KTU_HUMAN
ID KTU_HUMAN Reviewed; 837 AA.
AC Q9NVR5; B9WS54; C0JAP7; Q86TR1; Q86TY8; Q969Z5;
DT 26-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 2.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Protein kintoun {ECO:0000255|HAMAP-Rule:MF_03069};
DE AltName: Full=Dynein assembly factor 2, axonemal {ECO:0000255|HAMAP-Rule:MF_03069};
GN Name=DNAAF2 {ECO:0000255|HAMAP-Rule:MF_03069};
GN Synonyms=C14orf104, KTU {ECO:0000255|HAMAP-Rule:MF_03069};
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], INVOLVEMENT IN CILD10, AND SUBCELLULAR
RP LOCATION.
RX PubMed=19052621; DOI=10.1038/nature07471;
RA Omran H., Kobayashi D., Olbrich H., Tsukahara T., Loges N.T., Hagiwara H.,
RA Zhang Q., Leblond G., O'Toole E., Hara C., Mizuno H., Kawano H.,
RA Fliegauf M., Yagi T., Koshida S., Miyawaki A., Zentgraf H., Seithe H.,
RA Reinhardt R., Watanabe Y., Kamiya R., Mitchell D.R., Takeda H.;
RT "Ktu/PF13 is required for cytoplasmic pre-assembly of axonemal dyneins.";
RL Nature 456:611-616(2008).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-424, AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 396-837 (ISOFORM 2).
RC TISSUE=Neuroblastoma;
RA Li W.B., Gruber C., Jessee J., Polayes D.;
RT "Full-length cDNA libraries and normalization.";
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 379-837 (ISOFORM 1).
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12508121; DOI=10.1038/nature01348;
RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H.,
RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J.,
RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 386-837 (ISOFORM 2).
RC TISSUE=Bone marrow, and Colon;
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=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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-461 AND SER-467, 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 [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-640; SER-641 AND SER-773, 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-773, 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 [11]
RP INTERACTION WITH DNAAF4.
RX PubMed=23872636; DOI=10.1038/ng.2707;
RA Tarkar A., Loges N.T., Slagle C.E., Francis R., Dougherty G.W.,
RA Tamayo J.V., Shook B., Cantino M., Schwartz D., Jahnke C., Olbrich H.,
RA Werner C., Raidt J., Pennekamp P., Abouhamed M., Hjeij R., Kohler G.,
RA Griese M., Li Y., Lemke K., Klena N., Liu X., Gabriel G., Tobita K.,
RA Jaspers M., Morgan L.C., Shapiro A.J., Letteboer S.J., Mans D.A.,
RA Carson J.L., Leigh M.W., Wolf W.E., Chen S., Lucas J.S., Onoufriadis A.,
RA Plagnol V., Schmidts M., Boldt K., Roepman R., Zariwala M.A., Lo C.W.,
RA Mitchison H.M., Knowles M.R., Burdine R.D., Loturco J.J., Omran H.;
RT "DYX1C1 is required for axonemal dynein assembly and ciliary motility.";
RL Nat. Genet. 45:995-1003(2013).
RN [12]
RP INVOLVEMENT IN CILD10.
RX PubMed=25186273; DOI=10.1183/09031936.00052014;
RA Raidt J., Wallmeier J., Hjeij R., Onnebrink J.G., Pennekamp P., Loges N.T.,
RA Olbrich H., Haeffner K., Dougherty G.W., Omran H., Werner C.;
RT "Ciliary beat pattern and frequency in genetic variants of primary ciliary
RT dyskinesia.";
RL Eur. Respir. J. 44:1579-1588(2014).
RN [13]
RP INTERACTION WITH DNAAF6.
