MYZAP_HUMAN
ID MYZAP_HUMAN Reviewed; 466 AA.
AC P0CAP1; D2E9U7; Q6EER8; Q6EES2; Q6EEV3; Q6EF00; Q6EF01; Q6EF02; Q6EF46;
AC Q6EFN8; Q6EM48; Q6K046; Q6K050; Q6K051; Q6ZQZ3; Q8NC58; Q8NCF3; Q96DI5;
AC Q96JB7; Q96NF5;
DT 26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Myocardial zonula adherens protein;
DE AltName: Full=GRINL1A upstream protein;
DE Short=Gup;
DE Flags: Precursor;
GN Name=MYZAP; Synonyms=MYOZAP;
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] (ISOFORMS 1; 2; 3; 4; 5; 6; 7; 8; 9; 10 AND 11),
RP AND TISSUE SPECIFICITY.
RC TISSUE=Brain, and Lung;
RX PubMed=15233991; DOI=10.1016/j.ygeno.2004.04.004;
RA Roginski R.S., Mohan Raj B.K., Birditt B., Rowen L.;
RT "The human GRINL1A gene defines a complex transcription unit, an unusual
RT form of gene organization in eukaryotes.";
RL Genomics 84:265-276(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], VARIANT VAL-277, AND TISSUE SPECIFICITY.
RX PubMed=20093627; DOI=10.1161/circresaha.109.213256;
RA Seeger T.S., Frank D., Rohr C., Will R., Just S., Grund C., Lyon R.,
RA Luedde M., Koegl M., Sheikh F., Rottbauer W., Franke W.W., Katus H.A.,
RA Olson E.N., Frey N.;
RT "Myozap, a novel intercalated disc protein, activates serum response
RT factor-dependent signaling and is required to maintain cardiac function in
RT vivo.";
RL Circ. Res. 106:880-890(2010).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT VAL-277.
RC TISSUE=Heart;
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=16572171; DOI=10.1038/nature04601;
RA Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J.,
RA Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E.,
RA Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B.,
RA Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R.,
RA O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B.,
RA Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S.,
RA Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.;
RT "Analysis of the DNA sequence and duplication history of human chromosome
RT 15.";
RL Nature 440:671-675(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain cortex;
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 [7]
RP INTERACTION WITH GRIN1, AND SUBCELLULAR LOCATION.
RX PubMed=18849881; DOI=10.1097/wnr.0b013e328317f05f;
RA Roginski R.S., Goubaeva F., Mikami M., Fried-Cassorla E., Nair M.R.,
RA Yang J.;
RT "GRINL1A colocalizes with N-methyl D-aspartate receptor NR1 subunit and
RT reduces N-methyl D-aspartate toxicity.";
RL NeuroReport 19:1721-1726(2008).
RN [8]
RP INTERACTION WITH DYNLL1, AND MUTAGENESIS OF GLN-436; ARG-448 AND TYR-450.
RX PubMed=20412299; DOI=10.1111/j.1742-4658.2010.07649.x;
RA Garcia-Mayoral M.F., Martinez-Moreno M., Albar J.P., Rodriguez-Crespo I.,
RA Bruix M.;
RT "Structural basis for the interaction between dynein light chain 1 and the
RT glutamate channel homolog GRINL1A.";
RL FEBS J. 277:2340-2350(2010).
RN [9]
RP TISSUE SPECIFICITY.
RX PubMed=29034528; DOI=10.1111/ced.13214;
RA Abreu-Velez A.M., Valencia-Yepes C.A., Upegui-Zapata Y.A.,
RA Upegui-Quiceno E., Mesa-Herrera N.R., Velazquez-Velez J.E., Howard M.S.;
RT "Patients with a new variant of endemic pemphigus foliaceus have
RT autoantibodies against arrector pili muscle, colocalizing with MYZAP,
RT p0071, desmoplakins 1 and 2 and ARVCF.";
RL Clin. Exp. Dermatol. 42:874-880(2017).
RN [10]
RP STRUCTURE BY NMR OF 70-79 IN COMPLEX WITH TJP1, SUBCELLULAR LOCATION, AND
RP INTERACTION WITH TJP1.
