P38170 (CND2_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Condensin complex subunit 2

Alternative name(s):
Barren homolog
CAPH homolog

Gene names

Name:	BRN1
Ordered Locus Names:	YBL097W
ORF Names:	YBL0830

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	754 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Regulatory subunit of the condensin complex, a complex required for conversion of interphase chromatin into mitotic-like condense chromosomes. The condensin complex probably introduces positive supercoils into relaxed DNA in the presence of type I topoisomerases and converts nicked DNA into positive knotted forms in the presence of type II topoisomerases. The condensin complex probably also plays a role during interphase. Ref.6 Ref.7
Subunit structure	Component of the condensin complex, which contains the SMC2 and SMC4 heterodimer, and three non SMC subunits that probably regulate the complex: BRN1, YCS4 and YCG1/YCS5.
Subcellular location	Nucleus. Cytoplasm. Chromosome. Note: In interphase cells, the majority of the condensin complex is found in the cytoplasm, while a minority of the complex is associated with chromatin. A subpopulation of the complex however remains associated with chromosome foci in interphase cells. During mitosis, most of the condensin complex is associated with the chromatin. At the onset of prophase, condensin associates with chromosome arms and to chromosome condensation. Dissociation from chromosomes is observed in late telophase. Ref.7
Miscellaneous	Present with 704 molecules/cell in log phase SD medium. Ref.9
Sequence similarities	Belongs to the CND2 (condensin subunit 2) family.
Sequence caution	The sequence CAA56003.1 differs from that shown. Reason: Frameshift at position 25. The sequence CAA84919.1 differs from that shown. Reason: Frameshift at position 25.

Ontologies

Keywords
Biological process	Cell cycle Cell division DNA condensation Mitosis
Cellular component	Chromosome Cytoplasm Nucleus
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	cell division Inferred from electronic annotation. Source: UniProtKB-KW mitotic chromosome condensation Inferred from mutant phenotype Ref.5. Source: SGD tRNA gene clustering Inferred from mutant phenotype. Source: SGD
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nuclear condensin complex Inferred from physical interaction Ref.7. Source: SGD
Molecular function	protein binding Inferred from physical interaction Ref.7. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
SMC2	P38989	2	EBI-4792,EBI-17412

