CAMP1_HUMAN
ID CAMP1_HUMAN Reviewed; 1602 AA.
AC Q5T5Y3; A1L4L2; B2REB2; B2REB3; Q70W33; Q8NCY0; Q96E80; Q96FM3; Q9UFJ5;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 2.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Calmodulin-regulated spectrin-associated protein 1;
GN Name=CAMSAP1;
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), FUNCTION, SUBCELLULAR LOCATION, AND
RP DOMAIN CKK.
RC TISSUE=Placenta;
RX PubMed=19508979; DOI=10.1093/molbev/msp115;
RA Baines A.J., Bignone P.A., King M.D.A., Maggs A.M., Bennett P.M.,
RA Pinder J.C., Phillips G.W.;
RT "The CKK domain (DUF1781) binds microtubules and defines the CAMSAP/ssp4
RT family of animal proteins.";
RL Mol. Biol. Evol. 26:2005-2014(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 126-1602 (ISOFORM 3), AND
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 668-1602 (ISOFORM 1).
RC TISSUE=Brain, Eye, and Lung;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 494-789 AND 1217-1602 (ISOFORM
RP 1).
RC TISSUE=Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1537, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-722, 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-371; SER-375; THR-512;
RP SER-575 AND SER-589, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [8]
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-217, 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 [10]
RP FUNCTION.
RX PubMed=21834987; DOI=10.1186/1741-7007-9-54;
RA Bai S.W., Herrera-Abreu M.T., Rohn J.L., Racine V., Tajadura V.,
RA Suryavanshi N., Bechtel S., Wiemann S., Baum B., Ridley A.J.;
RT "Identification and characterization of a set of conserved and new
RT regulators of cytoskeletal organisation, cell morphology and migration.";
RL BMC Biol. 9:54-54(2011).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-416; SER-431; SER-563;
RP SER-629; SER-722; SER-1080 AND SER-1398, AND IDENTIFICATION BY MASS
RP 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 [12]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=24486153; DOI=10.1016/j.devcel.2014.01.001;
RA Jiang K., Hua S., Mohan R., Grigoriev I., Yau K.W., Liu Q., Katrukha E.A.,
RA Altelaar A.F., Heck A.J., Hoogenraad C.C., Akhmanova A.;
RT "Microtubule minus-end stabilization by polymerization-driven CAMSAP
RT deposition.";
RL Dev. Cell 28:295-309(2014).
RN [13]
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 [14]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=24706919; DOI=10.1073/pnas.1404133111;
RA Hendershott M.C., Vale R.D.;
RT "Regulation of microtubule minus-end dynamics by CAMSAPs and Patronin.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:5860-5865(2014).
RN [15]
RP FUNCTION, INTERACTION WITH SPTBN1, AND MUTAGENESIS OF 885-LEU--LYS-888.
RX PubMed=24117850; DOI=10.1111/jnc.12462;
RA King M.D., Phillips G.W., Bignone P.A., Hayes N.V., Pinder J.C.,
RA Baines A.J.;
RT "A conserved sequence in CAMSAP1 (calmodulin regulated spectrin-associated
RT protein 1) links its interaction with spectrin and calmodulin to neurite
RT outgrowth.";
RL J. Neurochem. 128:391-402(2014).
CC -!- FUNCTION: Key microtubule-organizing protein that specifically binds
CC the minus-end of non-centrosomal microtubules and regulates their
CC dynamics and organization (PubMed:19508979, PubMed:21834987,
CC PubMed:24486153, PubMed:24706919, PubMed:24117850). Specifically
CC recognizes growing microtubule minus-ends and stabilizes microtubules
CC (PubMed:24486153, PubMed:24706919). Acts on free microtubule minus-ends
CC that are not capped by microtubule-nucleating proteins or other factors
CC and protects microtubule minus-ends from depolymerization
CC (PubMed:24486153, PubMed:24706919). In contrast to CAMSAP2 and CAMSAP3,
CC tracks along the growing tips of minus-end microtubules without
CC significantly affecting the polymerization rate: binds at the very tip
CC of the microtubules minus-end and acts as a minus-end tracking protein
CC (-TIP) that dissociates from microtubules after allowing tubulin
CC incorporation (PubMed:24486153, PubMed:24706919). Through interaction
CC with spectrin may regulate neurite outgrowth (PubMed:24117850).
CC {ECO:0000269|PubMed:19508979, ECO:0000269|PubMed:21834987,
CC ECO:0000269|PubMed:24117850, ECO:0000269|PubMed:24486153,
CC ECO:0000269|PubMed:24706919}.
CC -!- SUBUNIT: Interacts with spectrin via SPTBN1; the interaction is direct
CC (PubMed:24117850). Interacts with calmodulin; calcium-dependent it
CC prevents interaction with spectrin (PubMed:24117850).
