CHIN_HUMAN
ID CHIN_HUMAN Reviewed; 459 AA.
AC P15882; A8K1M6; B3KNU6; B4DV19; Q53SD6; Q53SH5; Q96FB0;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2002, sequence version 3.
DT 03-AUG-2022, entry version 217.
DE RecName: Full=N-chimaerin;
DE AltName: Full=A-chimaerin;
DE AltName: Full=Alpha-chimerin;
DE AltName: Full=N-chimerin;
DE Short=NC;
DE AltName: Full=Rho GTPase-activating protein 2;
GN Name=CHN1; Synonyms=ARHGAP2, CHN;
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 ALPHA-1).
RC TISSUE=Retina;
RX PubMed=2299665; DOI=10.1016/0022-2836(90)90006-8;
RA Hall C., Monfries C., Smith P., Lim H.H., Kozma R., Ahmed S.,
RA Vanniasingham V., Leung T., Lim L.;
RT "Novel human brain cDNA encoding a 34,000 Mr protein n-chimaerin, related
RT to both the regulatory domain of protein kinase C and BCR, the product of
RT the breakpoint cluster region gene.";
RL J. Mol. Biol. 211:11-16(1990).
RN [2]
RP SEQUENCE REVISION.
RX PubMed=1445199; DOI=10.1042/bj2870415;
RA Lim H.H., Michael G.J., Smith P., Lim L., Hall C.;
RT "Developmental regulation and neuronal expression of the mRNA of rat n-
RT chimaerin, a p21rac GAP:cDNA sequence.";
RL Biochem. J. 287:415-422(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA-2).
RX PubMed=8336731; DOI=10.1128/mcb.13.8.4986-4998.1993;
RA Hall C., Sin W.C., Teo M., Michael G.J., Smith P., Dong J.M., Lim H.H.,
RA Manser E., Spurr N.K., Jones T.A., Lim L.;
RT "Alpha 2-chimerin, an SH2-containing GTPase-activating protein for the ras-
RT related protein p21rac derived by alternate splicing of the human n-
RT chimerin gene, is selectively expressed in brain regions and testes.";
RL Mol. Cell. Biol. 13:4986-4998(1993).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS ALPHA-1; ALPHA-2 AND 3).
RC TISSUE=Brain, Hippocampus, and Small intestine;
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 GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [6]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA-2).
RC TISSUE=Eye;
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 [8]
RP PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM ALPHA-1).
RC TISSUE=Fibroblast;
RX PubMed=7867622; DOI=10.1111/j.1432-1033.1995.tb20183.x;
RA Dong J.M., Smith P., Hall C., Lim L.;
RT "Promoter region of the transcriptional unit for human alpha 1-chimaerin, a
RT neuron-specific GTPase-activating protein for p21rac.";
RL Eur. J. Biochem. 227:636-646(1995).
RN [9]
RP PHORBOL-ESTER BINDING.
RX PubMed=2268301; DOI=10.1042/bj2720767;
RA Ahmed S., Kozma R., Monfries C., Hall C., Lim H.H., Smith P., Lim L.;
RT "Human brain n-chimaerin cDNA encodes a novel phorbol ester receptor.";
RL Biochem. J. 272:767-773(1990).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-192, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
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 X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 15-459 IN COMPLEX WITH ZINC IONS.
RG Structural genomics consortium (SGC);
RT "Crystal structure of human chimerin 1 (CHN1).";
RL Submitted (JUL-2011) to the PDB data bank.
RN [13]
RP VARIANTS DURS2 PHE-20; MET-126; HIS-143; VAL-223; SER-228; GLN-252 AND
RP LYS-313, AND CHARACTERIZATION OF VARIANTS DURS2 PHE-20; MET-126; HIS-143;
RP VAL-223; SER-228; GLN-252 AND LYS-313.
RX PubMed=18653847; DOI=10.1126/science.1156121;
RA Miyake N., Chilton J., Psatha M., Cheng L., Andrews C., Chan W.-M., Law K.,
RA Crosier M., Lindsay S., Cheung M., Allen J., Gutowski N.J., Ellard S.,
RA Young E., Iannaccone A., Appukuttan B., Stout J.T., Christiansen S.,
RA Ciccarelli M.L., Baldi A., Campioni M., Zenteno J.C., Davenport D.,
RA Mariani L.E., Sahin M., Guthrie S., Engle E.C.;
RT "Human CHN1 mutations hyperactivate alpha2-chimaerin and cause Duane's
RT retraction syndrome.";
RL Science 321:839-843(2008).
