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Protein

Probable 28S rRNA (cytosine(4447)-C(5))-methyltransferase

Gene

NOP2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

S-adenosyl-L-methionine-dependent methyltransferase that specifically methylates the C5 position of cytosine 4447 in 28S rRNA (Probable). May play a role in the regulation of the cell cycle and the increased nucleolar activity that is associated with the cell proliferation (Probable).Curated

Catalytic activityi

S-adenosyl-L-methionine + cytosine(4447) in 28S rRNA = S-adenosyl-L-homocysteine + C(5)-methylcytosine(4447) in 28S rRNA.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei416 – 4161S-adenosyl-L-methioninePROSITE-ProRule annotation
Binding sitei443 – 4431S-adenosyl-L-methioninePROSITE-ProRule annotation
Binding sitei460 – 4601S-adenosyl-L-methioninePROSITE-ProRule annotation
Active sitei517 – 5171NucleophilePROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

  • positive regulation of cell proliferation Source: ProtInc
  • rRNA processing Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Biological processi

rRNA processing

Keywords - Ligandi

RNA-binding, S-adenosyl-L-methionine

Enzyme and pathway databases

ReactomeiR-HSA-6790901. rRNA modification in the nucleus.

Names & Taxonomyi

Protein namesi
Recommended name:
Probable 28S rRNA (cytosine(4447)-C(5))-methyltransferase (EC:2.1.1.-1 Publication)
Alternative name(s):
Nucleolar protein 1
Nucleolar protein 2 homolog
Proliferating-cell nucleolar antigen p120
Proliferation-associated nucleolar protein p120
Gene namesi
Name:NOP2
Synonyms:NOL1, NSUN1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:7867. NOP2.

Subcellular locationi

GO - Cellular componenti

  • nucleolus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA164724026.

Polymorphism and mutation databases

BioMutaiNOP2.
DMDMi146289861.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 812812Probable 28S rRNA (cytosine(4447)-C(5))-methyltransferasePRO_0000211818Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei36 – 361PhosphoserineCombined sources
Modified residuei58 – 581PhosphoserineCombined sources
Modified residuei67 – 671PhosphoserineCombined sources
Modified residuei102 – 1021CitrullineBy similarity
Modified residuei164 – 1641CitrullineBy similarity
Modified residuei181 – 1811PhosphoserineCombined sources
Modified residuei185 – 1851PhosphothreonineCombined sources
Modified residuei195 – 1951PhosphothreonineCombined sources
Cross-linki615 – 615Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei649 – 6491N6-acetyllysineCombined sources
Modified residuei666 – 6661PhosphoserineCombined sources
Modified residuei675 – 6751PhosphoserineCombined sources
Modified residuei732 – 7321PhosphoserineCombined sources
Modified residuei734 – 7341PhosphoserineCombined sources
Modified residuei739 – 7391PhosphothreonineCombined sources
Modified residuei776 – 7761PhosphothreonineCombined sources
Modified residuei786 – 7861PhosphoserineCombined sources
Modified residuei801 – 8011PhosphoserineCombined sources
Modified residuei812 – 8121PhosphoserineCombined sources

Post-translational modificationi

Citrullinated by PADI4.By similarity

Keywords - PTMi

Acetylation, Citrullination, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP46087.
MaxQBiP46087.
PaxDbiP46087.
PeptideAtlasiP46087.
PRIDEiP46087.
TopDownProteomicsiP46087-2. [P46087-2]

2D gel databases

SWISS-2DPAGEP46087.

PTM databases

iPTMnetiP46087.
PhosphoSiteiP46087.
SwissPalmiP46087.

Expressioni

Developmental stagei

Expressed in G1 and peaks during the early S phase of the cell cycle.1 Publication

Gene expression databases

BgeeiP46087.
CleanExiHS_NOP2.
ExpressionAtlasiP46087. baseline and differential.
GenevisibleiP46087. HS.

Organism-specific databases

HPAiHPA040119.