RX PubMed=28041644; DOI=10.1016/j.ajhg.2016.11.019;
RA Paff T., Loges N.T., Aprea I., Wu K., Bakey Z., Haarman E.G., Daniels J.M.,
RA Sistermans E.A., Bogunovic N., Dougherty G.W., Hoeben I.M.,
RA Grosse-Onnebrink J., Matter A., Olbrich H., Werner C., Pals G.,
RA Schmidts M., Omran H., Micha D.;
RT "Mutations in PIH1D3 Cause X-Linked Primary Ciliary Dyskinesia with Outer
RT and Inner Dynein Arm Defects.";
RL Am. J. Hum. Genet. 100:160-168(2017).
RN [14]
RP INTERACTION WITH CFAP300.
RX PubMed=29727693; DOI=10.1016/j.ajhg.2018.03.025;
RA Hoeben I.M., Hjeij R., Olbrich H., Dougherty G.W., Noethe-Menchen T.,
RA Aprea I., Frank D., Pennekamp P., Dworniczak B., Wallmeier J., Raidt J.,
RA Nielsen K.G., Philipsen M.C., Santamaria F., Venditto L., Amirav I.,
RA Mussaffi H., Prenzel F., Wu K., Bakey Z., Schmidts M., Loges N.T.,
RA Omran H.;
RT "Mutations in C11orf70 cause primary ciliary dyskinesia with randomization
RT of left/right body asymmetry due to defects of outer and inner dynein
RT arms.";
RL Am. J. Hum. Genet. 102:973-984(2018).
CC -!- FUNCTION: Required for cytoplasmic pre-assembly of axonemal dyneins,
CC thereby playing a central role in motility in cilia and flagella.
CC Involved in pre-assembly of dynein arm complexes in the cytoplasm
CC before intraflagellar transport loads them for the ciliary compartment.
CC {ECO:0000255|HAMAP-Rule:MF_03069}.
CC -!- SUBUNIT: Interacts with CFAP300 (PubMed:29727693). Interacts with
CC DNAAF4 (PubMed:23872636). Interacts with DNAAF6/PIH1D3
CC (PubMed:28041644). Interacts with DNAI2 and HSPA1A (By similarity).
CC {ECO:0000255|HAMAP-Rule:MF_03069, ECO:0000269|PubMed:23872636,
CC ECO:0000269|PubMed:28041644, ECO:0000269|PubMed:29727693}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03069,
CC ECO:0000269|PubMed:19052621}. Dynein axonemal particle
CC {ECO:0000250|UniProtKB:B1H1W9}. Note=Localizes in the apical cytoplasm
CC around the gamma-tubulin-positive pericentriolar region, not in the
CC cilia. {ECO:0000255|HAMAP-Rule:MF_03069}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9NVR5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NVR5-2; Sequence=VSP_008390;
CC -!- DISEASE: Ciliary dyskinesia, primary, 10 (CILD10) [MIM:612518]: A
CC disorder characterized by abnormalities of motile cilia. Respiratory
CC infections leading to chronic inflammation and bronchiectasis are
CC recurrent, due to defects in the respiratory cilia; reduced fertility
CC is often observed in male patients due to abnormalities of sperm tails.
CC Half of the patients exhibit randomization of left-right body asymmetry
CC and situs inversus, due to dysfunction of monocilia at the embryonic
CC node. Primary ciliary dyskinesia associated with situs inversus is
CC referred to as Kartagener syndrome. {ECO:0000269|PubMed:19052621,
CC ECO:0000269|PubMed:25186273}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to exon skipping. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the PIH1 family. Kintoun subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_03069}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA91684.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAD66572.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; FJ158843; ACN30493.1; -; mRNA.
DR EMBL; BX248264; CAD62592.1; -; mRNA.
DR EMBL; BX248765; CAD66572.1; ALT_INIT; mRNA.
DR EMBL; AK001425; BAA91684.1; ALT_INIT; mRNA.
DR EMBL; AL139099; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC013322; AAH13322.2; -; mRNA.
DR EMBL; BC011400; AAH11400.2; -; mRNA.
DR CCDS; CCDS45100.1; -. [Q9NVR5-2]
DR CCDS; CCDS9691.2; -. [Q9NVR5-1]
DR RefSeq; NP_001077377.1; NM_001083908.1. [Q9NVR5-2]
DR RefSeq; NP_060609.2; NM_018139.2. [Q9NVR5-1]
DR AlphaFoldDB; Q9NVR5; -.
