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Protein

Bystin

Gene

BYSL

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

Functioni

Required for processing of 20S pre-rRNA precursor and biogenesis of 40S ribosomal subunits. May be required for trophinin-dependent regulation of cell adhesion during implantation of human embryos.2 Publications

GO - Molecular functioni

  • poly(A) RNA binding Source: UniProtKB

GO - Biological processi

  • cell adhesion Source: ProtInc
  • cell proliferation Source: Ensembl
  • female pregnancy Source: ProtInc
  • maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) Source: Ensembl
  • trophectodermal cell differentiation Source: Ensembl
Complete GO annotation...

Keywords - Biological processi

Ribosome biogenesis

Names & Taxonomyi

Protein namesi
Recommended name:
Bystin
Gene namesi
Name:BYSL
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 6

Organism-specific databases

HGNCiHGNC:1157. BYSL.

Subcellular locationi

GO - Cellular componenti

  • apical part of cell Source: Ensembl
  • cytoplasm Source: ProtInc
  • intracellular membrane-bounded organelle Source: HPA
  • membrane Source: UniProtKB
  • nucleolus Source: HPA
  • nucleus Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA25472.

Polymorphism and mutation databases

BioMutaiBYSL.
DMDMi108884834.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 437437BystinPRO_0000186114Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei98 – 981Phosphoserine7 Publications
Modified residuei167 – 1671Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ13895.
PaxDbiQ13895.
PeptideAtlasiQ13895.
PRIDEiQ13895.

2D gel databases

SWISS-2DPAGEQ13895.

Expressioni

Tissue specificityi

Found in the placenta from the sixth week of pregnancy. Was localized in the cytoplasm of the syncytiotrophoblast in the chorionic villi and in endometrial decidual cells at the uteroplacental interface. After week 10, the level decreased and then disappeared from placental villi.

Gene expression databases

BgeeiQ13895.
CleanExiHS_BYSL.
ExpressionAtlasiQ13895. baseline and differential.
GenevestigatoriQ13895.

Organism-specific databases

HPAiHPA031217.
HPA031219.

Interactioni

Subunit structurei

Binds trophinin, tastin and cytokeratins.

Binary interactionsi

WithEntry#Exp.IntActNotes
AESQ081175EBI-358049,EBI-717810
AIMP2Q131555EBI-358049,EBI-745226
BEND7Q8N7W2-25EBI-358049,EBI-10181188
C1orf94Q6P1W53EBI-358049,EBI-946029
CCDC102BA1A4H13EBI-358049,EBI-10171570
CCDC136Q96JN2-25EBI-358049,EBI-10171416
CDC23Q9UJX25EBI-358049,EBI-396137
CDCA7LQ96GN55EBI-358049,EBI-5278764
CEP44Q9C0F15EBI-358049,EBI-744115
CEP57L1Q8IYX8-25EBI-358049,EBI-10181988
CEP70Q8NHQ15EBI-358049,EBI-739624
COILP384326EBI-358049,EBI-945751
DDX17Q928413EBI-358049,EBI-746012
DOCK8Q8NF50-25EBI-358049,EBI-10174653
EMDP504023EBI-358049,EBI-489887
EPS8Q129293EBI-358049,EBI-375576
FAM9BQ8IZU05EBI-358049,EBI-10175124
FLJ13057Q53SE73EBI-358049,EBI-10172181
FXR2P511165EBI-358049,EBI-740459
GOLGA2Q083795EBI-358049,EBI-618309
HMBOX1Q6NT765EBI-358049,EBI-2549423
IKZF1Q134225EBI-358049,EBI-745305
KRT31Q153233EBI-358049,EBI-948001
KRT40Q6A1625EBI-358049,EBI-10171697
KRTAP10-5P603705EBI-358049,EBI-10172150
KRTAP10-7P604095EBI-358049,EBI-10172290
KRTAP4-2Q9BYR53EBI-358049,EBI-10172511
L3MBTL3Q96JM75EBI-358049,EBI-2686809
LONRF1Q17RB85EBI-358049,EBI-2341787
LTV1Q96GA35EBI-358049,EBI-2558389
LZTS2Q9BRK43EBI-358049,EBI-741037
MID1O153443EBI-358049,EBI-2340316
MID2Q9UJV3-25EBI-358049,EBI-10172526
MIPOL1Q8TD105EBI-358049,EBI-2548751
MRFAP1L1Q96HT86EBI-358049,EBI-748896
MTUS2Q5JR595EBI-358049,EBI-742948
NECAB2H3BTW23EBI-358049,EBI-10172876
OLIG3Q7RTU35EBI-358049,EBI-10225049
PDE4DIPQ5VU435EBI-358049,EBI-1105124
PHC2Q8IXK06EBI-358049,EBI-713786
PNMA1Q8ND903EBI-358049,EBI-302345
PNMA2Q9UL423EBI-358049,EBI-302355
RALYLQ86SE53EBI-358049,EBI-741520
SMN2Q166375EBI-358049,EBI-395421
SSX2IPQ9Y2D85EBI-358049,EBI-2212028
STX11O755585EBI-358049,EBI-714135
TEKT1Q969V45EBI-358049,EBI-10180409
THAP1Q9NVV95EBI-358049,EBI-741515
TNIP1Q150255EBI-358049,EBI-357849
TRAF4Q9BUZ46EBI-358049,EBI-3650647
TRIM27P143733EBI-358049,EBI-719493
TRIM37O949726EBI-358049,EBI-741602
TRIM54Q9BYV24EBI-358049,EBI-2130429
TRIP6Q156546EBI-358049,EBI-742327
TROQ128164EBI-358049,EBI-950001
TROAPQ128159EBI-358049,EBI-2349743
UBE2HA4D1L53EBI-358049,EBI-10230777
VPS37BQ9H9H45EBI-358049,EBI-4400866
ZBTB14O438295EBI-358049,EBI-10176632
ZBTB8AQ96BR95EBI-358049,EBI-742740
ZFP64Q9NTW75EBI-358049,EBI-745730

