Кальмодулін-3 (англ. Calmodulin 2) – білок, який кодується геном CALM3, розташованим у людей на короткому плечі 19-ї хромосоми. Довжина поліпептидного ланцюга білка становить 149 амінокислот, а молекулярна маса — 16 838.
кальмодулін-3 | |||||||||||||||||
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Ідентифікатори | |||||||||||||||||
Символи | CALM3, HEL-S-72, PHKD, PHKD3, calmodulin 3 (phosphorylase kinase, delta), CaM, CaMIII, calmodulin 3, CAM1, CAMB, CALM, CAM2, CPVT6, LQT16 | ||||||||||||||||
Зовнішні ІД | OMIM: 114183 HomoloGene: 134804 GeneCards: CALM3 | ||||||||||||||||
Пов'язані генетичні захворювання | |||||||||||||||||
синдром подовженого інтервалу QT | |||||||||||||||||
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Ортологи | |||||||||||||||||
Види | Людина | Миша | |||||||||||||||
Entrez |
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Ensembl |
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UniProt |
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RefSeq (мРНК) |
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RefSeq (білок) |
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Локус (UCSC) | Хр. 19: 46.6 – 46.61 Mb | н/д | |||||||||||||||
PubMed search | н/д | ||||||||||||||||
Вікідані | |||||||||||||||||
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10 | 20 | 30 | 40 | 50 | ||||
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MADQLTEEQI | AEFKEAFSLF | DKDGDGTITT | KELGTVMRSL | GQNPTEAELQ | ||||
DMINEVDADG | NGTIDFPEFL | TMMARKMKDT | DSEEEIREAF | RVFDKDGNGY | ||||
ISAAELRHVM | TNLGEKLTDE | EVDEMIREAD | IDGDGQVNYE | EFVQMMTAK |
Білок має сайт для зв'язування з іонами металів, іоном кальцію. Локалізований у цитоплазмі, цитоскелеті.
Література
- Koller M., Schnyder B., Strehler E.E. (1990). Structural organization of the human CaMIII calmodulin gene. Biochim. Biophys. Acta. 1087: 180—189. PMID 2223880 DOI:10.1016/0167-4781(90)90203-E
- Rhyner J.A., Ottiger M., Wicki R., Greenwood T.M., Strehler E.E. (1994). Structure of the human CALM1 calmodulin gene and identification of two CALM1-related pseudogenes CALM1P1 and CALM1P2. Eur. J. Biochem. 225: 71—82. PMID 7925473 DOI:10.1111/j.1432-1033.1994.00071.x
- The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 14: 2121—2127. 2004. PMID 15489334 DOI:10.1101/gr.2596504
- Kelly S., Yotis J., Macris M., Harley V. (2003). Recombinant expression, purification and characterisation of the HMG domain of human SRY. Protein Pept. Lett. 10: 281—286. PMID 12871148 DOI:10.2174/0929866033479004
- Spektor A., Tsang W.Y., Khoo D., Dynlacht B.D. (2007). Cep97 and CP110 suppress a cilia assembly program. Cell. 130: 678—690. PMID 17719545 DOI:10.1016/j.cell.2007.06.027
- Siedlecka M., Goch G., Ejchart A., Sticht H., Bierzyski A. (1999). Alpha-helix nucleation by a calcium-binding peptide loop. Proc. Natl. Acad. Sci. U.S.A. 96: 903—908. PMID 9927666 DOI:10.1073/pnas.96.3.903
Примітки
- Захворювання, генетично пов'язані з кальмодулін-3 переглянути/редагувати посилання на ВікіДаних.
- Human PubMed Reference:.
- HUGO Gene Nomenclature Commitee, HGNC:1442 (англ.) . Процитовано 30 січня 2017.
- (англ.) . Архів оригіналу за 11 вересня 2017. Процитовано 30 січня 2017.
