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Рибосомний білок S27a англ Ribosomal protein S27a білок який кодується геном RPS27A розташованим у людей на короткому пл

Рибосомний білок S27a

Рибосомний білок S27a

Рибосомний білок S27a (англ. Ribosomal protein S27a) – білок, який кодується геном RPS27A, розташованим у людей на короткому плечі 2-ї хромосоми. Довжина поліпептидного ланцюга білка становить 156 амінокислот, а молекулярна маса — 17 965.

Рибосомний білок S27a
image
Наявні структури
PDBПошук ортологів: PDBe RCSB
Ідентифікатори
Символи RPS27A, CEP80, HEL112, S27A, UBA80, UBC, UBCEP1, UBCEP80, ribosomal protein S27a
Зовнішні ІД OMIM: 191343 MGI: 1925544 HomoloGene: 37715 GeneCards: RPS27A
Ортологи
Види Людина Миша
Entrez
6233
78294
Ensembl
ENSG00000143947
ENSMUSG00000020460
UniProt
P62979
P62983
RefSeq (мРНК)
NM_002954
NM_001135592
NM_001177413
NM_001033865
NM_024277
RefSeq (білок)
NP_001129064
NP_001170884
NP_002945
NP_001029037
NP_077239
Локус (UCSC) Хр. 2: 55.23 – 55.24 Mb Хр. 11: 29.5 – 29.5 Mb
PubMed search
Вікідані
Див./Ред. для людейДив./Ред. для мишей
Послідовність амінокислот
1020304050
MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQL
EDGRTLSDYNIQKESTLHLVLRLRGGAKKRKKKSYTTPKKNKHKRKKVKL
AVLKYYKVDENGKISRLRRECPSDECGAGVFMASHFDRHYCGKCCLTYCF
NKPEDK

Цей білок за функціями належить до рибонуклеопротеїнів, рибосомних білків. Білок має сайт для зв'язування з іонами металів, іоном цинку. Локалізований у цитоплазмі, ядрі.

Література

  • Adams S.M., Sharp M.G., Walker R.A., Brammar W.J., Varley J.M. (1992). Differential expression of translation-associated genes in benign and malignant human breast tumours. Br. J. Cancer. 65: 65—71. PMID 1370760 DOI:10.1038/bjc.1992.12
  • 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
  • Schlesinger D.H., Goldstein G. (1975). Molecular conservation of 74 amino acid sequence of ubiquitin between cattle and man. Nature. 255: 423—424. PMID 1128706 DOI:10.1038/255423a0
  • Huang F., Kirkpatrick D., Jiang X., Gygi S.P., Sorkin A. (2006). Differential regulation of EGF receptor internalization and degradation by multiubiquitination within the kinase domain. Mol. Cell. 21: 737—748. PMID 16543144 DOI:10.1016/j.molcel.2006.02.018
  • Okumura F., Hatakeyama S., Matsumoto M., Kamura T., Nakayama K. (2004). Functional regulation of FEZ1 by the U-box-type ubiquitin ligase E4B contributes to neuritogenesis. J. Biol. Chem. 279: 53533—53543. PMID 15466860 DOI:10.1074/jbc.M402916200
  • Komander D. (2009). The emerging complexity of protein ubiquitination. Biochem. Soc. Trans. 37: 937—953. PMID 19754430 DOI:10.1042/BST0370937

Примітки

  1. Human PubMed Reference:.
  2. Mouse PubMed Reference:.
  3. HUGO Gene Nomenclature Commitee, HGNC:10417 (англ.) . Процитовано 27 лютого 2017.
  4. UniProt, P62979 (англ.) . Процитовано 27 лютого 2017.