RX PubMed=21240187; DOI=10.1038/emboj.2010.353;
RA Huo L., Wen W., Wang R., Kam C., Xia J., Feng W., Zhang M.;
RT "Cdc42-dependent formation of the ZO-1/MRCKbeta complex at the leading edge
RT controls cell migration.";
RL EMBO J. 30:665-678(2011).
CC -!- FUNCTION: Plays a role in cellular signaling via Rho-related GTP-
CC binding proteins and subsequent activation of transcription factor SRF
CC (By similarity). Targets TJP1 to cell junctions. In cortical neurons,
CC may play a role in glutaminergic signal transduction through
CC interaction with the NMDA receptor subunit GRIN1 (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts with DSP, MPRIP and TJP1/ZO1. Interaction with MPRIP
CC inhibits the activation of transcription factor SRF (By similarity).
CC Interacts with GRIN1. Interacts with DYNLL1. {ECO:0000250,
CC ECO:0000269|PubMed:18849881, ECO:0000269|PubMed:20412299,
CC ECO:0000269|PubMed:21240187}.
CC -!- INTERACTION:
CC P0CAP1; P63167: DYNLL1; NbExp=6; IntAct=EBI-7929343, EBI-349105;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q5EB94}. Cell membrane
CC {ECO:0000250|UniProtKB:Q5EB94}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q5EB94}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:Q5EB94}. Cytoplasm, myofibril, sarcomere, I band
CC {ECO:0000250|UniProtKB:Q5EB94}. Cytoplasm, myofibril, sarcomere, Z line
CC {ECO:0000250|UniProtKB:Q5EB94}. Cell junction
CC {ECO:0000269|PubMed:18849881, ECO:0000269|PubMed:21240187}.
CC Note=Detected predominantly at the intercalated disk in cardiomyocytes,
CC and at low levels on sarcomeric Z disks. Colocalizes with F-actin.
CC Colocalizes with cortical actin. {ECO:0000250|UniProtKB:Q5EB94}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=11;
CC Comment=Additional isoforms seem to exist.;
CC Name=1; Synonyms=Gcom8, Gup1;
CC IsoId=P0CAP1-1; Sequence=Displayed;
CC Name=2; Synonyms=Gcom2;
CC IsoId=P0CAP1-2; Sequence=VSP_037398;
CC Name=3; Synonyms=Gcom13;
CC IsoId=P0CAP1-3; Sequence=VSP_037390;
CC Name=4; Synonyms=Gcom9, Gup2;
CC IsoId=P0CAP1-4; Sequence=VSP_037392;
CC Name=5; Synonyms=Gcom10;
CC IsoId=P0CAP1-5; Sequence=VSP_037393;
CC Name=6; Synonyms=Gcom3;
CC IsoId=P0CAP1-6; Sequence=VSP_037394;
CC Name=7; Synonyms=Gcom4;
CC IsoId=P0CAP1-7; Sequence=VSP_037395;
CC Name=8; Synonyms=Gcom5;
CC IsoId=P0CAP1-8; Sequence=VSP_037391;
CC Name=9; Synonyms=Gcom6;
CC IsoId=P0CAP1-9; Sequence=VSP_037390, VSP_037392, VSP_037396;
CC Name=10; Synonyms=Gcom11;
CC IsoId=P0CAP1-10; Sequence=VSP_037389;
CC Name=11; Synonyms=Gcom1, GRINL1A complex locus protein 1;
CC IsoId=P0CAP1-11; Sequence=VSP_037397;
CC -!- TISSUE SPECIFICITY: Detected in heart, liver, skeletal muscle,
CC placenta, small intestine, lung, prostate and testis. Expressed in
CC arrector pili muscle (at protein level) (PubMed:29034528).
CC {ECO:0000269|PubMed:15233991, ECO:0000269|PubMed:20093627,
CC ECO:0000269|PubMed:29034528}.
CC -!- MISCELLANEOUS: The adjacent MYZAP and POLR2M genes are part of a
CC complex transcription unit. The respective transcripts derive from
CC different promoters and are alternatively spliced. In human, some
CC transcripts of the upstream promoter of MYZAP use exons of the
CC downstream POLR2M gene.
CC -!- MISCELLANEOUS: [Isoform 11]: Based on a naturally occurring readthrough
CC transcript which produces a MYZAP-POLR2M fusion protein. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the MYZAP family. {ECO:0000305}.