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 754	754	Condensin complex subunit 2		PRO_0000095047
Amino acid modifications
	Modified residue	256	1	Phosphoserine Ref.11
	Modified residue	682	1	Phosphothreonine Ref.10
Experimental info
	Sequence conflict	517	1	G → A in CAA56003. Ref.1
	Sequence conflict	517	1	G → A in CAA84919. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P38170 [UniParc]. Last modified July 27, 2011. Version 3. Checksum: 7B30373738D4AE7A	FASTA	754	86,216
	10 20 30 40 50 60 MTTQLRYENN DDDERVEYNL FTNRSTMMAN FEEWIKMATD NKINSRNSWN FALIDYFYDL 70 80 90 100 110 120 DVLKDGENNI NFQKASATLD GCIKIYSSRV DSVTTETGKL LSGLAQRKTN GASNGDDSNG 130 140 150 160 170 180 GNGEGLGGDS DEANIEIDPL TGMPISNDPD VNNTRRRVYN RVLETTLVEF ETIKMKELDQ 190 200 210 220 230 240 ELIIDPLFKK ALVDFDEGGA KSLLLNTLNI DNTARVIFDA SIKDTQNVGQ GKLQRKEEEL 250 260 270 280 290 300 IERDSLVDDE NEPSQSLIST RNDSTVNDSV ISAPSMEDEI LSLGMDFIKF DQIAVCEISG 310 320 330 340 350 360 SIEQLRNVVE DINQAKDFIE NVNNRFDNFL TEEELQAAVP DNAEDDSDGF DMGMQQELCY 370 380 390 400 410 420 PDENHDNTSH DEQDDDNVNS TTGSIFEKDL MAYFDENLNR NWRGREHWKV RNFKKANLVN 430 440 450 460 470 480 KESDLLEETR TTIGDTTDKN TTDDKSMDTK KKHKQKKVLE IDFFKTDDSF EDKVFASKGR 490 500 510 520 530 540 TKIDMPIKNR KNDTHYLLPD DFHFSTDRIT RLFIKPGQKM SLFSHRKHTR GDVSSGLFEK 550 560 570 580 590 600 STVSANHSNN DIPTIADEHF WADNYERKEQ EEKEKEQSKE VGDVVGGALD NPFEDDMDGV 610 620 630 640 650 660 DFNQAFEGTD DNEEASVKLD LQDDEDHKFP IRENKVTYSR VSKKVDVRRL KKNVWRSINN 670 680 690 700 710 720 LIQEHDSRKN REQSSNDSET HTEDESTKEL KFSDIIQGIS KMYSDDTLKD ISTSFCFICL 730 740 750 LHLANEHGLQ ITHTENYNDL IVNYEDLATT QAAS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence analysis of a 78.6 kb segment of the left end of Saccharomyces cerevisiae chromosome II." Obermaier B., Gassenhuber J., Piravandi E., Domdey H. Yeast 11:1103-1112(1995) [PubMed: 7502586] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: S288c / FY1678.
[2]	"Complete DNA sequence of yeast chromosome II." Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C., Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M., Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M., Cziepluch C. , Demolis N., Delaveau T., Doignon F., Domdey H., Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D., Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N., Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J., Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C., Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P., Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y., Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F., Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E., Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M., Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B., Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L., Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M., Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S., Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K., Mewes H.-W., Kleine K. EMBO J. 13:5795-5809(1994) [PubMed: 7813418] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[3]	Saccharomyces Genome Database Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION, SEQUENCE REVISION TO 517. Strain: ATCC 204508 / S288c.
[4]	"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae." Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J. Genome Res. 17:536-543(2007) [PubMed: 17322287] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 27-754. Strain: ATCC 204508 / S288c.
[5]	"The condensin complex governs chromosome condensation and mitotic transmission of rDNA." Freeman L., Aragon-Alcaide L., Strunnikov A.V. J. Cell Biol. 149:811-824(2000) [PubMed: 10811823] [Abstract] Cited for: IDENTIFICATION IN A CONDENSIN COMPLEX WITH SMC2; SMC4; YCG1 AND YCS4.
[6]	"Mitotic chromosome condensation requires Brn1p, the yeast homologue of Barren." Lavoie B.D., Tuffo K.M., Oh S., Koshland D., Holm C. Mol. Biol. Cell 11:1293-1304(2000) [PubMed: 10749930] [Abstract] Cited for: FUNCTION.
[7]	"Chromosome condensation factor Brn1p is required for chromatid separation in mitosis." Ouspenski I.I., Cabello O.A., Brinkley B.R. Mol. Biol. Cell 11:1305-1313(2000) [PubMed: 10749931] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH SMC2.
[8]	"Sequencing and comparison of yeast species to identify genes and regulatory elements." Kellis M., Patterson N., Endrizzi M., Birren B.W., Lander E.S. Nature 423:241-254(2003) [PubMed: 12748633] [Abstract] Cited for: IDENTIFICATION OF FRAMESHIFT.
[9]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[10]	"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed: 17563356] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-682, MASS SPECTROMETRY.
[11]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-256, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X79489 Genomic DNA. Translation: CAA56003.1. Frameshift. Z35858 Genomic DNA. Translation: CAA84919.1. Frameshift. AY558077 Genomic DNA. Translation: AAS56403.1. BK006936 Genomic DNA. Translation: DAA07028.2.
PIR	S45403.
RefSeq	NP_009455.3. NM_001178337.2.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-4662N.
IntAct	P38170. 5 interactions.
MINT	MINT-539913.
STRING	P38170.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	852180.
KEGG	sce:YBL097W.
NMPDR	fig|4932.3.peg.141.
Organism-specific databases
CYGD	YBL097w.
SGD	S000000193. BRN1.
Phylogenomic databases
eggNOG	fuNOG05728.
GeneTree	EFGT00050000003927.
HOGENOM	HBG396937.
OMA	DLSTSFC.
OrthoDB	EOG437VP1.
Gene expression databases
ArrayExpress	P38170.
Genevestigator	P38170.
GermOnline	YBL097W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR022816. Condensin_barren_su2. [Graphical view]
KO	K06676.
Pfam	PF05786. Cnd2. 1 hit. [Graphical view]
PIRSF	PIRSF017126. Condensin_H. 1 hit.
ProtoNet	Search...
Other
NextBio	970643.

Entry information

Entry name

CND2_YEAST

Accession

Primary (citable) accession number: P38170
Secondary accession number(s): D6VPQ8, Q6Q5G8

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1994
Last sequence update:	July 27, 2011
Last modified:	January 25, 2012
This is version 95 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program