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NOP56_BOVIN
ID   NOP56_BOVIN             Reviewed;         596 AA.
AC   Q3SZ63;
DT   11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   25-MAY-2022, entry version 89.
DE   RecName: Full=Nucleolar protein 56;
DE   AltName: Full=Nucleolar protein 5A;
GN   Name=NOP56; Synonyms=NOL5A;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Heart ventricle;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in the early to middle stages of 60S ribosomal
CC       subunit biogenesis. Core component of box C/D small nucleolar
CC       ribonucleoprotein (snoRNP) particles. Required for the biogenesis of
CC       box C/D snoRNAs such U3, U8 and U14 snoRNAs (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Part of a large pre-ribosomal ribonucleoprotein (RNP) complex,
CC       that consists of at least 62 ribosomal proteins, 45 nonribosomal
CC       proteins and both pre-rRNA and mature rRNA species. Within this complex
CC       directly interacts with TCOF1 in an RNA-independent manner. Core
CC       component of box C/D small nucleolar ribonucleoprotein (snoRNP)
CC       particles; the core proteins SNU13, NOP56, NOP58 and FBL assemble
CC       stepwise onto the snoRNA. Interacts NOP1 and NOP58. Interacts with
CC       NUFIP1, RUVBL1 and RUVBL2; RUVBL1:RUVBL2 seem to bridge the association
CC       of NOP56 with NUFIP1 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}. Cytoplasm
CC       {ECO:0000250}. Nucleus, nucleoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the NOP5/NOP56 family. {ECO:0000305}.
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DR   EMBL; BC103114; AAI03115.1; -; mRNA.
DR   RefSeq; NP_001028794.1; NM_001033622.2.
DR   AlphaFoldDB; Q3SZ63; -.
DR   SMR; Q3SZ63; -.
DR   STRING; 9913.ENSBTAP00000025042; -.
DR   PaxDb; Q3SZ63; -.
DR   PRIDE; Q3SZ63; -.
DR   GeneID; 404165; -.
DR   KEGG; bta:404165; -.
DR   CTD; 10528; -.
DR   eggNOG; KOG2573; Eukaryota.
DR   InParanoid; Q3SZ63; -.
DR   OrthoDB; 632707at2759; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0031428; C:box C/D RNP complex; IEA:InterPro.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0032040; C:small-subunit processome; IEA:InterPro.
DR   GO; GO:0030515; F:snoRNA binding; IEA:InterPro.
DR   GO; GO:0042254; P:ribosome biogenesis; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.246.90; -; 1.
DR   InterPro; IPR045056; Nop56/Nop58.
DR   InterPro; IPR012974; NOP5_N.
DR   InterPro; IPR042239; Nop_C.
DR   InterPro; IPR002687; Nop_dom.
DR   InterPro; IPR036070; Nop_dom_sf.
DR   InterPro; IPR012976; NOSIC.
DR   PANTHER; PTHR10894; PTHR10894; 1.
DR   Pfam; PF01798; Nop; 1.
DR   Pfam; PF08156; NOP5NT; 1.
DR   SMART; SM00931; NOSIC; 1.
DR   SUPFAM; SSF89124; SSF89124; 1.
DR   PROSITE; PS51358; NOP; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Cytoplasm; Isopeptide bond; Methylation; Nucleus;
KW   Phosphoprotein; Reference proteome; Ribonucleoprotein; Ribosome biogenesis;
KW   Ubl conjugation.
FT   CHAIN           1..596
FT                   /note="Nucleolar protein 56"
FT                   /id="PRO_0000246078"
FT   DOMAIN          292..410
FT                   /note="Nop"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00690"
FT   REGION          458..596
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        470..490
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        501..520
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        527..567
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         314
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O00567"
FT   MOD_RES         359
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:O00567"
FT   MOD_RES         465
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9D6Z1"
FT   MOD_RES         466
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9D6Z1"
FT   MOD_RES         510
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O00567"
FT   MOD_RES         518
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O00567"
FT   MOD_RES         519
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O00567"
FT   MOD_RES         536
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9D6Z1"
FT   MOD_RES         560
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9D6Z1"
FT   MOD_RES         562
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O00567"
FT   MOD_RES         569
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O00567"
FT   MOD_RES         570
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O00567"
FT   MOD_RES         581
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O00567"
FT   MOD_RES         583
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O00567"
FT   CROSSLNK        87
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:O00567"
FT   CROSSLNK        230
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:O00567"
FT   CROSSLNK        240
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:O00567"
FT   CROSSLNK        539
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:O00567"
FT   CROSSLNK        564
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:O00567"
SQ   SEQUENCE   596 AA;  66331 MW;  74D35A9E6B5DD0B6 CRC64;
     MVLLHVLFEH AVGYALLALK EVEEIILLLP QVEECVLNLG KFHNIVRLVA FCPFSSSQVA
     LENANAVSEG VVHEDLRLLL ETHLPPKKKK VLLGVGDPKI GAAIQEELGY NCQTGGVIAE
     ILRGVRLHFH NLVKGLTDLS ACKAQLGLGH SYSRAKVKFN VNRVDNMIIQ SISLLDQLDK
     DINTFSMRVR EWYGYHFPEL VKIINDNATY CRLAQFIGNR KELNEEKLEK LEELTMDAAK
     AKAILDASRS SMGMDISAID LINIESFSSR VVSLSEYRQS LHTYLRSKMS QVAPSLSALI
     GEAVGARLIA HAGSLTNLAK YPASTVQILG AEKALFRALK TRGNTPKYGL IFHSTFIGRA
     AAKNKGRISR YLANKCSIAS RIDCFSEVPT SVFGEKLREQ VEERLSFYET GEIPRKNLDV
     MKEAMVQAEE AAAEITRKLE KQEKKRLKKE KKRLAAIALA SSENSSAPEE CEETSERPKK
     KKKQKPQEVL QENGMEDPSV SFSKPKKKKS FSKEELVSSD LEETAGTGSL PKRKKSFPKE
     EPVTDPDESE NKRVPKKKRK LSPKEEPLSS GPEEAAASKS SGSKKKKKLR KLSQES
 
 
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