DR SMR; Q9NVR5; -.
DR BioGRID; 120471; 98.
DR ComplexPortal; CPX-6152; R2SD co-chaperone complex.
DR CORUM; Q9NVR5; -.
DR DIP; DIP-59041N; -.
DR IntAct; Q9NVR5; 72.
DR MINT; Q9NVR5; -.
DR STRING; 9606.ENSP00000298292; -.
DR GlyGen; Q9NVR5; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9NVR5; -.
DR MetOSite; Q9NVR5; -.
DR PhosphoSitePlus; Q9NVR5; -.
DR BioMuta; DNAAF2; -.
DR DMDM; 224471834; -.
DR EPD; Q9NVR5; -.
DR jPOST; Q9NVR5; -.
DR MassIVE; Q9NVR5; -.
DR MaxQB; Q9NVR5; -.
DR PaxDb; Q9NVR5; -.
DR PeptideAtlas; Q9NVR5; -.
DR PRIDE; Q9NVR5; -.
DR ProteomicsDB; 82849; -. [Q9NVR5-1]
DR ProteomicsDB; 82850; -. [Q9NVR5-2]
DR Antibodypedia; 139; 36 antibodies from 13 providers.
DR DNASU; 55172; -.
DR Ensembl; ENST00000298292.13; ENSP00000298292.8; ENSG00000165506.15. [Q9NVR5-1]
DR Ensembl; ENST00000406043.3; ENSP00000384862.3; ENSG00000165506.15. [Q9NVR5-2]
DR GeneID; 55172; -.
DR KEGG; hsa:55172; -.
DR MANE-Select; ENST00000298292.13; ENSP00000298292.8; NM_018139.3; NP_060609.2.
DR UCSC; uc001wws.4; human. [Q9NVR5-1]
DR CTD; 55172; -.
DR DisGeNET; 55172; -.
DR GeneCards; DNAAF2; -.
DR GeneReviews; DNAAF2; -.
DR HGNC; HGNC:20188; DNAAF2.
DR HPA; ENSG00000165506; Low tissue specificity.
DR MalaCards; DNAAF2; -.
DR MIM; 612517; gene.
DR MIM; 612518; phenotype.
DR neXtProt; NX_Q9NVR5; -.
DR OpenTargets; ENSG00000165506; -.
DR Orphanet; 244; Primary ciliary dyskinesia.
DR PharmGKB; PA134910310; -.
DR VEuPathDB; HostDB:ENSG00000165506; -.
DR eggNOG; KOG4356; Eukaryota.
DR GeneTree; ENSGT00510000048466; -.
DR HOGENOM; CLU_018349_0_0_1; -.
DR InParanoid; Q9NVR5; -.
DR OMA; KQCMSLT; -.
DR OrthoDB; 943252at2759; -.
DR PhylomeDB; Q9NVR5; -.
DR TreeFam; TF336215; -.
DR PathwayCommons; Q9NVR5; -.
DR SignaLink; Q9NVR5; -.
DR BioGRID-ORCS; 55172; 20 hits in 1080 CRISPR screens.
DR ChiTaRS; DNAAF2; human.
DR GeneWiki; C14orf104; -.
DR GenomeRNAi; 55172; -.
DR Pharos; Q9NVR5; Tbio.
DR PRO; PR:Q9NVR5; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; Q9NVR5; protein.
DR Bgee; ENSG00000165506; Expressed in bronchial epithelial cell and 199 other tissues.
DR Genevisible; Q9NVR5; HS.
DR GO; GO:0101031; C:chaperone complex; IPI:ComplexPortal.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0120293; C:dynein axonemal particle; ISS:UniProtKB.
DR GO; GO:0005576; C:extracellular region; IEA:GOC.
DR GO; GO:0070286; P:axonemal dynein complex assembly; IMP:UniProtKB.