CC -!- FUNCTION: GTPase-activating protein for p21-rac and a phorbol ester
CC receptor. Involved in the assembly of neuronal locomotor circuits as a
CC direct effector of EPHA4 in axon guidance.
CC -!- SUBUNIT: Interacts with EPHA4; effector of EPHA4 in axon guidance
CC linking EPHA4 activation to RAC1 regulation. {ECO:0000250}.
CC -!- INTERACTION:
CC P15882; Q8NFD2: ANKK1; NbExp=3; IntAct=EBI-718947, EBI-13280688;
CC P15882; Q9Y5R4: HEMK1; NbExp=8; IntAct=EBI-718947, EBI-10329202;
CC P15882; P28482: MAPK1; NbExp=3; IntAct=EBI-718947, EBI-959949;
CC P15882; O43639: NCK2; NbExp=16; IntAct=EBI-718947, EBI-713635;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=Alpha-2;
CC IsoId=P15882-1; Sequence=Displayed;
CC Name=Alpha-1;
CC IsoId=P15882-2; Sequence=VSP_001636;
CC Name=3;
CC IsoId=P15882-3; Sequence=VSP_043297;
CC -!- TISSUE SPECIFICITY: In neurons in brain regions that are involved in
CC learning and memory processes.
CC -!- DEVELOPMENTAL STAGE: Increases in amount during brain development
CC coincident with synaptogenesis.
CC -!- PTM: Phosphorylated. Phosphorylation is EPHA4 kinase activity-dependent
CC (By similarity). {ECO:0000250}.
CC -!- DISEASE: Duane retraction syndrome 2 (DURS2) [MIM:604356]: A form of
CC Duane retraction syndrome, a congenital eye movement disorder
CC characterized by a failure of cranial nerve VI (the abducens nerve) to
CC develop normally, resulting in restriction or absence of abduction,
CC adduction or both, narrowing of the palpebral fissure, and retraction
CC of the globe on attempted adduction. Undiagnosed in children, it can
CC lead to amblyopia, a permanent uncorrectable loss of vision.
CC {ECO:0000269|PubMed:18653847}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA35769.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; X51408; CAA35769.1; ALT_INIT; mRNA.
DR EMBL; Z22641; CAA80354.1; -; mRNA.
DR EMBL; AK055060; BAG51458.1; -; mRNA.
DR EMBL; AK289941; BAF82630.1; -; mRNA.
DR EMBL; AK300890; BAG62531.1; -; mRNA.
DR EMBL; AC007435; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC018890; AAY14688.1; -; Genomic_DNA.
DR EMBL; AC020596; AAY14940.1; -; Genomic_DNA.
DR EMBL; CH471058; EAX11117.1; -; Genomic_DNA.
DR EMBL; CH471058; EAX11118.1; -; Genomic_DNA.
DR EMBL; CH471058; EAX11119.1; -; Genomic_DNA.
DR EMBL; BC011393; AAH11393.1; -; mRNA.
DR EMBL; S75654; AAB33506.1; -; Genomic_DNA.
DR CCDS; CCDS46454.1; -. [P15882-3]
DR CCDS; CCDS46455.1; -. [P15882-1]
DR CCDS; CCDS56147.1; -. [P15882-2]
DR PIR; A48090; A48090.
DR PIR; I53329; I53329.
DR RefSeq; NP_001020372.2; NM_001025201.3. [P15882-3]
DR RefSeq; NP_001193531.1; NM_001206602.1. [P15882-2]
DR RefSeq; NP_001813.1; NM_001822.5. [P15882-1]
DR PDB; 2OSA; X-ray; 1.80 A; A=260-459.
DR PDB; 3CXL; X-ray; 2.60 A; A=15-459.
DR PDBsum; 2OSA; -.
DR PDBsum; 3CXL; -.
DR AlphaFoldDB; P15882; -.
DR SMR; P15882; -.
DR BioGRID; 107547; 27.
DR DIP; DIP-42177N; -.
DR IntAct; P15882; 15.
DR MINT; P15882; -.
DR STRING; 9606.ENSP00000386741; -.
DR iPTMnet; P15882; -.
DR PhosphoSitePlus; P15882; -.
