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Protein

Ribosome biogenesis protein BOP1

Gene

BOP1

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

Functioni

Component of the PeBoW complex, which is required for maturation of 28S and 5.8S ribosomal RNAs and formation of the 60S ribosome.UniRule annotation1 Publication

GO - Molecular functioni

  • poly(A) RNA binding Source: UniProtKB
  • ribonucleoprotein complex binding Source: UniProtKB-HAMAP

GO - Biological processi

  • cell proliferation Source: UniProtKB
  • cleavage in ITS2 between 5.8S rRNA and LSU-rRNA of tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) Source: Ensembl
  • maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) Source: UniProtKB
  • regulation of cell cycle Source: UniProtKB
  • ribosome biogenesis Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Ribosome biogenesis, rRNA processing

Enzyme and pathway databases

SignaLinkiQ14137.

Names & Taxonomyi

Protein namesi
Recommended name:
Ribosome biogenesis protein BOP1UniRule annotation
Alternative name(s):
Block of proliferation 1 proteinUniRule annotation
Gene namesi
Name:BOP1UniRule annotation
Synonyms:KIAA0124
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 8

Organism-specific databases

HGNCiHGNC:15519. BOP1.

Subcellular locationi

GO - Cellular componenti

  • nucleoplasm Source: UniProtKB-SubCell
  • PeBoW complex Source: UniProtKB
  • preribosome, large subunit precursor Source: UniProtKB-HAMAP
  • ribonucleoprotein complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA25398.

Polymorphism and mutation databases

BioMutaiBOP1.
DMDMi23830903.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 746746Ribosome biogenesis protein BOP1PRO_0000050885Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei106 – 1061Phosphothreonine2 Publications
Modified residuei122 – 1221Phosphotyrosine1 Publication
Modified residuei126 – 1261Phosphoserine5 Publications
Modified residuei127 – 1271Phosphoserine5 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ14137.
PaxDbiQ14137.
PeptideAtlasiQ14137.
PRIDEiQ14137.

2D gel databases

SWISS-2DPAGEQ14137.

PTM databases

PhosphoSiteiQ14137.

Expressioni

Inductioni

By MYC.1 Publication

Gene expression databases

BgeeiQ14137.
CleanExiHS_BOP1.
ExpressionAtlasiQ14137. baseline and differential.
GenevisibleiQ14137. HS.

Organism-specific databases

HPAiHPA047869.
HPA048336.

Interactioni

Subunit structurei

Component of the PeBoW complex, composed of BOP1, PES1 and WDR12. Within the PeBoW complex BOP1 interacts directly with PES1 and WDR12. The PeBoW complex also associates with the 66S pre-ribosome.UniRule annotation4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
PES1O005413EBI-1050828,EBI-1053271
WDR12Q9GZL73EBI-1050828,EBI-2490660

Protein-protein interaction databases

BioGridi116850. 37 interactions.
IntActiQ14137. 11 interactions.
MINTiMINT-3029124.

Structurei

3D structure databases

ProteinModelPortaliQ14137.
SMRiQ14137. Positions 410-745.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati411 – 45040WD 1Add
BLAST
Repeati452 – 49241WD 2Add
BLAST
Repeati532 – 57645WD 3Add
BLAST
Repeati577 – 61539WD 4Add
BLAST
Repeati618 – 65740WD 5Add
BLAST
Repeati661 – 70040WD 6Add
BLAST
Repeati716 – 74631WD 7Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni265 – 427163Sufficient for nucleolar localizationBy similarityAdd
BLAST

Sequence similaritiesi

Belongs to the WD repeat BOP1/ERB1 family.UniRule annotation
Contains 7 WD repeats.UniRule annotation

Keywords - Domaini

Repeat, WD repeat

Phylogenomic databases

eggNOGiCOG2319.
GeneTreeiENSGT00390000018422.
HOGENOMiHOG000029368.
HOVERGENiHBG008113.
InParanoidiQ14137.
KOiK14824.
OMAiLVQCVSF.
OrthoDBiEOG7MPRD9.
PhylomeDBiQ14137.
TreeFamiTF300437.