Protein-protein interaction databases

BioGridi107167. 104 interactions.
DIPiDIP-50092N.
IntActiQ13895. 66 interactions.
MINTiMINT-1148396.
STRINGi9606.ENSP00000230340.

Structurei

3D structure databases

ProteinModelPortaliQ13895.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the bystin family.Curated

Phylogenomic databases

eggNOGiNOG280148.
GeneTreeiENSGT00390000007241.
HOGENOMiHOG000178028.
HOVERGENiHBG024425.
InParanoidiQ13895.
KOiK14797.
OMAiMTGAGHH.
OrthoDBiEOG7J1804.
PhylomeDBiQ13895.
TreeFamiTF312968.

Family and domain databases

InterProiIPR007955. Bystin.
[Graphical view]
PANTHERiPTHR12821. PTHR12821. 1 hit.
PfamiPF05291. Bystin. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q13895-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPKFKAARGV GGQEKHAPLA DQILAGNAVR AGVREKRRGR GTGEAEEEYV
60 70 80 90 100
GPRLSRRILQ QARQQQEELE AEHGTGDKPA APRERTTRLG PRMPQDGSDD
110 120 130 140 150
EDEEWPTLEK AATMTAAGHH AEVVVDPEDE RAIEMFMNKN PPARRTLADI
160 170 180 190 200
IMEKLTEKQT EVETVMSEVS GFPMPQLDPR VLEVYRGVRE VLSKYRSGKL
210 220 230 240 250
PKAFKIIPAL SNWEQILYVT EPEAWTAAAM YQATRIFASN LKERMAQRFY
260 270 280 290 300
NLVLLPRVRD DVAEYKRLNF HLYMALKKAL FKPGAWFKGI LIPLCESGTC
310 320 330 340 350
TLREAIIVGS IITKCSIPVL HSSAAMLKIA EMEYSGANSI FLRLLLDKKY
360 370 380 390 400
ALPYRVLDAL VFHFLGFRTE KRELPVLWHQ CLLTLVQRYK ADLATDQKEA
410 420 430
LLELLRLQPH PQLSPEIRRE LQSAVPRDVE DVPITVE
Length:437
Mass (Da):49,601
Last modified:May 30, 2006 - v3
Checksum:i1A8C5E5EB108DF1A
GO

Sequence cautioni

The sequence AAC16603.2 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti214 – 2141E → D in AAH07340 (PubMed:15489334).Curated
Sequence conflicti263 – 2631A → G in AAC16603 (PubMed:9560222).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti103 – 1031E → K.
Corresponds to variant rs2296916 [ dbSNP | Ensembl ].
VAR_033641
Natural varianti426 – 4261P → S.
Corresponds to variant rs3828855 [ dbSNP | Ensembl ].
VAR_048439

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC007340 mRNA. Translation: AAH07340.3.
BC050645 mRNA. Translation: AAH50645.1.
BC062627 mRNA. Translation: AAH62627.2.
L36720 mRNA. Translation: AAC16603.2. Different initiation.
CCDSiCCDS34450.1.
RefSeqiNP_004044.3. NM_004053.3.
UniGeneiHs.106880.

