NSA2_HUMAN
ID NSA2_HUMAN Reviewed; 260 AA.
AC O95478;
DT 19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Ribosome biogenesis protein NSA2 homolog;
DE AltName: Full=Hairy cell leukemia protein 1;
DE AltName: Full=TGF-beta-inducible nuclear protein 1;
GN Name=NSA2; Synonyms=TINP1; ORFNames=HUSSY-29;
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].
RX PubMed=10486207; DOI=10.1006/geno.1999.5911;
RA Wu X., Ivanova G., Merup M., Jansson M., Stellan B., Grander D.,
RA Zabarovsky E., Gahrton G., Einhorn S.;
RT "Molecular analysis of the human chromosome 5q13.3 region in patients with
RT hairy cell leukemia and identification of tumor suppressor gene
RT candidates.";
RL Genomics 60:161-171(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Skeletal muscle;
RX PubMed=11124703;
RX DOI=10.1002/1097-0061(200101)18:1<69::aid-yea647>3.0.co;2-h;
RA Stanchi F., Bertocco E., Toppo S., Dioguardi R., Simionati B., Cannata N.,
RA Zimbello R., Lanfranchi G., Valle G.;
RT "Characterization of 16 novel human genes showing high similarity to yeast
RT sequences.";
RL Yeast 18:69-80(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Zhang J.S., Smith D.I.;
RT "TGF beta induced nuclear protein.";
RL Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Urinary bladder;
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 [5]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=12429849; DOI=10.1091/mbc.e02-05-0271;
RA Scherl A., Coute Y., Deon C., Calle A., Kindbeiter K., Sanchez J.-C.,
RA Greco A., Hochstrasser D.F., Diaz J.-J.;
RT "Functional proteomic analysis of human nucleolus.";
RL Mol. Biol. Cell 13:4100-4109(2002).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-81, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-81, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [8]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-80, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
CC -!- FUNCTION: Involved in the biogenesis of the 60S ribosomal subunit. May
CC play a part in the quality control of pre-60S particles (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Component of the pre-66S ribosomal particle. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:12429849}.
CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eS8 family.
CC Ribosome biogenesis protein NSA2 subfamily. {ECO:0000305}.
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DR EMBL; AF372458; AAK53761.1; -; mRNA.
DR EMBL; AJ012409; CAA10008.1; -; mRNA.
DR EMBL; AF077615; AAG43048.1; -; mRNA.
DR EMBL; BC005288; AAH05288.1; -; mRNA.
DR CCDS; CCDS4025.1; -.
DR RefSeq; NP_001258594.1; NM_001271665.1.
DR RefSeq; NP_055701.1; NM_014886.4.
DR AlphaFoldDB; O95478; -.
DR SMR; O95478; -.
DR BioGRID; 115683; 199.
DR IntAct; O95478; 65.
DR MINT; O95478; -.
DR STRING; 9606.ENSP00000483484; -.
DR iPTMnet; O95478; -.
DR PhosphoSitePlus; O95478; -.
DR SwissPalm; O95478; -.
DR BioMuta; NSA2; -.
DR SWISS-2DPAGE; O95478; -.
DR EPD; O95478; -.
DR jPOST; O95478; -.
DR MassIVE; O95478; -.
DR PaxDb; O95478; -.
DR PeptideAtlas; O95478; -.
DR PRIDE; O95478; -.
DR ProteomicsDB; 50909; -.
DR Antibodypedia; 12347; 84 antibodies from 28 providers.
DR DNASU; 10412; -.
DR Ensembl; ENST00000610426.5; ENSP00000483484.1; ENSG00000164346.10.
DR GeneID; 10412; -.
DR KEGG; hsa:10412; -.
DR MANE-Select; ENST00000610426.5; ENSP00000483484.1; NM_014886.6; NP_055701.1.
DR CTD; 10412; -.
DR DisGeNET; 10412; -.
DR GeneCards; NSA2; -.
DR HGNC; HGNC:30728; NSA2.
DR HPA; ENSG00000164346; Low tissue specificity.
DR MIM; 612497; gene.
DR neXtProt; NX_O95478; -.
DR OpenTargets; ENSG00000164346; -.
DR PharmGKB; PA165660390; -.
DR VEuPathDB; HostDB:ENSG00000164346; -.
DR eggNOG; KOG3163; Eukaryota.
DR GeneTree; ENSGT00390000018706; -.
DR HOGENOM; CLU_1070048_0_0_1; -.
DR InParanoid; O95478; -.
DR OMA; TKSWKRM; -.
DR OrthoDB; 1079827at2759; -.
DR PhylomeDB; O95478; -.
DR TreeFam; TF300766; -.
DR PathwayCommons; O95478; -.
DR SignaLink; O95478; -.
DR BioGRID-ORCS; 10412; 756 hits in 1023 CRISPR screens.
DR ChiTaRS; NSA2; human.
DR GeneWiki; TINP1; -.
DR GenomeRNAi; 10412; -.
DR Pharos; O95478; Tbio.
DR PRO; PR:O95478; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; O95478; protein.
DR Bgee; ENSG00000164346; Expressed in calcaneal tendon and 215 other tissues.
DR ExpressionAtlas; O95478; baseline and differential.
DR Genevisible; O95478; HS.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0030687; C:preribosome, large subunit precursor; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0000460; P:maturation of 5.8S rRNA; IBA:GO_Central.
DR GO; GO:0000470; P:maturation of LSU-rRNA; IBA:GO_Central.
DR CDD; cd11381; NSA2; 1.
DR InterPro; IPR039411; NSA2_fam.
DR InterPro; IPR022309; Ribosomal_S8e/biogenesis_NSA2.
DR PANTHER; PTHR12642; PTHR12642; 1.
DR Pfam; PF01201; Ribosomal_S8e; 1.
PE 1: Evidence at protein level;
KW Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome;
KW Ribonucleoprotein; Ribosome biogenesis; rRNA processing; Ubl conjugation.
FT CHAIN 1..260
FT /note="Ribosome biogenesis protein NSA2 homolog"
FT /id="PRO_0000122259"
FT REGION 20..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 11..18
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT COMPBIAS 20..38
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 81
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT CROSSLNK 80
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VARIANT 11
FT /note="R -> C (in dbSNP:rs3733793)"
FT /id="VAR_051862"
SQ SEQUENCE 260 AA; 30065 MW; C42D3E8EFB2669D8 CRC64;
MPQNEYIELH RKRYGYRLDY HEKKRKKESR EAHERSKKAK KMIGLKAKLY HKQRHAEKIQ
MKKTIKMHEK RNTKQKNDEK TPQGAVPAYL LDREGQSRAK VLSNMIKQKR KEKAGKWEVP
LPKVRAQGET EVLKVIRTGK RKKKAWKRMV TKVCFVGDGF TRKPPKYERF IRPMGLRFKK
AHVTHPELKA TFCLPILGVK KNPSSPLYTT LGVITKGTVI EVNVSELGLV TQGGKVIWGK
YAQVTNNPEN DGCINAVLLV
