases thereafter. {ECO:0000269|PubMed:16826565}.
CC -!- PTM: Phosphorylated. Phosphorylation increases in colcemide-treated
CC cells. {ECO:0000269|PubMed:15580290}.
CC -!- DISEASE: Joubert syndrome 21 (JBTS21) [MIM:615636]: A disorder
CC presenting with cerebellar ataxia, oculomotor apraxia, hypotonia,
CC neonatal breathing abnormalities and psychomotor delay.
CC Neuroradiologically, it is characterized by cerebellar vermian
CC hypoplasia/aplasia, thickened and reoriented superior cerebellar
CC peduncles, and an abnormally large interpeduncular fossa, giving the
CC appearance of a molar tooth on transaxial slices (molar tooth sign).
CC Additional variable features include retinal dystrophy, renal disease,
CC liver fibrosis, and polydactyly. {ECO:0000269|PubMed:24360803,
CC ECO:0000269|PubMed:24360807, ECO:0000269|PubMed:24360808}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH22867.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AJ583433; CAE47426.1; -; mRNA.
DR EMBL; AM156947; CAJ42307.1; -; mRNA.
DR EMBL; AC087359; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC109335; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK127108; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC022867; AAH22867.1; ALT_INIT; mRNA.
DR EMBL; BC152993; AAI52994.1; -; mRNA.
DR CCDS; CCDS43744.1; -. [Q1MSJ5-1]
DR CCDS; CCDS78344.1; -. [Q1MSJ5-2]
DR RefSeq; NP_001278268.1; NM_001291339.1. [Q1MSJ5-2]
DR RefSeq; NP_079066.5; NM_024790.6. [Q1MSJ5-1]
DR AlphaFoldDB; Q1MSJ5; -.
DR SMR; Q1MSJ5; -.
DR BioGRID; 122939; 93.
DR IntAct; Q1MSJ5; 58.
DR MINT; Q1MSJ5; -.
DR STRING; 9606.ENSP00000262210; -.
DR GlyGen; Q1MSJ5; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q1MSJ5; -.
DR PhosphoSitePlus; Q1MSJ5; -.
DR BioMuta; CSPP1; -.
DR DMDM; 313104301; -.
DR EPD; Q1MSJ5; -.
DR jPOST; Q1MSJ5; -.
DR MassIVE; Q1MSJ5; -.
DR MaxQB; Q1MSJ5; -.
DR PaxDb; Q1MSJ5; -.
DR PeptideAtlas; Q1MSJ5; -.
DR PRIDE; Q1MSJ5; -.
DR ProteomicsDB; 61228; -. [Q1MSJ5-3]
DR ProteomicsDB; 61229; -. [Q1MSJ5-1]
DR ProteomicsDB; 61230; -. [Q1MSJ5-2]
DR Antibodypedia; 42498; 178 antibodies from 28 providers.
DR DNASU; 79848; -.
DR Ensembl; ENST00000519668.1; ENSP00000430092.1; ENSG00000104218.16. [Q1MSJ5-2]
DR Ensembl; ENST00000674993.1; ENSP00000502454.1; ENSG00000104218.16. [Q1MSJ5-3]
DR Ensembl; ENST00000676317.1; ENSP00000502047.1; ENSG00000104218.16. [Q1MSJ5-1]
DR GeneID; 79848; -.
DR KEGG; hsa:79848; -.
DR UCSC; uc003xxj.4; human. [Q1MSJ5-3]
DR CTD; 79848; -.
DR DisGeNET; 79848; -.
DR GeneCards; CSPP1; -.
DR GeneReviews; CSPP1; -.
DR HGNC; HGNC:26193; CSPP1.
DR HPA; ENSG00000104218; Low tissue specificity.
DR MalaCards; CSPP1; -.
DR MIM; 611654; gene.
DR MIM; 615636; phenotype.
DR neXtProt; NX_Q1MSJ5; -.
DR OpenTargets; ENSG00000104218; -.
DR Orphanet; 475; Joubert syndrome.
DR Orphanet; 397715; Joubert syndrome with Jeune asphyxiating thoracic dystrophy.
DR Orphanet; 564; Meckel syndrome.
DR PharmGKB; PA142672066; -.
DR VEuPathDB; HostDB:ENSG00000104218; -.
DR eggNOG; ENOG502QTSW; Eukaryota.
DR GeneTree; ENSGT00390000015084; -.
DR HOGENOM; CLU_009662_0_0_1; -.
DR InParanoid; Q1MSJ5; -.
DR OrthoDB; 1439603at2759; -.
DR PhylomeDB; Q1MSJ5; -.
DR TreeFam; TF335475; -.
DR PathwayCommons; Q1MSJ5; -.
DR SignaLink; Q1MSJ5; -.
DR BioGRID-ORCS; 79848; 14 hits in 1079 CRISPR screens.
DR ChiTaRS; CSPP1; human.
DR GenomeRNAi; 79848; -.
DR Pharos; Q1MSJ5; Tbio.
DR PRO; PR:Q1MSJ5; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; Q1MSJ5; protein.
DR Bgee; ENSG00000104218; Expressed in bronchial epithelial cell and 193 other tissues.
DR ExpressionAtlas; Q1MSJ5; baseline and differential.
DR Genevisible; Q1MSJ5; HS.
DR GO; GO:0034451; C:centriolar satellite; IDA:HPA.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005819; C:spindle; IDA:UniProtKB.
DR GO; GO:0000922; C:spindle pole; IDA:UniProtKB.
DR GO; GO:0051781; P:positive regulation of cell division; IMP:UniProtKB.