Interactioni

Subunit structurei

Interaction with MCRS1 (PubMed:9654073). Interacts with WDR46 (PubMed:23848194).2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CDCA7LQ96GN53EBI-356811,EBI-5278764
CEP70Q8NHQ13EBI-356811,EBI-739624
KPNA6O606843EBI-356811,EBI-359923
MT1FP047333EBI-356811,EBI-10209483
VPS52Q8N1B43EBI-356811,EBI-2799833

Protein-protein interaction databases

BioGridi110902. 158 interactions.
IntActiP46087. 38 interactions.
MINTiMINT-1137742.
STRINGi9606.ENSP00000382392.

Structurei

3D structure databases

ProteinModelPortaliP46087.
SMRiP46087. Positions 280-592.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni392 – 3987S-adenosyl-L-methionine bindingPROSITE-ProRule annotation

Sequence similaritiesi

Belongs to the class I-like SAM-binding methyltransferase superfamily. RsmB/NOP family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG1122. Eukaryota.
COG0144. LUCA.
GeneTreeiENSGT00660000095341.
HOGENOMiHOG000224258.
HOVERGENiHBG082043.
InParanoidiP46087.
KOiK14835.
OrthoDBiEOG7FBRHF.
PhylomeDBiP46087.
TreeFamiTF105660.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
InterProiIPR018314. Fmu/NOL1/Nop2p_CS.
IPR031341. Methyltr_RsmF_N.
IPR001678. MeTrfase_RsmB/NOP2.
IPR011023. Nop2p.
IPR012586. P120R_rpt.
IPR023267. RCMT.
IPR023273. RCMT_NOP2.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PfamiPF01189. Methyltr_RsmB-F. 1 hit.
PF17125. Methyltr_RsmF_N. 1 hit.
PF08062. P120R. 3 hits.
[Graphical view]
PRINTSiPR02008. RCMTFAMILY.
PR02012. RCMTNOP2.
SUPFAMiSSF53335. SSF53335. 1 hit.
TIGRFAMsiTIGR00446. nop2p. 1 hit.
PROSITEiPS01153. NOL1_NOP2_SUN. 1 hit.
PS51686. SAM_MT_RSMB_NOP. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P46087-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MGRKLDPTKE KRGPGRKARK QKGAETELVR FLPAVSDENS KRLSSRARKR
60 70 80 90 100
AAKRRLGSVE APKTNKSPEA KPLPGKLPKG ISAGAVQTAG KKGPQSLFNA
110 120 130 140 150
PRGKKRPAPG SDEEEEEEDS EEDGMVNHGD LWGSEDDADT VDDYGADSNS
160 170 180 190 200
EDEEEGEALL PIERAARKQK AREAAAGIQW SEEETEDEEE EKEVTPESGP
210 220 230 240 250
PKVEEADGGL QINVDEEPFV LPPAGEMEQD AQAPDLQRVH KRIQDIVGIL
260 270 280 290 300
RDFGAQREEG RSRSEYLNRL KKDLAIYYSY GDFLLGKLMD LFPLSELVEF
310 320 330 340 350
LEANEVPRPV TLRTNTLKTR RRDLAQALIN RGVNLDPLGK WSKTGLVVYD
360 370 380 390 400
SSVPIGATPE YLAGHYMLQG ASSMLPVMAL APQEHERILD MCCAPGGKTS
410 420 430 440 450
YMAQLMKNTG VILANDANAE RLKSVVGNLH RLGVTNTIIS HYDGRQFPKV
460 470 480 490 500
VGGFDRVLLD APCSGTGVIS KDPAVKTNKD EKDILRCAHL QKELLLSAID
510 520 530 540 550
SVNATSKTGG YLVYCTCSIT VEENEWVVDY ALKKRNVRLV PTGLDFGQEG
560 570 580 590 600
FTRFRERRFH PSLRSTRRFY PHTHNMDGFF IAKFKKFSNS IPQSQTGNSE
610 620 630 640 650
TATPTNVDLP QVIPKSENSS QPAKKAKGAA KTKQQLQKQQ HPKKASFQKL
660 670 680 690 700
NGISKGADSE LSTVPSVTKT QASSSFQDSS QPAGKAEGIR EPKVTGKLKQ
710 720 730 740 750
RSPKLQSSKK VAFLRQNAPP KGTDTQTPAV LSPSKTQATL KPKDHHQPLG
760 770 780 790 800
RAKGVEKQQL PEQPFEKAAF QKQNDTPKGP QPPTVSPIRS SRPPPAKRKK
810
SQSRGNSQLL LS
Length:812
Mass (Da):89,302
Last modified:March 6, 2007 - v2
Checksum:i4C7A1BE79388F1C5
GO
Isoform 2 (identifier: P46087-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     81-84: Missing.