Див. також
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Kalmodulin 3 angl Calmodulin 2 bilok yakij koduyetsya genom CALM3 roztashovanim u lyudej na korotkomu plechi 19 yi hromosomi Dovzhina polipeptidnogo lancyuga bilka stanovit 149 aminokislot a molekulyarna masa 16 838 kalmodulin 3Nayavni strukturiPDBPoshuk dlya lyudej PDBe RCSB Spisok kodiv PDB2VAY 1Y6W 4JPZ 3UCY 1WRZ 4G28 1ZOT 1YRT 1IQ5 1CDL 2LL6 3HR4 4BW7 4BW8 1YR5 4J9Y 4LZX 1L7Z 1ZUZ 2BE6 2V01 1XFV 2M55 1CTR 2I08 2MG5 2R28 3O77 4UPU 2L7L 2K0F 2M0K 4V0C 1SW8 2WEL 3DVK 2M0J 3DVM 2KUH 1K90 1K93 4G27 1CLL 2KUG 1XFX 4DJC 2LQC 2LQP 4L79 2W73 2LV6 1NKF 2JZI 3UCT 4GOW 1J7O 1PK0 4Q5U 2V02 3BYA 4Q57 2KNE 1YRU 2Y4V 2L53 2F3Y 3O78 1LVC 4M1L 2K0E 1S26 4DCK 1XFW 3SUI 2X0G 3EWV 1XFY 2LL7 4OVN 3J41 2BKI 1SK6 3DVJ 3UCW 2LGF 4UMO 3DVE 4JQ0 3OXQ 2K61 1XFU 3SJQ 2K0J 4BYF 1J7P 3G43 3EWT 4J9Z 1XFZ 2F3Z 1IWQ 2N6A 2HF5 2N27 4ZLK 5COC s2HF5IdentifikatoriSimvoliCALM3 HEL S 72 PHKD PHKD3 calmodulin 3 phosphorylase kinase delta CaM CaMIII calmodulin 3 CAM1 CAMB CALM CAM2 CPVT6 LQT16Zovnishni ID OMIM 114183 HomoloGene 134804 GeneCards CALM3Pov yazani genetichni zahvoryuvannyasindrom podovzhenogo intervalu QT Ontologiya genaMolekulyarna funkciya calcium ion binding GO 0001948 GO 0016582 protein binding calcium channel inhibitor activity protein kinase binding titin binding protein serine threonine kinase activator activity transmembrane transporter binding zv yazuvannya z ionom metalu protein phosphatase activator activity adenylate cyclase binding disordered domain specific binding inositol 1 4 5 trisphosphate 3 kinase activity ligand gated ion channel activity adenylate cyclase activator activity protein domain specific binding nitric oxide synthase regulator activity type 3 metabotropic glutamate receptor binding N terminal myristoylation domain binding phosphatidylinositol 3 kinase binding protein N terminus binding calcium dependent protein binding nitric oxide synthase binding kinase activityKlitinna komponenta citoplazma gialoplazma Kalciyevi kanali extracellular region spindle microtubule neuron projection citoskelet klitinne yadro centrosoma voltage gated potassium channel complex ekzosoma spindle pole growth cone klitinna membrana vereteno podilu sarkomera nukleoplazma vezikula GO 0097483 GO 0097481 postsinaptichne ushilnennya catalytic complex centr organizaciyi mikrotrubochok synaptic vesicle membrane mitohondrialna membrana GO 0009327 protein containing complex myelin sheath vnutrishnoklitinnijBiologichnij proces m yazove skorochennya response to amphetamine positive regulation of protein serine threonine kinase activity detection of calcium ion Fc epsilon receptor signaling pathway positive regulation of phosphoprotein phosphatase activity G2 M transition of mitotic cell cycle regulation of high voltage gated calcium channel activity positive regulation of DNA binding substantia nigra development positive regulation of protein dephosphorylation inositol phosphate metabolic process positive regulation of nitric oxide synthase activity Glikogenoliz positive regulation of cyclic nucleotide phosphodiesterase activity G protein coupled receptor signaling pathway regulation of cytokinesis regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion regulation of rhodopsin mediated signaling pathway response to corticosterone negative regulation of peptidyl threonine phosphorylation activation of adenylate cyclase activity regulyaciya sercevogo ritmu positive regulation of ryanodine sensitive calcium release channel activity response to calcium ion regulation of ryanodine sensitive calcium release channel