CC {ECO:0000269|PubMed:24117850}.
CC -!- INTERACTION:
CC Q5T5Y3-3; P78358: CTAG1B; NbExp=3; IntAct=EBI-12036363, EBI-1188472;
CC Q5T5Y3-3; P31321: PRKAR1B; NbExp=6; IntAct=EBI-12036363, EBI-2805516;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:19508979}. Note=Associates with the minus-end of
CC microtubules (PubMed:24486153, PubMed:24706919). In contrast to CAMSAP2
CC and CAMSAP3, does not form stretches of decorated microtubule minus-
CC ends (PubMed:24486153, PubMed:24706919). {ECO:0000269|PubMed:19508979,
CC ECO:0000269|PubMed:24486153, ECO:0000269|PubMed:24706919}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q5T5Y3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5T5Y3-2; Sequence=VSP_030800;
CC Name=3;
CC IsoId=Q5T5Y3-3; Sequence=VSP_030801;
CC -!- DOMAIN: The CKK domain binds microtubules. {ECO:0000255|PROSITE-
CC ProRule:PRU00841, ECO:0000269|PubMed:19508979}.
CC -!- SIMILARITY: Belongs to the CAMSAP1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00841}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI30581.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AJ519841; CAD58627.1; -; mRNA.
DR EMBL; AL158822; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL353636; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL355574; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC010646; AAH10646.1; -; mRNA.
DR EMBL; BC012778; AAH12778.2; -; mRNA.
DR EMBL; BC130580; AAI30581.1; ALT_INIT; mRNA.
DR EMBL; AL117634; CAB56024.2; -; mRNA.
DR EMBL; AL834528; CAD39184.1; -; mRNA.
DR CCDS; CCDS35176.2; -. [Q5T5Y3-1]
DR PIR; T17334; T17334.
DR RefSeq; NP_056262.3; NM_015447.3. [Q5T5Y3-1]
DR RefSeq; XP_005263453.1; XM_005263396.3. [Q5T5Y3-3]
DR RefSeq; XP_005263454.1; XM_005263397.1. [Q5T5Y3-2]
DR PDB; 5M54; EM; 8.00 A; C=1473-1589.
DR PDB; 5M5C; EM; 4.80 A; C=1472-1589.
DR PDB; 6QUS; EM; 3.70 A; I=1462-1602.
DR PDB; 6QVJ; EM; 3.80 A; I=1462-1602.
DR PDBsum; 5M54; -.
DR PDBsum; 5M5C; -.
DR PDBsum; 6QUS; -.
DR PDBsum; 6QVJ; -.
DR AlphaFoldDB; Q5T5Y3; -.
DR SMR; Q5T5Y3; -.
DR BioGRID; 127632; 66.
DR IntAct; Q5T5Y3; 37.
DR MINT; Q5T5Y3; -.
DR STRING; 9606.ENSP00000374183; -.
DR iPTMnet; Q5T5Y3; -.
DR MetOSite; Q5T5Y3; -.
DR PhosphoSitePlus; Q5T5Y3; -.
DR BioMuta; CAMSAP1; -.
DR DMDM; 166991445; -.
DR EPD; Q5T5Y3; -.
DR jPOST; Q5T5Y3; -.
DR MassIVE; Q5T5Y3; -.
DR MaxQB; Q5T5Y3; -.
DR PaxDb; Q5T5Y3; -.
DR PeptideAtlas; Q5T5Y3; -.
DR PRIDE; Q5T5Y3; -.
DR ProteomicsDB; 64558; -. [Q5T5Y3-1]
DR ProteomicsDB; 64559; -. [Q5T5Y3-2]
DR ProteomicsDB; 64560; -. [Q5T5Y3-3]
DR Antibodypedia; 18656; 130 antibodies from 19 providers.
DR Ensembl; ENST00000312405.10; ENSP00000312463.6; ENSG00000130559.19. [Q5T5Y3-2]
DR Ensembl; ENST00000389532.9; ENSP00000374183.4; ENSG00000130559.19. [Q5T5Y3-1]
DR Ensembl; ENST00000409386.3; ENSP00000386420.3; ENSG00000130559.19. [Q5T5Y3-3]
DR GeneID; 157922; -.
DR KEGG; hsa:157922; -.
DR MANE-Select; ENST00000389532.9; ENSP00000374183.4; NM_015447.4; NP_056262.3.
DR UCSC; uc004cgr.5; human. [Q5T5Y3-1]
DR CTD; 157922; -.
DR DisGeNET; 157922; -.
DR GeneCards; CAMSAP1; -.
DR HGNC; HGNC:19946; CAMSAP1.