Family and domain databases

Gene3Di2.130.10.10. 2 hits.
HAMAPiMF_03027. BOP1.
InterProiIPR028598. BOP1/Erb1.
IPR012953. BOP1_N_dom.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamiPF08145. BOP1NT. 1 hit.
PF00400. WD40. 3 hits.
[Graphical view]
SMARTiSM01035. BOP1NT. 1 hit.
SM00320. WD40. 7 hits.
[Graphical view]
SUPFAMiSSF50978. SSF50978. 2 hits.
PROSITEiPS00678. WD_REPEATS_1. 1 hit.
PS50082. WD_REPEATS_2. 2 hits.
PS50294. WD_REPEATS_REGION. 2 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q14137-1) [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
MAGSRGAGRT AAPSVRPEKR RSEPELEPEP EPEPPLLCTS PLSHSTGSDS
60 70 80 90 100
GVSDSEESVF SGLEDSGSDS SEDDDEGDEE GEDGALDDEG HSGIKKTTEE
110 120 130 140 150
QVQASTPCPR TEMASARIGD EYAEDSSDEE DIRNTVGNVP LEWYDDFPHV
160 170 180 190 200
GYDLDGRRIY KPLRTRDELD QFLDKMDDPD YWRTVQDPMT GRDLRLTDEQ
210 220 230 240 250
VALVRRLQSG QFGDVGFNPY EPAVDFFSGD VMIHPVTNRP ADKRSFIPSL
260 270 280 290 300
VEKEKVSRMV HAIKMGWIQP RRPRDPTPSF YDLWAQEDPN AVLGRHKMHV
310 320 330 340 350
PAPKLALPGH AESYNPPPEY LLSEEERLAW EQQEPGERKL SFLPRKFPSL
360 370 380 390 400
RAVPAYGRFI QERFERCLDL YLCPRQRKMR VNVDPEDLIP KLPRPRDLQP
410 420 430 440 450
FPTCQALVYR GHSDLVRCLS VSPGGQWLVS GSDDGSLRLW EVATARCVRT
460 470 480 490 500
VPVGGVVKSV AWNPSPAVCL VAAAVEDSVL LLNPALGDRL VAGSTDQLLS
510 520 530 540 550
AFVPPEEPPL QPARWLEASE EERQVGLRLR ICHGKPVTQV TWHGRGDYLA
560 570 580 590 600
VVLATQGHTQ VLIHQLSRRR SQSPFRRSHG QVQRVAFHPA RPFLLVASQR
610 620 630 640 650
SVRLYHLLRQ ELTKKLMPNC KWVSSLAVHP AGDNVICGSY DSKLVWFDLD
660 670 680 690 700
LSTKPYRMLR HHKKALRAVA FHPRYPLFAS GSDDGSVIVC HGMVYNDLLQ
710 720 730 740
NPLLVPVKVL KGHVLTRDLG VLDVIFHPTQ PWVFSSGADG TVRLFT
Length:746
Mass (Da):83,630
Last modified:October 10, 2002 - v2
Checksum:i49A97BE21B0EB3DD
GO
Isoform 2 (identifier: Q14137-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-112: Missing.

Show »
Length:634
Mass (Da):71,930
Checksum:iE7A5608B28D65C36
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti577 – 5771R → H in BAA09473 (PubMed:8590280).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 112112Missing in isoform 2. 1 PublicationVSP_056391Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB060694 mRNA. Translation: BAB70666.1.
AC145291 Genomic DNA. No translation available.
AC231662 Genomic DNA. No translation available.
BC001086 mRNA. Translation: AAH01086.2.
BC005160 mRNA. Translation: AAH05160.2.
BC007274 mRNA. Translation: AAH07274.1.
BC013787 mRNA. Translation: AAH13787.1.
BC013980 mRNA. Translation: AAH13980.1.
BC017674 mRNA. Translation: AAH17674.1.
D50914 mRNA. Translation: BAA09473.1.
CCDSiCCDS6418.2. [Q14137-1]
RefSeqiNP_056016.1. NM_015201.4. [Q14137-1]
UniGeneiHs.535901.
Hs.645279.

Genome annotation databases

EnsembliENST00000569669; ENSP00000455106; ENSG00000261236. [Q14137-1]
GeneIDi23246.
KEGGihsa:23246.
UCSCiuc003zbm.3. human. [Q14137-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB060694 mRNA. Translation: BAB70666.1.
AC145291 Genomic DNA. No translation available.
AC231662 Genomic DNA. No translation available.
BC001086 mRNA. Translation: AAH01086.2.
BC005160 mRNA. Translation: AAH05160.2.
BC007274 mRNA. Translation: AAH07274.1.
BC013787 mRNA. Translation: AAH13787.1.
BC013980 mRNA. Translation: AAH13980.1.
BC017674 mRNA. Translation: AAH17674.1.
D50914 mRNA. Translation: BAA09473.1.
CCDSiCCDS6418.2. [Q14137-1]
RefSeqiNP_056016.1. NM_015201.4. [Q14137-1]
UniGeneiHs.535901.
Hs.645279.

3D structure databases

ProteinModelPortaliQ14137.
SMRiQ14137. Positions 410-745.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116850. 37 interactions.
IntActiQ14137. 11 interactions.
MINTiMINT-3029124.

PTM databases

PhosphoSiteiQ14137.

Polymorphism and mutation databases

BioMutaiBOP1.
DMDMi23830903.

2D gel databases

SWISS-2DPAGEQ14137.

Proteomic databases

MaxQBiQ14137.
PaxDbiQ14137.
PeptideAtlasiQ14137.
PRIDEiQ14137.