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DR EMBL; AY207007; AAO39707.1; -; mRNA.
DR EMBL; AY207459; AAP41548.1; -; mRNA.
DR EMBL; AY208913; AAP41549.1; -; mRNA.
DR EMBL; AY237639; AAP75897.1; -; mRNA.
DR EMBL; AY331564; AAQ76825.1; -; mRNA.
DR EMBL; AY333779; AAQ76826.1; -; mRNA.
DR EMBL; AY334560; AAQ76827.1; -; mRNA.
DR EMBL; AY334561; AAQ76828.1; -; mRNA.
DR EMBL; AY334562; AAQ76829.1; -; mRNA.
DR EMBL; AY341345; AAQ76831.1; -; mRNA.
DR EMBL; AY353056; AAQ76832.1; -; mRNA.
DR EMBL; AY353057; AAQ76833.1; -; mRNA.
DR EMBL; AY353058; AAQ76834.1; -; mRNA.
DR EMBL; AY353060; AAQ76836.1; -; mRNA.
DR EMBL; FJ970029; ADA68358.1; -; mRNA.
DR EMBL; AK055535; BAB70944.1; -; mRNA.
DR EMBL; AC025271; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC090651; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471082; EAW77522.1; -; Genomic_DNA.
DR EMBL; CH471082; EAW77527.1; -; Genomic_DNA.
DR EMBL; BC101645; AAI01646.1; -; mRNA.
DR EMBL; BC112148; AAI12149.1; -; mRNA.
DR CCDS; CCDS10162.1; -. [P0CAP1-1]
DR CCDS; CCDS42044.1; -. [P0CAP1-4]
DR RefSeq; NP_001018100.1; NM_001018090.6. [P0CAP1-11]
DR RefSeq; NP_001018101.1; NM_001018091.6. [P0CAP1-2]
DR RefSeq; NP_001018110.1; NM_001018100.4. [P0CAP1-1]
DR RefSeq; NP_001018112.1; NM_001018102.2.
DR RefSeq; NP_689664.3; NM_152451.7. [P0CAP1-4]
DR PDB; 2KXS; NMR; -; A=70-79.
DR PDBsum; 2KXS; -.
DR AlphaFoldDB; P0CAP1; -.
DR SMR; P0CAP1; -.
DR BioGRID; 123498; 131.
DR BioGRID; 126937; 3.
DR BioGRID; 1530817; 1.
DR IntAct; P0CAP1; 3.
DR MINT; P0CAP1; -.
DR STRING; 9606.ENSP00000267853; -.
DR iPTMnet; P0CAP1; -.
DR PhosphoSitePlus; P0CAP1; -.
DR BioMuta; MYZAP; -.
DR DMDM; 238064959; -.
DR jPOST; P0CAP1; -.
DR MassIVE; P0CAP1; -.
DR MaxQB; P0CAP1; -.
DR PaxDb; P0CAP1; -.
DR PeptideAtlas; P0CAP1; -.
DR PRIDE; P0CAP1; -.
DR ProteomicsDB; 52417; -. [P0CAP1-1]
DR ProteomicsDB; 52418; -. [P0CAP1-10]
DR ProteomicsDB; 52419; -. [P0CAP1-11]
DR ProteomicsDB; 52420; -. [P0CAP1-2]
DR ProteomicsDB; 52421; -. [P0CAP1-3]
DR ProteomicsDB; 52422; -. [P0CAP1-4]
DR ProteomicsDB; 52423; -. [P0CAP1-5]
DR ProteomicsDB; 52424; -. [P0CAP1-6]
DR ProteomicsDB; 52425; -. [P0CAP1-7]
DR ProteomicsDB; 52426; -. [P0CAP1-8]
DR ProteomicsDB; 52427; -. [P0CAP1-9]
DR TopDownProteomics; P0CAP1-7; -. [P0CAP1-7]
DR Antibodypedia; 70823; 30 antibodies from 13 providers.
DR DNASU; 81488; -.
DR Ensembl; ENST00000267853.10; ENSP00000267853.5; ENSG00000263155.6. [P0CAP1-1]
DR Ensembl; ENST00000380565.8; ENSP00000369939.4; ENSG00000263155.6. [P0CAP1-4]
DR GeneID; 100820829; -.