activity regulation of nitric oxide synthase activity platelet degranulation negative regulation of ryanodine sensitive calcium release channel activity MAPK cascade positive regulation of peptidyl threonine phosphorylation positive regulation of protein autophosphorylation regulation of cardiac muscle contraction regulation of cell communication by electrical coupling involved in cardiac conduction regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum calcium mediated signaling ion transmembrane transport Wnt signaling pathway calcium modulating pathway GO 0032320 GO 0032321 GO 0032855 GO 0043089 GO 0032854 positive regulation of GTPase activity Metilyuvannya bilkiv establishment of protein localization to membrane establishment of protein localization to mitochondrial membrane regulation of synaptic vesicle endocytosis regulation of synaptic vesicle exocytosis fosforilyuvannyaDzherela Amigo QuickGOOrtologiVidi Lyudina MishaEntrez808 n dEnsembl ENSG00000160014 n dUniProt P0DP23 Q96HY3 P0DP24 n dRefSeq mRNK NM 001329921 NM 001329922 NM 001329923 NM 001329924 NM 001329925NM 001329926 NM 005184n dRefSeq bilok NP 001292553 NP 001292554 NP 001292555 NP 001734 NP 001316850NP 001316851 NP 001316852 NP 001316853 NP 001316854 NP 001316855 NP 005175 NP 008819 NP 001292554 1 NP 001292555 1 NP 001350598 NP 001350599 NP 008819 NP 001292553 NP 001292554 NP 001292555 NP 001734 NP 001316850 NP 001316851 NP 001316852 NP 001316853 NP 001316854 NP 001316855 NP 005175n dLokus UCSC Hr 19 46 6 46 61 Mbn dPubMed search n dVikidaniDiv Red dlya lyudej Poslidovnist aminokislot1020304050 MADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQ DMINEVDADGNGTIDFPEFLTMMARKMKDTDSEEEIREAFRVFDKDGNGY ISAAELRHVMTNLGEKLTDEEVDEMIREADIDGDGQVNYEEFVQMMTAK A Alanin D Asparaginova kislota E Glutaminova kislota F Fenilalanin G Glicin H Gistidin I Izolejcin K Lizin L Lejcin M Metionin N Asparagin P Prolin Q Glutamin R Arginin S Serin T Treonin V Valin Y Tirozin Bilok maye sajt dlya zv yazuvannya z ionami metaliv ionom kalciyu Lokalizovanij u citoplazmi citoskeleti LiteraturaKoller M Schnyder B Strehler E E 1990 Structural organization of the human CaMIII calmodulin gene Biochim Biophys Acta 1087 180 189 PMID 2223880 DOI 10 1016 0167 4781 90 90203 E Rhyner J A Ottiger M Wicki R Greenwood T M Strehler E E 1994 Structure of the human CALM1 calmodulin gene and identification of two CALM1 related pseudogenes CALM1P1 and CALM1P2 Eur J Biochem 225 71 82 PMID 7925473 DOI 10 1111 j 1432 1033 1994 00071 x The status quality and expansion of the NIH full length cDNA project the Mammalian Gene Collection MGC Genome Res 14 2121 2127 2004 PMID 15489334 DOI 10 1101 gr 2596504 Kelly S Yotis J Macris M Harley V 2003 Recombinant expression purification and characterisation of the HMG domain of human SRY Protein Pept Lett 10 281 286 PMID 12871148 DOI 10 2174 0929866033479004 Spektor A Tsang W Y Khoo D Dynlacht B D 2007 Cep97 and CP110 suppress a cilia assembly program Cell 130 678 690 PMID 17719545 DOI 10 1016 j cell 2007 06 027 Siedlecka M Goch G Ejchart A Sticht H Bierzyski A 1999 Alpha helix nucleation by a calcium binding peptide loop Proc Natl Acad Sci U S A 96 903 908 PMID 9927666 DOI 10 1073 pnas 96 3 903PrimitkiZahvoryuvannya genetichno pov yazani z kalmodulin 3 pereglyanuti redaguvati posilannya na VikiDanih Human PubMed Reference HUGO Gene Nomenclature Commitee HGNC 1442 angl Procitovano 30 sichnya 2017 angl Arhiv originalu za 11 veresnya 2017 Procitovano 30 sichnya 2017 Div takozhHromosoma 19 Ce nezavershena stattya pro bilki Vi mozhete dopomogti proyektu vipravivshi abo dopisavshi yiyi