Genome annotation databases

EnsembliENST00000230340; ENSP00000230340; ENSG00000112578.
GeneIDi705.
KEGGihsa:705.
UCSCiuc003orl.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC007340 mRNA. Translation: AAH07340.3.
BC050645 mRNA. Translation: AAH50645.1.
BC062627 mRNA. Translation: AAH62627.2.
L36720 mRNA. Translation: AAC16603.2. Different initiation.
CCDSiCCDS34450.1.
RefSeqiNP_004044.3. NM_004053.3.
UniGeneiHs.106880.

3D structure databases

ProteinModelPortaliQ13895.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107167. 104 interactions.
DIPiDIP-50092N.
IntActiQ13895. 66 interactions.
MINTiMINT-1148396.
STRINGi9606.ENSP00000230340.

Polymorphism and mutation databases

BioMutaiBYSL.
DMDMi108884834.

2D gel databases

SWISS-2DPAGEQ13895.

Proteomic databases

MaxQBiQ13895.
PaxDbiQ13895.
PeptideAtlasiQ13895.
PRIDEiQ13895.

Protocols and materials databases

DNASUi705.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000230340; ENSP00000230340; ENSG00000112578.
GeneIDi705.
KEGGihsa:705.
UCSCiuc003orl.3. human.

Organism-specific databases

CTDi705.
GeneCardsiGC06P041888.
HGNCiHGNC:1157. BYSL.
HPAiHPA031217.
HPA031219.
MIMi603871. gene.
neXtProtiNX_Q13895.
PharmGKBiPA25472.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG280148.
GeneTreeiENSGT00390000007241.
HOGENOMiHOG000178028.
HOVERGENiHBG024425.
InParanoidiQ13895.
KOiK14797.
OMAiMTGAGHH.
OrthoDBiEOG7J1804.
PhylomeDBiQ13895.
TreeFamiTF312968.

Miscellaneous databases

ChiTaRSiBYSL. human.
GeneWikiiBYSL.
GenomeRNAii705.
NextBioi2870.
PROiQ13895.
SOURCEiSearch...

Gene expression databases

BgeeiQ13895.
CleanExiHS_BYSL.
ExpressionAtlasiQ13895. baseline and differential.
GenevestigatoriQ13895.

Family and domain databases

InterProiIPR007955. Bystin.
[Graphical view]
PANTHERiPTHR12821. PTHR12821. 1 hit.
PfamiPF05291. Bystin. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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].
    Tissue: Lung, Ovary and Pancreas.
  2. "A cytoplasmic protein, bystin, interacts with trophinin, tastin, and cytokeratin and may be involved in trophinin-mediated cell adhesion between trophoblast and endometrial epithelial cells."
    Suzuki N., Zara J., Sato T., Ong E., Bakhiet N., Oshima R.G., Watson K.L., Fukuda M.N.
    Proc. Natl. Acad. Sci. U.S.A. 95:5027-5032(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 131-437.
    Tissue: Choriocarcinoma.
  3. Fukuda M.N.
    Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION.
  4. "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-98, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  5. "Bystin in human cancer cells: intracellular localization and function in ribosome biogenesis."
    Miyoshi M., Okajima T., Matsuda T., Fukuda M.N., Nadano D.
    Biochem. J. 404:373-381(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  6. Cited for: FUNCTION.
  7. "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-98, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-98, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-98, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  10. "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].
  11. "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-98 AND SER-167, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  12. "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-98, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "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-98, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiBYST_HUMAN
AccessioniPrimary (citable) accession number: Q13895
Secondary accession number(s): Q6P5W4, Q86W44, Q96IP8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: May 30, 2006
Last modified: May 27, 2015
This is version 126 of the entry and version 3 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

Miscellaneous

HeLa cells lacking BYSL show a delay in the processing of the 18S rRNA component of the 40S ribosomal subunit. HT-H cells lacking BYSL show trophinin-independent signaling through ERBB4.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: 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

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.