Show »
Length:808
Mass (Da):88,973
Checksum:i5984B2D2A8F64780
GO
Isoform 3 (identifier: P46087-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     81-84: Missing.
     597-812: GNSETATPTN...SRGNSQLLLS → DGVLLCRSGW...QAILVPQTPK

Show »
Length:628
Mass (Da):69,615
Checksum:iF29EB2BF00FC514F
GO
Isoform 4 (identifier: P46087-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     158-158: A → AAGVQWLGLGSLQPPPPGFKQFSCLSFPSSWDLQ

Show »
Length:845
Mass (Da):92,860
Checksum:iB3AD501991F1F8F4
GO

Sequence cautioni

The sequence AAA36398.1 differs from that shown. Reason: Frameshift at position 780. Curated
The sequence CAA39119.1 differs from that shown. Reason: Frameshift at position 780. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti559 – 5591F → L in AAI28185 (PubMed:15489334).Curated
Sequence conflicti630 – 6301A → G in AAA36398 (PubMed:2576976).Curated
Sequence conflicti760 – 7612LP → FA in AAA36398 (PubMed:2576976).Curated
Sequence conflicti760 – 7612LP → FA in CAA39119 (PubMed:1394192).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti73 – 731L → S.2 Publications
Corresponds to variant rs1128164 [ dbSNP | Ensembl ].
VAR_030938

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei81 – 844Missing in isoform 2 and isoform 3. 2 PublicationsVSP_023494
Alternative sequencei158 – 1581A → AAGVQWLGLGSLQPPPPGFK QFSCLSFPSSWDLQ in isoform 4. 1 PublicationVSP_045308
Alternative sequencei597 – 812216GNSET…QLLLS → DGVLLCRSGWTAVVQSQLIA TSTFQVQAILVPQTPK in isoform 3. 1 PublicationVSP_045309Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M32110 mRNA. Translation: AAA36398.1. Sequence problems.
M33132 Genomic DNA. No translation available.
X55504 mRNA. Translation: CAA39119.1. Frameshift.
AK056208 mRNA. Translation: BAG51648.1.
AC006064 Genomic DNA. No translation available.
BC082985 mRNA. Translation: AAH82985.1.
BC000656 mRNA. Translation: AAH00656.1.
BC065257 mRNA. Translation: AAH65257.1.
BC106072 mRNA. Translation: AAI06073.1.
BC128183 mRNA. Translation: AAI28184.1.
BC128184 mRNA. Translation: AAI28185.1.
CCDSiCCDS44811.1. [P46087-2]
CCDS58202.1. [P46087-3]
CCDS58203.1. [P46087-1]
CCDS58204.1. [P46087-4]
PIRiA48168.
RefSeqiNP_001028886.1. NM_001033714.2. [P46087-2]
NP_001245237.1. NM_001258308.1. [P46087-1]
NP_001245238.1. NM_001258309.1. [P46087-4]
NP_001245239.1. NM_001258310.1. [P46087-3]
NP_006161.2. NM_006170.3. [P46087-2]
XP_005253748.1. XM_005253691.1. [P46087-1]
UniGeneiHs.534334.