DR BioMuta; CHN1; -.
DR DMDM; 21903393; -.
DR EPD; P15882; -.
DR jPOST; P15882; -.
DR MassIVE; P15882; -.
DR MaxQB; P15882; -.
DR PaxDb; P15882; -.
DR PeptideAtlas; P15882; -.
DR PRIDE; P15882; -.
DR ProteomicsDB; 53234; -. [P15882-1]
DR ProteomicsDB; 53235; -. [P15882-2]
DR ProteomicsDB; 53236; -. [P15882-3]
DR Antibodypedia; 33886; 451 antibodies from 29 providers.
DR DNASU; 1123; -.
DR Ensembl; ENST00000295497.12; ENSP00000295497.7; ENSG00000128656.15. [P15882-2]
DR Ensembl; ENST00000409156.7; ENSP00000386470.3; ENSG00000128656.15. [P15882-3]
DR Ensembl; ENST00000409900.9; ENSP00000386741.4; ENSG00000128656.15. [P15882-1]
DR GeneID; 1123; -.
DR KEGG; hsa:1123; -.
DR MANE-Select; ENST00000409900.9; ENSP00000386741.4; NM_001822.7; NP_001813.1.
DR UCSC; uc002ujg.4; human. [P15882-1]
DR CTD; 1123; -.
DR DisGeNET; 1123; -.
DR GeneCards; CHN1; -.
DR GeneReviews; CHN1; -.
DR HGNC; HGNC:1943; CHN1.
DR HPA; ENSG00000128656; Group enriched (brain, choroid plexus).
DR MalaCards; CHN1; -.
DR MIM; 118423; gene.
DR MIM; 604356; phenotype.
DR neXtProt; NX_P15882; -.
DR OpenTargets; ENSG00000128656; -.
DR Orphanet; 233; Duane retraction syndrome.
DR PharmGKB; PA26473; -.
DR VEuPathDB; HostDB:ENSG00000128656; -.
DR eggNOG; KOG1453; Eukaryota.
DR GeneTree; ENSGT01030000234635; -.
DR HOGENOM; CLU_015883_0_1_1; -.
DR InParanoid; P15882; -.
DR OrthoDB; 1300981at2759; -.
DR PhylomeDB; P15882; -.
DR TreeFam; TF342052; -.
DR PathwayCommons; P15882; -.
DR Reactome; R-HSA-9013148; CDC42 GTPase cycle.
DR Reactome; R-HSA-9013149; RAC1 GTPase cycle.
DR SignaLink; P15882; -.
DR SIGNOR; P15882; -.
DR BioGRID-ORCS; 1123; 15 hits in 1069 CRISPR screens.
DR ChiTaRS; CHN1; human.
DR EvolutionaryTrace; P15882; -.
DR GenomeRNAi; 1123; -.
DR Pharos; P15882; Tbio.
DR PRO; PR:P15882; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; P15882; protein.
DR Bgee; ENSG00000128656; Expressed in middle temporal gyrus and 194 other tissues.
DR ExpressionAtlas; P15882; baseline and differential.
DR Genevisible; P15882; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0046875; F:ephrin receptor binding; IBA:GO_Central.
DR GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0048013; P:ephrin receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0008045; P:motor neuron axon guidance; ISS:UniProtKB.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IEA:InterPro.
DR GO; GO:0050770; P:regulation of axonogenesis; ISS:UniProtKB.
DR GO; GO:0043087; P:regulation of GTPase activity; IBA:GO_Central.
DR GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; TAS:Reactome.
DR CDD; cd00029; C1; 1.
DR CDD; cd04372; RhoGAP_chimaerin; 1.
DR CDD; cd10352; SH2_a2chimerin_b2chimerin; 1.
DR Gene3D; 1.10.555.10; -; 1.
DR Gene3D; 3.30.505.10; -; 1.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR035840; Chimaerin_SH2.
DR InterPro; IPR017356; CHN1/CHN2.
DR InterPro; IPR020454; DAG/PE-bd.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR037860; RhoGAP_chimaerin.
DR InterPro; IPR000198; RhoGAP_dom.
DR InterPro; IPR000980; SH2.
DR InterPro; IPR036860; SH2_dom_sf.
DR Pfam; PF00130; C1_1; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR Pfam; PF00017; SH2; 1.
DR PIRSF; PIRSF038015; N-chimaerin; 1.