DR GeneID; 145781; -.
DR GeneID; 81488; -.
DR KEGG; hsa:100820829; -.
DR KEGG; hsa:145781; -.
DR MANE-Select; ENST00000267853.10; ENSP00000267853.5; NM_001018100.5; NP_001018110.1.
DR UCSC; uc002aei.4; human. [P0CAP1-1]
DR CTD; 100820829; -.
DR CTD; 145781; -.
DR CTD; 81488; -.
DR DisGeNET; 100820829; -.
DR DisGeNET; 145781; -.
DR DisGeNET; 81488; -.
DR GeneCards; MYZAP; -.
DR HGNC; HGNC:43444; MYZAP.
DR HPA; ENSG00000263155; Tissue enriched (heart).
DR MIM; 614071; gene.
DR neXtProt; NX_P0CAP1; -.
DR OpenTargets; ENSG00000137878; -.
DR OpenTargets; ENSG00000263155; -.
DR PharmGKB; PA28986; -.
DR VEuPathDB; HostDB:ENSG00000263155; -.
DR eggNOG; ENOG502QSEE; Eukaryota.
DR GeneTree; ENSGT00950000183065; -.
DR HOGENOM; CLU_022112_0_0_1; -.
DR InParanoid; P0CAP1; -.
DR OMA; RKEQHPD; -.
DR PhylomeDB; P0CAP1; -.
DR PathwayCommons; P0CAP1; -.
DR SignaLink; P0CAP1; -.
DR BioGRID-ORCS; 100820829; 6 hits in 616 CRISPR screens.
DR BioGRID-ORCS; 145781; 17 hits in 622 CRISPR screens.
DR BioGRID-ORCS; 81488; 154 hits in 1035 CRISPR screens.
DR EvolutionaryTrace; P0CAP1; -.
DR GeneWiki; GRINL1A; -.
DR Pharos; P0CAP1; Tdark.
DR PRO; PR:P0CAP1; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; P0CAP1; protein.
DR Bgee; ENSG00000263155; Expressed in left ventricle myocardium and 158 other tissues.
DR ExpressionAtlas; P0CAP1; baseline and differential.
DR Genevisible; P0CAP1; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-SubCell.
DR GO; GO:0030864; C:cortical actin cytoskeleton; IEA:Ensembl.
DR GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; ISS:UniProtKB.
DR GO; GO:0031674; C:I band; ISS:UniProtKB.
DR GO; GO:0030018; C:Z disc; IEA:UniProtKB-SubCell.
DR GO; GO:0035556; P:intracellular signal transduction; ISS:UniProtKB.
DR InterPro; IPR028273; Myozap.
DR PANTHER; PTHR23171:SF2; PTHR23171:SF2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell junction; Cell membrane;
KW Coiled coil; Cytoplasm; Cytoskeleton; Membrane; Reference proteome; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..466
FT /note="Myocardial zonula adherens protein"
FT /id="PRO_0000376013"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 96..142
FT /evidence="ECO:0000255"
FT COILED 174..418
FT /evidence="ECO:0000255"
FT MOTIF 424..425
FT /note="Required for DYNLL1-binding"
FT VAR_SEQ 107..175
FT /note="Missing (in isoform 10)"
FT /evidence="ECO:0000303|PubMed:15233991"
FT /id="VSP_037389"
FT VAR_SEQ 108..138
FT /note="Missing (in isoform 9 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:15233991"
FT /id="VSP_037390"
FT VAR_SEQ 374..466
FT /note="IESLKKKLQQKQLLILQLLEKISFLEGENNELQSRLDYLTETQAKTEVETRE
FT IGVGCDLLPSQTGRTREIVMPSRNYTPYTRVLELTMKKTLT -> VTFSTK (in