Genome annotation databases

EnsembliENST00000322166; ENSP00000313272; ENSG00000111641. [P46087-1]
ENST00000382421; ENSP00000371858; ENSG00000111641. [P46087-4]
ENST00000399466; ENSP00000382392; ENSG00000111641. [P46087-2]
ENST00000537442; ENSP00000444437; ENSG00000111641. [P46087-1]
ENST00000541778; ENSP00000443150; ENSG00000111641. [P46087-2]
ENST00000545200; ENSP00000439422; ENSG00000111641. [P46087-3]
ENST00000617555; ENSP00000484384; ENSG00000111641. [P46087-3]
ENST00000620535; ENSP00000479320; ENSG00000111641. [P46087-4]
GeneIDi4839.
KEGGihsa:4839.
UCSCiuc031yro.1. human. [P46087-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M32110 mRNA. Translation: AAA36398.1. Sequence problems.
M33132 Genomic DNA. No translation available.
X55504 mRNA. Translation: CAA39119.1. Frameshift.
AK056208 mRNA. Translation: BAG51648.1.
AC006064 Genomic DNA. No translation available.
BC082985 mRNA. Translation: AAH82985.1.
BC000656 mRNA. Translation: AAH00656.1.
BC065257 mRNA. Translation: AAH65257.1.
BC106072 mRNA. Translation: AAI06073.1.
BC128183 mRNA. Translation: AAI28184.1.
BC128184 mRNA. Translation: AAI28185.1.
CCDSiCCDS44811.1. [P46087-2]
CCDS58202.1. [P46087-3]
CCDS58203.1. [P46087-1]
CCDS58204.1. [P46087-4]
PIRiA48168.
RefSeqiNP_001028886.1. NM_001033714.2. [P46087-2]
NP_001245237.1. NM_001258308.1. [P46087-1]
NP_001245238.1. NM_001258309.1. [P46087-4]
NP_001245239.1. NM_001258310.1. [P46087-3]
NP_006161.2. NM_006170.3. [P46087-2]
XP_005253748.1. XM_005253691.1. [P46087-1]
UniGeneiHs.534334.

3D structure databases

ProteinModelPortaliP46087.
SMRiP46087. Positions 280-592.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110902. 158 interactions.
IntActiP46087. 38 interactions.
MINTiMINT-1137742.
STRINGi9606.ENSP00000382392.

PTM databases

iPTMnetiP46087.
PhosphoSiteiP46087.
SwissPalmiP46087.

Polymorphism and mutation databases

BioMutaiNOP2.
DMDMi146289861.

2D gel databases

SWISS-2DPAGEP46087.

Proteomic databases

EPDiP46087.
MaxQBiP46087.
PaxDbiP46087.
PeptideAtlasiP46087.
PRIDEiP46087.
TopDownProteomicsiP46087-2. [P46087-2]

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000322166; ENSP00000313272; ENSG00000111641. [P46087-1]
ENST00000382421; ENSP00000371858; ENSG00000111641. [P46087-4]
ENST00000399466; ENSP00000382392; ENSG00000111641. [P46087-2]
ENST00000537442; ENSP00000444437; ENSG00000111641. [P46087-1]
ENST00000541778; ENSP00000443150; ENSG00000111641. [P46087-2]
ENST00000545200; ENSP00000439422; ENSG00000111641. [P46087-3]
ENST00000617555; ENSP00000484384; ENSG00000111641. [P46087-3]
ENST00000620535; ENSP00000479320; ENSG00000111641. [P46087-4]
GeneIDi4839.
KEGGihsa:4839.
UCSCiuc031yro.1. human. [P46087-1]

Organism-specific databases

CTDi4839.
GeneCardsiNOP2.
HGNCiHGNC:7867. NOP2.
HPAiHPA040119.
MIMi164031. gene.
neXtProtiNX_P46087.
PharmGKBiPA164724026.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1122. Eukaryota.
COG0144. LUCA.
GeneTreeiENSGT00660000095341.
HOGENOMiHOG000224258.
HOVERGENiHBG082043.
InParanoidiP46087.
KOiK14835.
OrthoDBiEOG7FBRHF.
PhylomeDBiP46087.
TreeFamiTF105660.

Enzyme and pathway databases

ReactomeiR-HSA-6790901. rRNA modification in the nucleus.

Miscellaneous databases

ChiTaRSiNOP2. human.
GeneWikiiNOL1.
GenomeRNAii4839.
PROiP46087.
SOURCEiSearch...