DR HPA; ENSG00000130559; Tissue enhanced (retina).
DR MIM; 613774; gene.
DR neXtProt; NX_Q5T5Y3; -.
DR OpenTargets; ENSG00000130559; -.
DR PharmGKB; PA134866541; -.
DR VEuPathDB; HostDB:ENSG00000130559; -.
DR eggNOG; KOG3654; Eukaryota.
DR GeneTree; ENSGT00950000182975; -.
DR HOGENOM; CLU_004833_1_0_1; -.
DR InParanoid; Q5T5Y3; -.
DR OMA; PHMAMID; -.
DR OrthoDB; 741937at2759; -.
DR PhylomeDB; Q5T5Y3; -.
DR TreeFam; TF315529; -.
DR PathwayCommons; Q5T5Y3; -.
DR SignaLink; Q5T5Y3; -.
DR BioGRID-ORCS; 157922; 7 hits in 1076 CRISPR screens.
DR ChiTaRS; CAMSAP1; human.
DR GenomeRNAi; 157922; -.
DR Pharos; Q5T5Y3; Tbio.
DR PRO; PR:Q5T5Y3; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q5T5Y3; protein.
DR Bgee; ENSG00000130559; Expressed in secondary oocyte and 199 other tissues.
DR ExpressionAtlas; Q5T5Y3; baseline and differential.
DR Genevisible; Q5T5Y3; HS.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005874; C:microtubule; IDA:UniProtKB.
DR GO; GO:0005516; F:calmodulin binding; ISS:UniProtKB.
DR GO; GO:0008017; F:microtubule binding; IDA:UniProtKB.
DR GO; GO:0051011; F:microtubule minus-end binding; IDA:UniProtKB.
DR GO; GO:0030507; F:spectrin binding; IDA:UniProtKB.
DR GO; GO:0031122; P:cytoplasmic microtubule organization; IBA:GO_Central.
DR GO; GO:0007010; P:cytoskeleton organization; IMP:UniProtKB.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IDA:UniProtKB.
DR GO; GO:0007026; P:negative regulation of microtubule depolymerization; IBA:GO_Central.
DR GO; GO:0031175; P:neuron projection development; IMP:UniProtKB.
DR GO; GO:0022604; P:regulation of cell morphogenesis; IMP:UniProtKB.
DR GO; GO:0031113; P:regulation of microtubule polymerization; IDA:UniProtKB.
DR Gene3D; 3.10.20.360; -; 1.
DR InterPro; IPR032940; CAMSAP.
DR InterPro; IPR022613; CAMSAP-like_CH_dom.
DR InterPro; IPR031372; CAMSAP_CC1.
DR InterPro; IPR001715; CH-domain.
DR InterPro; IPR036872; CH_dom_sf.
DR InterPro; IPR038209; CKK_dom_sf.
DR InterPro; IPR014797; CKK_domain.
DR InterPro; IPR011033; PRC_barrel-like_sf.
DR PANTHER; PTHR21595; PTHR21595; 1.
DR Pfam; PF17095; CAMSAP_CC1; 1.
DR Pfam; PF11971; CAMSAP_CH; 1.
DR Pfam; PF08683; CAMSAP_CKK; 1.
DR SMART; SM01051; CAMSAP_CKK; 1.
DR SUPFAM; SSF47576; SSF47576; 1.
DR SUPFAM; SSF50346; SSF50346; 1.
DR PROSITE; PS50021; CH; 1.
DR PROSITE; PS51508; CKK; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Coiled coil; Cytoplasm; Cytoskeleton;
KW Microtubule; Phosphoprotein; Reference proteome.
FT CHAIN 1..1602
FT /note="Calmodulin-regulated spectrin-associated protein 1"
FT /id="PRO_0000316828"
FT DOMAIN 216..331
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 1463..1597
FT /note="CKK"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00841"
FT REGION 426..471
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 603..637
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 772..808
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 825..870
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 871..892
FT /note="Sufficient for interaction with SPTBN1"
FT /evidence="ECO:0000269|PubMed:24117850"
FT REGION 903..922
FT /note="Sufficient for interaction with calmodulin"
FT REGION 1075..1165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1206..1226
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1301..1448
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 873..909
FT /evidence="ECO:0000255"
FT COILED 1016..1048
FT /evidence="ECO:0000255"
FT COILED 1291..1343
FT /evidence="ECO:0000255"
FT COMPBIAS 432..448
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 605..624
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 772..790
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 791..808
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 825..860
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1301..1350
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1382..1424
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1434..1448
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 217
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 371
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 375
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 416
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 431
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 512
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 563
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 575
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 589
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 629
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 722
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 728
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A2AHC3"
FT MOD_RES 738
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:D3Z8E6"
FT MOD_RES 740
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:D3Z8E6"
FT MOD_RES 1080
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1398
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1427
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A2AHC3"
FT MOD_RES 1537
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:15592455"
FT VAR_SEQ 1..278
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:19508979"
FT /id="VSP_030800"
FT VAR_SEQ 222
FT /note="K -> KSPSKWYWKLVP (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_030801"
FT VARIANT 476
FT /note="A -> V (in dbSNP:rs35639321)"
FT /id="VAR_038398"
FT MUTAGEN 885..888
FT /note="LEEK->AAAA: Loss of interaction with SPTBN1."
