Q13895 (BYST_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Bystin

Gene names

Name:

BYSL

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	437 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.5 Ref.6
Subunit structure	Binds trophinin, tastin and cytokeratins.
Subcellular location	Cytoplasm. Nucleus › nucleolus. Note: Associated with 40S ribosomal subunits. Ref.5
Tissue specificity	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.
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.
Sequence similarities	Belongs to the bystin family.
Sequence caution	The sequence AAC16603.2 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Ribosome biogenesis
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Polymorphism
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell adhesion Traceable author statement Ref.2. Source: ProtInc female pregnancy Traceable author statement Ref.2. Source: ProtInc ribosome biogenesis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytoplasm Traceable author statement Ref.2. Source: ProtInc nucleolus Inferred from direct assay. Source: HPA
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
TRO	Q12816	4	EBI-358049,EBI-950001
TROAP	Q12815	9	EBI-358049,EBI-2349743

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 437	437	Bystin		PRO_0000186114
Amino acid modifications
	Modified residue	98	1	Phosphoserine Ref.4 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.13
	Modified residue	167	1	Phosphoserine Ref.10
Natural variations
	Natural variant	103	1	E → K. Corresponds to variant rs2296916 [ dbSNP | Ensembl ].		VAR_033641
	Natural variant	426	1	P → S. Corresponds to variant rs3828855 [ dbSNP | Ensembl ].		VAR_048439
Experimental info
	Sequence conflict	214	1	E → D in AAH07340. Ref.1
	Sequence conflict	263	1	A → G in AAC16603. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q13895 [UniParc]. Last modified May 30, 2006. Version 3. Checksum: 1A8C5E5EB108DF1A	FASTA	437	49,601
	10 20 30 40 50 60 MPKFKAARGV GGQEKHAPLA DQILAGNAVR AGVREKRRGR GTGEAEEEYV GPRLSRRILQ 70 80 90 100 110 120 QARQQQEELE AEHGTGDKPA APRERTTRLG PRMPQDGSDD EDEEWPTLEK AATMTAAGHH 130 140 150 160 170 180 AEVVVDPEDE RAIEMFMNKN PPARRTLADI IMEKLTEKQT EVETVMSEVS GFPMPQLDPR 190 200 210 220 230 240 VLEVYRGVRE VLSKYRSGKL PKAFKIIPAL SNWEQILYVT EPEAWTAAAM YQATRIFASN 250 260 270 280 290 300 LKERMAQRFY NLVLLPRVRD DVAEYKRLNF HLYMALKKAL FKPGAWFKGI LIPLCESGTC 310 320 330 340 350 360 TLREAIIVGS IITKCSIPVL HSSAAMLKIA EMEYSGANSI FLRLLLDKKY ALPYRVLDAL 370 380 390 400 410 420 VFHFLGFRTE KRELPVLWHQ CLLTLVQRYK ADLATDQKEA LLELLRLQPH PQLSPEIRRE 430 LQSAVPRDVE DVPITVE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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, MASS SPECTROMETRY. 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]	"Trophoblast cell activation by trophinin ligation is implicated in human embryo implantation." Sugihara K., Sugiyama D., Byrne J., Wolf D.P., Lowitz K.P., Kobayashi Y., Kabir-Salmani M., Nadano D., Aoki D., Nozawa S., Nakayama J., Mustelin T., Ruoslahti E., Yamaguchi N., Fukuda M.N. Proc. Natl. Acad. Sci. U.S.A. 104:3799-3804(2007) [PubMed] [Europe PMC] [Abstract] 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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[8]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-98, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. Tissue: Liver.
[10]	"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, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[11]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[12]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]	"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, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BC007340 mRNA. Translation: AAH07340.3. BC050645 mRNA. Translation: AAH50645.1. BC062627 mRNA. Translation: AAH62627.2. L36720 mRNA. Translation: AAC16603.2. Different initiation.
IPI	IPI00328987.
RefSeq	NP_004044.3. NM_004053.3.
UniGene	Hs.106880.
3D structure databases
ProteinModelPortal	Q13895.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q13895. 7 interactions.
MINT	MINT-1148396.
STRING	9606.ENSP00000230340.
Polymorphism databases
DMDM	108884834.
2D gel databases
SWISS-2DPAGE	Q13895.
Proteomic databases
PaxDb	Q13895.
PeptideAtlas	Q13895.
PRIDE	Q13895.
Protocols and materials databases
DNASU	705.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000230340; ENSP00000230340; ENSG00000112578.
GeneID	705.
KEGG	hsa:705.
UCSC	uc003orl.3. human.
Organism-specific databases
CTD	705.
GeneCards	GC06P041888.
HGNC	HGNC:1157. BYSL.
HPA	HPA031217. HPA031219.
MIM	603871. gene.
neXtProt	NX_Q13895.
PharmGKB	PA25472.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG280148.
HOGENOM	HOG000178028.
HOVERGEN	HBG024425.
InParanoid	Q13895.
KO	K14797.
OMA	LNFHLYQ.
OrthoDB	EOG4VHK6H.
PhylomeDB	Q13895.
Gene expression databases
ArrayExpress	Q13895.
Bgee	Q13895.
CleanEx	HS_BYSL.
Genevestigator	Q13895.
GermOnline	ENSG00000112578. Homo sapiens.
Family and domain databases
InterPro	IPR007955. Bystin. [Graphical view]
PANTHER	PTHR12821. PTHR12821. 1 hit.
Pfam	PF05291. Bystin. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	705.
NextBio	2870.
SOURCE	Search...

Entry information

Entry name

BYST_HUMAN

Accession

Primary (citable) accession number: Q13895
Secondary accession number(s): Q6P5W4, Q86W44, Q96IP8

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 1998
Last sequence update:	May 30, 2006
Last modified:	April 3, 2013
This is version 106 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.