Gene expression databases

BgeeiP46087.
CleanExiHS_NOP2.
ExpressionAtlasiP46087. baseline and differential.
GenevisibleiP46087. HS.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
InterProiIPR018314. Fmu/NOL1/Nop2p_CS.
IPR031341. Methyltr_RsmF_N.
IPR001678. MeTrfase_RsmB/NOP2.
IPR011023. Nop2p.
IPR012586. P120R_rpt.
IPR023267. RCMT.
IPR023273. RCMT_NOP2.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PfamiPF01189. Methyltr_RsmB-F. 1 hit.
PF17125. Methyltr_RsmF_N. 1 hit.
PF08062. P120R. 3 hits.
[Graphical view]
PRINTSiPR02008. RCMTFAMILY.
PR02012. RCMTNOP2.
SUPFAMiSSF53335. SSF53335. 1 hit.
TIGRFAMsiTIGR00446. nop2p. 1 hit.
PROSITEiPS01153. NOL1_NOP2_SUN. 1 hit.
PS51686. SAM_MT_RSMB_NOP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning of the cDNA and sequence of the human proliferating-cell nucleolar protein P120."
    Fonagy A., Henning D., Jhiang S., Haidar M.A., Busch R.K., Larson R.G., Valdez B., Busch H.
    Cancer Commun. 1:243-251(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), DEVELOPMENTAL STAGE, VARIANT SER-73.
  2. "Genomic structure of the human proliferating cell nucleolar protein p120."
    Larson R.G., Henning D., Haidar M.A., Jhiang S., Lin W.L., Zhang W.W., Busch H.
    Cancer Commun. 2:63-71(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "A region of antisense RNA from human p120 cDNA with high homology to mouse p120 cDNA inhibits NIH 3T3 proliferation."
    Valdez B.C., Perlaky L., Saijo Y., Henning D., Zhu C., Busch R.K., Zhang W.W., Busch H.
    Cancer Res. 52:5681-5686(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT SER-73.
  4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
  5. "The finished DNA sequence of human chromosome 12."
    Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
    , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
    Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 3 AND 4).
    Tissue: Colon, Eye and Ovary.
  7. "The 58-kDa microspherule protein (MSP58), a nucleolar protein, interacts with nucleolar protein p120."
    Ren Y., Busch R.K., Perlaky L., Busch H.
    Eur. J. Biochem. 253:734-742(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MCRS1.
  8. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181 AND THR-185, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
    Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
    Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-732, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."
    Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.
    J. Proteome Res. 6:4150-4162(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-67, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
    Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
    J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-58; SER-181 AND THR-185, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36; SER-67; SER-181; THR-185; SER-666; SER-675; SER-732; SER-734; THR-739; THR-776; SER-786 AND SER-812, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181; THR-185 AND SER-732, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  17. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-649, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181; THR-185; SER-732; SER-786 AND SER-812, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  19. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  20. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-67; SER-181; THR-185; THR-195; SER-732; SER-786 AND SER-801, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  21. "Nucleolar scaffold protein, WDR46, determines the granular compartmental localization of nucleolin and DDX21."
    Hirai Y., Louvet E., Oda T., Kumeta M., Watanabe Y., Horigome T., Takeyasu K.
    Genes Cells 18:780-797(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH WDR46.
  22. "Toward a comprehensive characterization of a human cancer cell phosphoproteome."
    Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S.
    J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-58; SER-67; SER-732 AND SER-786, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma and Erythroleukemia.
  23. "Yeast Nop2 and Rcm1 methylate C2870 and C2278 of the 25S rRNA, respectively."
    Sharma S., Yang J., Watzinger P., Kotter P., Entian K.D.
    Nucleic Acids Res. 41:9062-9076(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROBABLE FUNCTION, CATALYTIC ACTIVITY.
  24. "Mapping of SUMO sites and analysis of SUMOylation changes induced by external stimuli."
    Impens F., Radoshevich L., Cossart P., Ribet D.
    Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-615, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiNOP2_HUMAN
AccessioniPrimary (citable) accession number: P46087
Secondary accession number(s): A1A4Z3
, B3KPD6, Q05BA7, Q0P5S5, Q3KQS4, Q58F30
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: March 6, 2007
Last modified: July 6, 2016
This is version 158 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.