Protocols and materials databases

DNASUi23246.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000569669; ENSP00000455106; ENSG00000261236. [Q14137-1]
GeneIDi23246.
KEGGihsa:23246.
UCSCiuc003zbm.3. human. [Q14137-1]

Organism-specific databases

CTDi23246.
GeneCardsiGC08M145486.
H-InvDBHIX0168814.
HGNCiHGNC:15519. BOP1.
HPAiHPA047869.
HPA048336.
MIMi610596. gene.
neXtProtiNX_Q14137.
PharmGKBiPA25398.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG2319.
GeneTreeiENSGT00390000018422.
HOGENOMiHOG000029368.
HOVERGENiHBG008113.
InParanoidiQ14137.
KOiK14824.
OMAiLVQCVSF.
OrthoDBiEOG7MPRD9.
PhylomeDBiQ14137.
TreeFamiTF300437.

Enzyme and pathway databases

SignaLinkiQ14137.

Miscellaneous databases

ChiTaRSiBOP1. human.
GeneWikiiBOP1.
GenomeRNAii23246.
NextBioi44934.
PROiQ14137.
SOURCEiSearch...

Gene expression databases

BgeeiQ14137.
CleanExiHS_BOP1.
ExpressionAtlasiQ14137. baseline and differential.
GenevisibleiQ14137. HS.

Family and domain databases

Gene3Di2.130.10.10. 2 hits.
HAMAPiMF_03027. BOP1.
InterProiIPR028598. BOP1/Erb1.
IPR012953. BOP1_N_dom.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamiPF08145. BOP1NT. 1 hit.
PF00400. WD40. 3 hits.
[Graphical view]
SMARTiSM01035. BOP1NT. 1 hit.
SM00320. WD40. 7 hits.
[Graphical view]
SUPFAMiSSF50978. SSF50978. 2 hits.
PROSITEiPS00678. WD_REPEATS_1. 1 hit.
PS50082. WD_REPEATS_2. 2 hits.
PS50294. WD_REPEATS_REGION. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Gene cloning of immunogenic antigens overexpressed in pancreatic cancer."
    Nakatsura T., Senju S., Yamada K., Jotsuka T., Ogawa M., Nishimura Y.
    Biochem. Biophys. Res. Commun. 281:936-944(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
  2. "DNA sequence and analysis of human chromosome 8."
    Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., Asakawa T.
    , Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., Lander E.S.
    Nature 439:331-335(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "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] (ISOFORM 1).
    Tissue: Brain, Eye, Lymph, Muscle and Pancreas.
  4. "Prediction of the coding sequences of unidentified human genes. IV. The coding sequences of 40 new genes (KIAA0121-KIAA0160) deduced by analysis of cDNA clones from human cell line KG-1."
    Nagase T., Seki N., Tanaka A., Ishikawa K., Nomura N.
    DNA Res. 2:167-174(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 65-746 (ISOFORM 1).
    Tissue: Bone marrow.
  5. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  6. "Mammalian WDR12 is a novel member of the Pes1-Bop1 complex and is required for ribosome biogenesis and cell proliferation."
    Hoelzel M., Rohrmoser M., Schlee M., Grimm T., Harasim T., Malamoussi A., Gruber-Eber A., Kremmer E., Hiddemann W., Bornkamm G.W., Eick D.
    J. Cell Biol. 170:367-378(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PES1 AND WDR12, INDUCTION.
  7. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. "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 THR-106, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "Dominant-negative Pes1 mutants inhibit ribosomal RNA processing and cell proliferation via incorporation into the PeBoW-complex."
    Grimm T., Hoelzel M., Rohrmoser M., Harasim T., Malamoussi A., Gruber-Eber A., Kremmer E., Eick D.
    Nucleic Acids Res. 34:3030-3043(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PES1 AND WDR12.
  10. "Interdependence of Pes1, Bop1, and WDR12 controls nucleolar localization and assembly of the PeBoW complex required for maturation of the 60S ribosomal subunit."
    Rohrmoser M., Hoelzel M., Grimm T., Malamoussi A., Harasim T., Orban M., Pfisterer I., Gruber-Eber A., Kremmer E., Eick D.
    Mol. Cell. Biol. 27:3682-3694(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH PES1 AND WDR12.
  11. "The BRCT domain of mammalian Pes1 is crucial for nucleolar localization and rRNA processing."
    Hoelzel M., Grimm T., Rohrmoser M., Malamoussi A., Harasim T., Gruber-Eber A., Kremmer E., Eick D.
    Nucleic Acids Res. 35:789-800(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PES1 AND WDR12.
  12. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-106; SER-126 AND SER-127, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. "Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography."
    Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.
    Proteomics 8:1346-1361(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  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-126 AND SER-127, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  17. "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-126 AND SER-127, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  18. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. "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-126 AND SER-127, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  20. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-122; SER-126 AND SER-127, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiBOP1_HUMAN
AccessioniPrimary (citable) accession number: Q14137
Secondary accession number(s): Q969Z6
, Q96IS8, Q96Q25, Q9BSA7, Q9BVM0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: October 10, 2002
Last modified: June 24, 2015
This is version 161 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 8
    Human chromosome 8: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.