DR PRINTS; PR00008; DAGPEDOMAIN.
DR SMART; SM00109; C1; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SMART; SM00252; SH2; 1.
DR SUPFAM; SSF48350; SSF48350; 1.
DR SUPFAM; SSF55550; SSF55550; 1.
DR SUPFAM; SSF57889; SSF57889; 1.
DR PROSITE; PS50238; RHOGAP; 1.
DR PROSITE; PS50001; SH2; 1.
DR PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Disease variant;
KW GTPase activation; Metal-binding; Neurogenesis; Phosphoprotein;
KW Reference proteome; SH2 domain; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330"
FT CHAIN 2..459
FT /note="N-chimaerin"
FT /id="PRO_0000056694"
FT DOMAIN 49..135
FT /note="SH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT DOMAIN 268..459
FT /note="Rho-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT ZN_FING 205..255
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19413330"
FT MOD_RES 192
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 340
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P30337"
FT VAR_SEQ 1..183
FT /note="MALTLFDTDEYRPPVWKSYLYQLQQEAPHPRRITCTCEVENRPKYYGREFHG
FT MISREAADQLLIVAEGSYLIRESQRQPGTYTLALRFGSQTRNFRLYYDGKHFVGEKRFE
FT SIHDLVTDGLITLYIETKAAEYIAKMTINPIYEHVGYTTLNREPAYKKHMPVLKETHDE
FT RDSTGQDGVSEKR -> MPSKESWSGRKTNRAAVHKSKQEGRQQDLLIAALGMKLGSPK
FT SSVTIWQPLKLFAYSQ (in isoform Alpha-1)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:2299665"
FT /id="VSP_001636"
FT VAR_SEQ 184..209
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043297"
FT VARIANT 20
FT /note="L -> F (in DURS2; behaves as a dominant gain-of-
FT function allele that increases CHN1 activity in vitro;
FT appears to enhance membrane translocation and CHN1 activity
FT by destabilizing the closed conformation of CHN1 protein in
FT response to phorbol 12-myristate 13-acetate (PMA);
FT dbSNP:rs121912792)"
FT /evidence="ECO:0000269|PubMed:18653847"
FT /id="VAR_047940"
FT VARIANT 126
FT /note="I -> M (in DURS2; behaves as a dominant gain-of
FT -function allele that increases CHN1 activity in vitro;
FT dbSNP:rs121912793)"
FT /evidence="ECO:0000269|PubMed:18653847"
FT /id="VAR_047941"
FT VARIANT 143
FT /note="Y -> H (in DURS2; behaves as a dominant gain-of-
FT function allele that increases CHN1 activity in vitro;
FT appears to enhance membrane translocation and CHN1 activity
FT by destabilizing the closed conformation of CHN1 protein in
FT response to phorbol 12-myristate 13-acetate (PMA);
FT dbSNP:rs121912794)"
FT /evidence="ECO:0000269|PubMed:18653847"
FT /id="VAR_047942"
FT VARIANT 223
FT /note="A -> V (in DURS2; behaves as a dominant gain-of-
FT function allele that increases CHN1 activity in vitro;
FT appears to enhance membrane translocation and CHN1 activity
FT by destabilizing the closed conformation of CHN1 protein in
FT response to phorbol 12-myristate 13-acetate (PMA);
FT dbSNP:rs121912795)"
FT /evidence="ECO:0000269|PubMed:18653847"
FT /id="VAR_047943"
FT VARIANT 228
FT /note="G -> S (in DURS2; behaves as a dominant gain-of-
FT function allele that increases CHN1 activity in vitro;
FT dbSNP:rs121912796)"
FT /evidence="ECO:0000269|PubMed:18653847"