DR GO; GO:0032467; P:positive regulation of cytokinesis; IMP:UniProtKB.
DR InterPro; IPR026708; CSPP1.
DR PANTHER; PTHR21616; PTHR21616; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Ciliopathy; Coiled coil; Cytoplasm; Cytoskeleton;
KW Joubert syndrome; Microtubule; Phosphoprotein; Reference proteome.
FT CHAIN 1..1256
FT /note="Centrosome and spindle pole-associated protein 1"
FT /id="PRO_0000293464"
FT REGION 189..244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 381..403
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 735..757
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 813..853
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 913..932
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1114..1147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1232..1256
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 38..62
FT /evidence="ECO:0000255"
FT COILED 114..135
FT /evidence="ECO:0000255"
FT COILED 244..270
FT /evidence="ECO:0000255"
FT COILED 417..449
FT /evidence="ECO:0000255"
FT COILED 625..669
FT /evidence="ECO:0000255"
FT COILED 925..964
FT /evidence="ECO:0000255"
FT COMPBIAS 189..214
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 218..235
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 381..401
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 735..751
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 244
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 459
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 527
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 901
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 920
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 966
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..329
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15580290"
FT /id="VSP_026475"
FT VAR_SEQ 138..172
FT /note="Missing (in isoform 1)"
FT /evidence="ECO:0000303|PubMed:16826565"
FT /id="VSP_040072"
FT VAR_SEQ 689..740
FT /note="TDLNRMHRQNIDAYHNPDARTYEDKRAVVSLDPNLATSNAENLEDAANKSSG
FT -> S (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15580290"
FT /id="VSP_026476"
FT VARIANT 907
FT /note="R -> H (in dbSNP:rs16933182)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_033045"
FT VARIANT 1135
FT /note="W -> R (in dbSNP:rs1808140)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_047014"
FT CONFLICT 855
FT /note="E -> G (in Ref. 1; CAE47426 and 2; CAJ42307)"
FT /evidence="ECO:0000305"
FT CONFLICT 860
FT /note="Q -> E (in Ref. 5; AAH22867)"
FT /evidence="ECO:0000305"
FT CONFLICT 905
FT /note="I -> T (in Ref. 1; CAE47426 and 2; CAJ42307)"
FT /evidence="ECO:0000305"
FT CONFLICT 955
FT /note="R -> K (in Ref. 1; CAE47426 and 2; CAJ42307)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1256 AA; 145522 MW; 81AA10E05F7A5A71 CRC64;
MLFPLQVAAV TSSVRDDPLE HCVSPRTRAR SPEICKMADN LDEFIEEQKA RLAEDKAELE
SDPPYMEMKG KLSAKLSENS KILISMAKEN IPPNSQQTRG SLGIDYGLSL PLGEDYERKK
HKLKEELRQD YRRYLTQGIT QGKRKKNFLS TSETDPSTLG VSLPIGERLS AKERLKLERN
KEYNQFLRGK EESSEKFRQV EKSTEPKSQR NKKPIGQVKP DLTSQIQTSC ENSEGPRKDV
LTPSEAYEEL LNQRRLEEDR YRQLDDEIEL RNRRIIKKAN EEVGISNLKH QRFASKAGIP
DRRFHRFNED RVFDRRYHRP DQDPEVSEEM DERFRYESDF DRRLSRVYTN DRMHRNKRGN
MPPMEHDGDV IEQSNIRISS AENKSAPDNE TSKSANQDTC SPFAGMLFGG EDRELIQRRK
EKYRLELLEQ MAEQQRNKRR EKDLELRVAA SGAQDPEKSP DRLKQFSVAP RHFEEMIPPE
RPRIAFQTPL PPLSAPSVPP IPSVHPVPSQ NEDLRSGLSS ALGEMVSPRI APLPPPPLLP
PLATNYRTPY DDAYYFYGSR NTFDPSLAYY GSGMMGVQPA AYVSAPVTHQ LAQPVVNTVG
QNELKITSDQ VINSGLIFED KPKPSKQSLQ SYQEALQQQI REREERRKKE REEKEEYEAK
LEAEMRTYNP WGKGGGGAPL RDAKGNLITD LNRMHRQNID AYHNPDARTY EDKRAVVSLD
PNLATSNAEN LEDAANKSSG HMQTQSSPFA RGNVFGEPPT ELQIKQQELY KNFLRFQIEE
KKQREEAERE RLRIAEEKEE RRLAEQRARI QQEYEEEQEK KREKEEEQRL KNEEHIRLAE
ERQKEAERKK KEEEEKYNLQ LQHYCERDNL IGEETKHMRQ PSPIVPALQN KIASKLQRPP
SVDSIIRSFI HESSMSRAQS PPVPARKNQL RAEEEKKNVI MELSEMRKQL RSEERRLQER
LLHMDSDDEI PIRKKERNPM DIFDMARHRL QAPVRRQSPK GLDAATFQNV HDFNELKDRD
SETRVDLKFM YLDPPRDHHT LEIQQQALLR EQQKRLNRIK MQEGAKVDLD AIPSAKVREQ
RMPRDDTSDF LKNSLLESDS AFIGAYGETY PAIEDDVLPP PSQLPSARER RRNKWKGLDI
DSSRPNVAPD GLSLKSISSV NVDELRVRNE ERMRRLNEFH NKPINTDDES SLVDPDDIMK
HIGDDGSNSV ATEPWLRPGT SETLKRFMAE QLNQEQQQIP GKPGTFTWQG LSTAHG