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Ribosomnij bilok S27a angl Ribosomal protein S27a bilok yakij koduyetsya genom RPS27A roztashovanim u lyudej na korotkomu plechi 2 yi hromosomi Dovzhina polipeptidnogo lancyuga bilka stanovit 156 aminokislot a molekulyarna masa 17 965 Ribosomnij bilok S27aNayavni strukturiPDBPoshuk ortologiv PDBe RCSB Spisok kodiv PDB2KTF 2L0F 2L0T 2XK5 3AXC 3NHE 3NOB 3PHW 3TBL 4UG0 4V6X 5AJ0 4R62 5FLX 4UJD 4KZZ 4UJC 3J7P 4KZY 4D5L 3J7R 4D61 4KZX 4UJE 5A2QIdentifikatoriSimvoliRPS27A CEP80 HEL112 S27A UBA80 UBC UBCEP1 UBCEP80 ribosomal protein S27aZovnishni ID OMIM 191343 MGI 1925544 HomoloGene 37715 GeneCards RPS27AOntologiya genaMolekulyarna funkciya zv yazuvannya z ionom metalu structural constituent of ribosome GO 0001948 GO 0016582 protein binding RNA binding protein tag ubiquitin protein ligase bindingKlitinna komponenta citoplazma endocytic vesicle membrane gialoplazma membrana klitinne yadro ribosoma myelin sheath cytosolic small ribosomal subunit yaderce ekzosoma klitinna membrana nukleoplazma small ribosomal subunit endosome membrane mizhklitinnij prostir mitohondrialna zovnishnya membrana endoplasmic reticulum quality control compartment vezikula endoplasmic reticulum membrane host cellBiologichnij proces DNA damage response signal transduction by p53 class mediator resulting in cell cycle arrest negative regulation of epidermal growth factor receptor signaling pathway interstrand cross link repair nucleotide excision repair DNA damage recognition positive regulation of canonical Wnt signaling pathway tumor necrosis factor mediated signaling pathway regulation of type I interferon production TRIF dependent toll like receptor signaling pathway Fc epsilon receptor signaling pathway endosomal transport global genome nucleotide excision repair NIK NF kappaB signaling G2 M transition of mitotic cell cycle stress activated MAPK cascade transforming growth factor beta receptor signaling pathway macroautophagy negative regulation of canonical Wnt signaling pathway nucleotide excision repair DNA gap filling viral transcription error free translesion synthesis regulation of tumor necrosis factor mediated signaling pathway stimulatory C type lectin receptor signaling pathway negative regulation of transforming growth factor beta receptor signaling pathway SRP dependent cotranslational protein targeting to membrane JNK cascade regulation of transcription from RNA polymerase II promoter in response to hypoxia nucleotide excision repair DNA incision I kappaB kinase NF kappaB signaling vrodzhenij imunitet Signalnij shlyah Notch regulation of mRNA stability protein polyubiquitination negative regulation of apoptotic process GO 1901227 negative regulation of transcription by RNA polymerase II virion assembly positive regulation of NF kappaB transcription factor activity anaphase promoting complex dependent catabolic process negative regulation of type I interferon production nuclear transcribed mRNA catabolic process nonsense mediated decay nucleotide binding oligomerization domain containing signaling pathway GO 0046795 intracellular transport of virus GO 0019067 viral life cycle MyD88 dependent toll like receptor signaling pathway error prone translesion synthesis MAPK cascade fibroblast growth factor receptor signaling pathway ion transmembrane transport glycogen biosynthetic process positive regulation of apoptotic process translational initiation positive regulation of I kappaB kinase NF kappaB signaling translesion synthesis transcription coupled nucleotide excision repair T cell receptor signaling pathway MyD88 independent toll like receptor signaling pathway GO 0003257 GO 0010735 GO 1901228 GO 1900622 GO 1904488 positive regulation of transcription by RNA polymerase II regulation of signal transduction by p53 class mediator positive regulation of epidermal growth factor receptor signaling pathway Wnt signaling pathway nucleotide excision repair DNA duplex unwinding nucleotide excision repair DNA incision 5 to lesion Biosintez bilkiv rRNA processing ERBB2 signaling pathway Wnt signaling pathway planar cell polarity pathway nucleotide excision repair preincision complex assembly proteasome mediated ubiquitin dependent protein catabolic process zgortannya bilkiv negative regulation of G2 M transition of mitotic cell cycle Ubikvitin zalezhnij proteoliz protein deubiquitination SCF dependent proteasomal ubiquitin dependent protein catabolic process entry of bacterium into host cell transmembrannij transport regulation of necroptotic process membrane organization endoplasmic reticulum mannose trimming cellular iron ion homeostasis regulation of hematopoietic stem cell differentiation protein targeting to peroxisome cytokine mediated signaling pathway modification dependent protein catabolic process interleukin 1 mediated signaling pathwayDzherela Amigo QuickGOOrtologiVidi Lyudina MishaEntrez6233 78294Ensembl ENSG00000143947 ENSMUSG00000020460UniProt P62979 P62983RefSeq mRNK NM 002954 NM 001135592 NM 001177413NM 001033865 NM 024277RefSeq bilok NP 001129064 NP 001170884 NP 002945NP 001029037 NP 077239Lokus UCSC Hr 2 55 23 55 24 MbHr 11 29 5 29 5 MbPubMed searchVikidaniDiv Red dlya lyudejDiv Red dlya mishej Poslidovnist aminokislot1020304050 MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQL EDGRTLSDYNIQKESTLHLVLRLRGGAKKRKKKSYTTPKKNKHKRKKVKL AVLKYYKVDENGKISRLRRECPSDECGAGVFMASHFDRHYCGKCCLTYCF NKPEDK A Alanin C Cisteyin 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 Cej bilok za funkciyami nalezhit do ribonukleoproteyiniv ribosomnih bilkiv Bilok maye sajt dlya zv yazuvannya z ionami metaliv ionom cinku Lokalizovanij u citoplazmi yadri LiteraturaAdams S M Sharp M G Walker R A Brammar W J Varley J M 1992 Differential expression of translation associated genes in benign and malignant human breast tumours Br J Cancer 65 65 71 PMID 1370760 DOI 10 1038 bjc 1992 12 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 Schlesinger D H Goldstein G 1975 Molecular conservation of 74 amino acid sequence of ubiquitin between cattle and man Nature 255 423 424 PMID 1128706 DOI 10 1038 255423a0 Huang F Kirkpatrick D Jiang X Gygi S P Sorkin A 2006 Differential regulation of EGF receptor internalization and degradation by multiubiquitination within the kinase domain Mol Cell 21 737 748 PMID 16543144 DOI 10 1016 j molcel 2006 02 018 Okumura F Hatakeyama S Matsumoto M Kamura T Nakayama K 2004 Functional regulation of FEZ1 by the U box type ubiquitin ligase E4B contributes to neuritogenesis J Biol Chem 279 53533 53543 PMID 15466860 DOI 10 1074 jbc M402916200 Komander D 2009 The emerging complexity of protein ubiquitination Biochem Soc Trans 37 937 953 PMID 19754430 DOI 10 1042 BST0370937PrimitkiHuman PubMed Reference Mouse PubMed Reference HUGO Gene Nomenclature Commitee HGNC 10417 angl Procitovano 27 lyutogo 2017 UniProt P62979 angl Procitovano 27 lyutogo 2017 Div takozhHromosoma 2 Ce nezavershena stattya pro bilki Vi mozhete dopomogti proyektu vipravivshi abo dopisavshi yiyi

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