FT isoform 8)"
FT /evidence="ECO:0000303|PubMed:15233991"
FT /id="VSP_037391"
FT VAR_SEQ 374..401
FT /note="Missing (in isoform 4 and isoform 9)"
FT /evidence="ECO:0000303|PubMed:15233991"
FT /id="VSP_037392"
FT VAR_SEQ 375..466
FT /note="ESLKKKLQQKQLLILQLLEKISFLEGENNELQSRLDYLTETQAKTEVETREI
FT GVGCDLLPSQTGRTREIVMPSRNYTPYTRVLELTMKKTLT -> MSHELFSRFSLRLFG
FT R (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15233991"
FT /id="VSP_037393"
FT VAR_SEQ 402..466
FT /note="NNELQSRLDYLTETQAKTEVETREIGVGCDLLPSQTGRTREIVMPSRNYTPY
FT TRVLELTMKKTLT -> GRKGLKGRLKMSC (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:15233991"
FT /id="VSP_037394"
FT VAR_SEQ 402..466
FT /note="NNELQSRLDYLTETQAKTEVETREIGVGCDLLPSQTGRTREIVMPSRNYTPY
FT TRVLELTMKKTLT -> VTFSTK (in isoform 7)"
FT /evidence="ECO:0000303|PubMed:15233991"
FT /id="VSP_037395"
FT VAR_SEQ 435..466
FT /note="SQTGRTREIVMPSRNYTPYTRVLELTMKKTLT -> RLPFRQNDSSSHCQKS
FT GSPISSEERRRRDKQHLDDITAARLLPLHHMPTQLLSIEESLALQKQQKQNYEEMQAKL
FT AAQKLAERLNIKMRSYNPEGESSGRYREVRDEDDDWSSDEF (in isoform 11)"
FT /evidence="ECO:0000303|PubMed:15233991"
FT /id="VSP_037397"
FT VAR_SEQ 435..466
FT /note="SQTGRTREIVMPSRNYTPYTRVLELTMKKTLT -> RRCKQSSQRKN (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:15233991"
FT /id="VSP_037398"
FT VAR_SEQ 435..466
FT /note="SQTGRTREIVMPSRNYTPYTRVLELTMKKTLT -> RQSRKFEKVLNEFVQL
FT LPLPHHLLWAFGNVCWRRHFGLLQ (in isoform 9)"
FT /evidence="ECO:0000303|PubMed:15233991"
FT /id="VSP_037396"
FT VARIANT 277
FT /note="A -> V (in dbSNP:rs16977629)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:20093627"
FT /id="VAR_055453"
FT MUTAGEN 436
FT /note="Q->G: No effect on DYNLL1-binding; when associated
FT with G-448."
FT /evidence="ECO:0000269|PubMed:20412299"
FT MUTAGEN 448
FT /note="R->G: No effect on DYNLL1-binding; when associated
FT with G-436."
FT /evidence="ECO:0000269|PubMed:20412299"
FT MUTAGEN 450
FT /note="Y->G: No effect on DYNLL1-binding."
FT /evidence="ECO:0000269|PubMed:20412299"
FT CONFLICT 144..146
FT /note="Missing (in Ref. 2; ADA68358)"
FT /evidence="ECO:0000305"
FT STRAND 70..77
FT /evidence="ECO:0007829|PDB:2KXS"
SQ SEQUENCE 466 AA; 54206 MW; 2A6B9C464B8641B4 CRC64;
MLRSTSTVTL LSGGAARTPG APSRRANVCR LRLTVPPESP VPEQCEKKIE RKEQLLDLSN
GEPTRKLPQG VVYGVVRRSD QNQQKEMVVY GWSTSQLKEE MNYIKDVRAT LEKVRKRMYG
DYDEMRQKIR QLTQELSVSH AQQEYLENHI QTQSSALDRF NAMNSALASD SIGLQKTLVD
VTLENSNIKD QIRNLQQTYE ASMDKLREKQ RQLEVAQVEN QLLKMKVESS QEANAEVMRE
MTKKLYSQYE EKLQEEQRKH SAEKEALLEE TNSFLKAIEE ANKKMQAAEI SLEEKDQRIG
ELDRLIERME KERHQLQLQL LEHETEMSGE LTDSDKERYQ QLEEASASLR ERIRHLDDMV
HCQQKKVKQM VEEIESLKKK LQQKQLLILQ LLEKISFLEG ENNELQSRLD YLTETQAKTE
VETREIGVGC DLLPSQTGRT REIVMPSRNY TPYTRVLELT MKKTLT