DR GO; GO:0060285; P:cilium-dependent cell motility; IMP:UniProtKB.
DR GO; GO:0003351; P:epithelial cilium movement involved in extracellular fluid movement; IBA:GO_Central.
DR GO; GO:0061966; P:establishment of left/right asymmetry; IEA:Ensembl.
DR GO; GO:0051649; P:establishment of localization in cell; IEA:Ensembl.
DR GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR GO; GO:0036159; P:inner dynein arm assembly; IEA:Ensembl.
DR GO; GO:0036158; P:outer dynein arm assembly; IEA:Ensembl.
DR GO; GO:0050821; P:protein stabilization; IC:ComplexPortal.
DR GO; GO:0032526; P:response to retinoic acid; IEA:Ensembl.
DR HAMAP; MF_03069; Kintoun; 1.
DR InterPro; IPR034727; Kintoun.
DR InterPro; IPR012981; PIH1_N.
DR InterPro; IPR041442; PIH1D1/2/3_CS-like.
DR Pfam; PF08190; PIH1; 1.
DR Pfam; PF18201; PIH1_CS; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Ciliopathy; Cytoplasm; Kartagener syndrome;
KW Phosphoprotein; Primary ciliary dyskinesia; Reference proteome.
FT CHAIN 1..837
FT /note="Protein kintoun"
FT /id="PRO_0000089911"
FT REGION 100..119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 205..224
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 230..249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 363..515
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 210..224
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 230..248
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 465..487
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 461
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 467
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 640
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 641
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 773
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT VAR_SEQ 622..669
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.2"
FT /id="VSP_008390"
FT VARIANT 62
FT /note="E -> D (in dbSNP:rs2985684)"
FT /id="VAR_057788"
FT VARIANT 768
FT /note="D -> G (in dbSNP:rs9989177)"
FT /id="VAR_024309"
FT CONFLICT 403
FT /note="C -> G (in Ref. 5; AAH13322)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 837 AA; 91114 MW; 55C2F2F709F55FFC CRC64;
MAKAAASSSL EDLDLSGEEV QRLTSAFQDP EFRRMFSQYA EELTDPENRR RYEAEITALE
RERGVEVRFV HPEPGHVLRT SLDGARRCFV NVCSNALVGA PSSRPGSGGD RGAAPGSHWS
LPYSLAPGRE YAGRSSSRYM VYDVVFHPDA LALARRHEGF RQMLDATALE AVEKQFGVKL
DRRNAKTLKA KYKGTPEAAV LRTPLPGVIP ARPDGEPKGP LPDFPYPYQY PAAPGPRAPS
PPEAALQPAP TEPRYSVVQR HHVDLQDYRC SRDSAPSPVP HELVITIELP LLRSAEQAAL
EVTRKLLCLD SRKPDYRLRL SLPYPVDDGR GKAQFNKARR QLVVTLPVVL PAARREPAVA
VAAAAPEESA DRSGTDGQAC ASAREGEAGP ARSRAEDGGH DTCVAGAAGS GVTTLGDPEV
APPPAAAGEE RVPKPGEQDL SRHAGSPPGS VEEPSPGGEN SPGGGGSPCL SSRSLAWGSS
AGRESARGDS SVETREESEG TGGQRSACAM GGPGTKSGEP LCPPLLCNQD KETLTLLIQV
PRIQPQSLQG DLNPLWYKLR FSAQDLVYSF FLQFAPENKL STTEPVISIS SNNAVIELAK
SPESHGHWRE WYYGVNNDSL EERLFVNEEN VNEFLEEVLS SPFKQSMSLT PPLIEVLQVT
DNKIQINAKL QECSNSDQLQ GKEERVNEES HLTEKEYIEH CNTPTTDSDS SIAVKALQID
SFGLVTCFQQ ESLDVSQMIL GKSQQPESKM QSEFIKEKSA TCSNEEKDNL NESVITEEKE
TDGDHLSSLL NKTTVHNIPG FDSIKETNMQ DGSVQVIKDH VTNCAFSFQN SLLYDLD