FT /evidence="ECO:0000269|PubMed:24117850"
FT CONFLICT 823
FT /note="Q -> H (in Ref. 3; AAH12778)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1602 AA; 177972 MW; 184823C2A151F8A7 CRC64;
MVDASGRAAA EGWRKMEAPP DGAADLVPLD RYDAARAKIA ANLQWICAKA YGRDNIPEDL
RDPFYVDQYE QEHIKPPVIK LLLSSELYCR VCSLILKGDQ VAALQGHQSV IQALSRKGIY
VMESDDTPVT ESDLSRAPIK MSAHMAMVDA LMMAYTVEMI SIEKVVASVK RFSTFSASKE
LPYDLEDAMV FWINKVNLKM REITEKEVKL KQQLLESPAH QKVRYRREHL SARQSPYFPL
LEDLMRDGSD GAALLAVIHY YCPEQMKLDD ICLKEVTSMA DSLYNIRLLR EFSNEYLNKC
FYLTLEDMLY APLVLKPNVM VFIAELFWWF ENVKPDFVQP RDVQELKDAK TVLHQKSSRP
PVPISNATKR SFLGSPAAGT LAELQPPVQL PAEGCHRHYL HPEEPEYLGK GTAAFSPSHP
LLPLRQKQQK SIQGEDIPDQ RHRSNSLTRV DGQPRGAAIA WPEKKTRPAS QPTPFALHHA
ASCEVDPSSG DSISLARSIS KDSLASNIVN LTPQNQPHPT ATKSHGKSLL SNVSIEDEEE
ELVAIVRADV VPQQADPEFP RASPRALGLT ANARSPQGQL DTSESKPDSF FLEPLMPAVL
KPAKEKQVIT KEDERGEGRP RSIVSRRPSE GPQPLVRRKM TGSRDLNRTF TPIPCSEFPM
GIDPTETGPL SVETAGEVCG GPLALGGFDP FPQGPSTDGF FLHVGRADED TEGRLYVSCS
KSPNSHDSEP WTLLRQDSDS DVVDIEEAEH DFMGEAHPVV FSRYIGEEES AKLQEDMKVK
EHEDKDDASG RSSPCLSTAS QMSSVSMASG SVKMTSFAER KLQRLNSCET KSSTSSSQKT
TPDASESCPA PLTTWRQKRE QSPSQHGKDP ASLLASELVQ LHMQLEEKRR AIEAQKKKME
ALSARQRLKL GKAAFLHVVK KGKAEAAPPL RPEHFAKEYS QHNGEDCGDA VSKTEDFLVK
EEQREELLHE PQDVDKESLA FAQQHKAKDP VALHELERNK VISAALLEDT VGEVVDVNEC
DLSIEKLNET ISTLQQAILK ISQQQEQLLM KSPTVPVPGS KNNSQDHKVK APVHFVEPLS
PTGVAGHRKA PRLGQGRNSR SGRPAELKVP KDRPQGSSRS KTPTPSVETL PHLRPFPASS
HPRTPTDPGL DSALEPSGDP HGKCLFDSYR LHDESNQRTL TLSSSKDANI LSEQMSLKEV
LDASVKEVGS SSSDVSGKES VPVEEPLRSR ASLIEVDLSD LKAPDEDGEL VSLDGSADLV
SEGDQKPGVG FFFKDEQKAE DELAKKRAAF LLKQQRKAEE ARVRKQQLEA EVELKRDEAR
RKAEEDRVRK EEEKARRELI KQEYLRRKQQ QILEEQGLGK PKSKPKKPRP KSVHREESCS
DSGTKCSSTP DNLSRTQSGS SLSLASAATT EPESVHSGGT PSQRVESMEA LPILSRNPSR
STDRDWETAS AASSLASVAE YTGPKLFKEP SSKSNKPIIH NAISHCCLAG KVNEPHKNSI
LEELEKCDAN HYIILFRDAG CQFRALYCYY PDTEEIYKLT GTGPKNITKK MIDKLYKYSS
DRKQFNLIPA KTMSVSVDAL TIHNHLWQPK RPAVPKKAQT RK