FT /id="VAR_047944"
FT VARIANT 252
FT /note="P -> Q (in DURS2; behaves as a dominant gain-of-
FT function allele that increases CHN1 activity in vitro;
FT appears to enhance membrane translocation and CHN1 activity
FT by destabilizing the closed conformation of CHN1 protein in
FT response to phorbol 12-myristate 13-acetate (PMA);
FT dbSNP:rs121912797)"
FT /evidence="ECO:0000269|PubMed:18653847"
FT /id="VAR_047945"
FT VARIANT 313
FT /note="E -> K (in DURS2; behaves as a dominant gain-of-
FT function allele that increases CHN1 activity in vitro;
FT dbSNP:rs121912798)"
FT /evidence="ECO:0000269|PubMed:18653847"
FT /id="VAR_047946"
FT HELIX 19..26
FT /evidence="ECO:0007829|PDB:3CXL"
FT HELIX 56..63
FT /evidence="ECO:0007829|PDB:3CXL"
FT STRAND 69..74
FT /evidence="ECO:0007829|PDB:3CXL"
FT STRAND 76..78
FT /evidence="ECO:0007829|PDB:3CXL"
FT STRAND 82..87
FT /evidence="ECO:0007829|PDB:3CXL"
FT STRAND 89..96
FT /evidence="ECO:0007829|PDB:3CXL"
FT STRAND 98..107
FT /evidence="ECO:0007829|PDB:3CXL"
FT HELIX 113..129
FT /evidence="ECO:0007829|PDB:3CXL"
FT HELIX 131..136
FT /evidence="ECO:0007829|PDB:3CXL"
FT TURN 143..145
FT /evidence="ECO:0007829|PDB:3CXL"
FT STRAND 146..148
FT /evidence="ECO:0007829|PDB:3CXL"
FT HELIX 164..166
FT /evidence="ECO:0007829|PDB:3CXL"
FT STRAND 208..211
FT /evidence="ECO:0007829|PDB:3CXL"
FT TURN 220..222
FT /evidence="ECO:0007829|PDB:3CXL"
FT STRAND 228..230
FT /evidence="ECO:0007829|PDB:3CXL"
FT STRAND 233..236
FT /evidence="ECO:0007829|PDB:3CXL"
FT TURN 237..239
FT /evidence="ECO:0007829|PDB:3CXL"
FT HELIX 245..248
FT /evidence="ECO:0007829|PDB:3CXL"
FT HELIX 257..261
FT /evidence="ECO:0007829|PDB:3CXL"
FT HELIX 270..277
FT /evidence="ECO:0007829|PDB:2OSA"
FT HELIX 283..295
FT /evidence="ECO:0007829|PDB:2OSA"
FT TURN 300..304
FT /evidence="ECO:0007829|PDB:2OSA"
FT HELIX 309..322
FT /evidence="ECO:0007829|PDB:2OSA"
FT HELIX 323..325
FT /evidence="ECO:0007829|PDB:2OSA"
FT TURN 330..332
FT /evidence="ECO:0007829|PDB:2OSA"
FT HELIX 336..348
FT /evidence="ECO:0007829|PDB:2OSA"
FT TURN 357..359
FT /evidence="ECO:0007829|PDB:2OSA"
FT HELIX 360..368
FT /evidence="ECO:0007829|PDB:2OSA"
FT HELIX 372..384
FT /evidence="ECO:0007829|PDB:2OSA"
FT HELIX 388..406
FT /evidence="ECO:0007829|PDB:2OSA"
FT HELIX 408..411
FT /evidence="ECO:0007829|PDB:2OSA"
FT HELIX 415..426
FT /evidence="ECO:0007829|PDB:2OSA"
FT HELIX 434..453
FT /evidence="ECO:0007829|PDB:2OSA"
FT HELIX 455..458
FT /evidence="ECO:0007829|PDB:2OSA"
SQ SEQUENCE 459 AA; 53172 MW; 04C4CC9BCC611389 CRC64;
MALTLFDTDE YRPPVWKSYL YQLQQEAPHP RRITCTCEVE NRPKYYGREF HGMISREAAD
QLLIVAEGSY LIRESQRQPG TYTLALRFGS QTRNFRLYYD GKHFVGEKRF ESIHDLVTDG
LITLYIETKA AEYIAKMTIN PIYEHVGYTT LNREPAYKKH MPVLKETHDE RDSTGQDGVS
EKRLTSLVRR ATLKENEQIP KYEKIHNFKV HTFRGPHWCE YCANFMWGLI AQGVKCADCG
LNVHKQCSKM VPNDCKPDLK HVKKVYSCDL TTLVKAHTTK RPMVVDMCIR EIESRGLNSE
GLYRVSGFSD LIEDVKMAFD RDGEKADISV NMYEDINIIT GALKLYFRDL PIPLITYDAY
PKFIESAKIM DPDEQLETLH EALKLLPPAH CETLRYLMAH LKRVTLHEKE NLMNAENLGI
VFGPTLMRSP ELDAMAALND IRYQRLVVEL LIKNEDILF
