DSK2/YMR276W Protein Information

Standard Name	Dsk2p 1
Systematic Name	Ymr276wp
ORF Classification	Verified
Description	Nuclear-enriched ubiquitin-like polyubiquitin-binding protein; required for spindle pole body (SPB) duplication and for transit through the G2/M phase of the cell cycle; involved in proteolysis; interacts with the proteasome; protein abundance increases in response to DNA replication stress (2, 3, 4, 5, 6, 7, 8)

Experimental Data
Molecules/cell	3930 9

Predicted Sequence	Formatted Sequence or sequence in FASTA format
Length (a.a.)	373
Molecular Weight (Da)	39,345
Isoelectric Point (pI)	4.63

Click on image for expanded interactive view

Post-translational Modifications	PhosphoGRID \| PhosphoPep Database
Domains/motifs	See the graphical view and list of proteins that share domains/motifs in common with Dsk2p (InterPro)
Physical Interactions	There are 65 total physical interactions (BioGRID)
Homologs	PDB Homologs \| BLASTP \| BLASTP v. fungi \| Fungal Alignment \| Synteny Viewer
External Sequence Databases	EBI: UPI00001683E5 \| P48510 MIPS: YMR276W NCBI: 1352321 \| 253722444 \| 295322002 \| 308153440 \| 6323932 \| 786151 \| 825542 \| 88192467 \| 88192468 \| 88192469 \| 88192470 \| 88192471 \| 88192472 \| 88192473 \| 88192474 \| 88192475 \| 88192476 \| 88192477 \| 88192478 \| 88192479 \| 88192480 \| 88192481 \| 88192482 \| 88192483 \| 88192484 \| 88192485 \| 88192486 \| 88192487 \| 88192488 \| 88192489 \| 88192490 \| 88192491 \| 88192492 \| 88192493 \| 88192494 \| 88192495 \| 88192496 \| 88192497 \| 88192498 \| NP_014003.1 GenBank/EMBL/DDBJ: DAA10177.1 \| L40587 \| Z49704

Amino Acid Sequence (or in FASTA format)
1 MSLNIHIKSG QDKWEVNVAP ESTVLQFKEA INKANGIPVA NQRLIYSGKI 51 LKDDQTVESY HIQDGHSVHL VKSQPKPQTA SAAGANNATA TGAAAGTGAT 101 PNMSSGQSAG FNPLADLTSA RYAGYLNMPS ADMFGPDGGA LNNDSNNQDE 151 LLRMMENPIF QSQMNEMLSN PQMLDFMIQS NPQLQAMGPQ ARQMLQSPMF 201 RQMLTNPDMI RQSMQFARMM DPNAGMGSAG GAASAFPAPG GDAPEEGSNT 251 NTTSSSNTGN NAGTNAGTNA GANTAANPFA SLLNPALNPF ANAGNAASTG 301 MPAFDPALLA SMFQPPVQAS QAEDTRPPEE RYEHQLRQLN DMGFFDFDRN 351 VAALRRSGGS VQGALDSLLN GDV*

Amino Acid Sequence (or in FASTA format)

       1  MSLNIHIKSG QDKWEVNVAP ESTVLQFKEA INKANGIPVA NQRLIYSGKI
      51  LKDDQTVESY HIQDGHSVHL VKSQPKPQTA SAAGANNATA TGAAAGTGAT
     101  PNMSSGQSAG FNPLADLTSA RYAGYLNMPS ADMFGPDGGA LNNDSNNQDE
     151  LLRMMENPIF QSQMNEMLSN PQMLDFMIQS NPQLQAMGPQ ARQMLQSPMF
     201  RQMLTNPDMI RQSMQFARMM DPNAGMGSAG GAASAFPAPG GDAPEEGSNT
     251  NTTSSSNTGN NAGTNAGTNA GANTAANPFA SLLNPALNPF ANAGNAASTG
     301  MPAFDPALLA SMFQPPVQAS QAEDTRPPEE RYEHQLRQLN DMGFFDFDRN
     351  VAALRRSGGS VQGALDSLLN GDV*

external links for Dsk2p

Homologs	Interaction Resources	Protein databases/Other	Localization Resources
BLASTP (NCBI)	BioGRID	SCOP Superfamily	Organelle DB
Ashbya (AGD)	BOND	GPMdb (Mass Spec.)	YPL+
Candida (CGD)	BioPIXIE	MIPS	YeastGFP
Candida (CandidaDB)	CYC2008 (complexes)	Pfam domains	YeastRC Public Image Repository
YGOB	Complexome	YeastRC Structure Prediction (Seattle)
YOGY	DIP
	GeneMANIA
	YeastRC Two-Hybrid (Seattle)

References cited on this page View Complete Literature Guide for Dsk2p

1)	Vallen EA, et al. (1994) Genetic interactions between CDC31 and KAR1, two genes required for duplication of the microtubule organizing center in Saccharomyces cerevisiae. Genetics 137(2):407-22
2)	Biggins S, et al. (1996) Yeast ubiquitin-like genes are involved in duplication of the microtubule organizing center. J Cell Biol 133(6):1331-46
3)	Khalfan W, et al. (2000) Functional interaction between the PKC1 pathway and CDC31 network of SPB duplication genes. Genetics 155(4):1543-59
4)	Kaye FJ, et al. (2000) A family of ubiquitin-like proteins binds the ATPase domain of Hsp70-like Stch. FEBS Lett 467(2-3):348-55
5)	Funakoshi M, et al. (2002) Budding yeast Dsk2p is a polyubiquitin-binding protein that can interact with the proteasome. Proc Natl Acad Sci U S A 99(2):745-50
6)	Rao H and Sastry A (2002) Recognition of specific ubiquitin conjugates is important for the proteolytic functions of the ubiquitin-associated domain proteins Dsk2 and Rad23. J Biol Chem 277(14):11691-5
7)	Saeki Y, et al. (2002) Ubiquitin-like proteins and Rpn10 play cooperative roles in ubiquitin-dependent proteolysis. Biochem Biophys Res Commun 293(3):986-92
8)	Tkach JM, et al. (2012) Dissecting DNA damage response pathways by analysing protein localization and abundance changes during DNA replication stress. Nat Cell Biol 14(9):966-76
9)	Ghaemmaghami S, et al. (2003) Global analysis of protein expression in yeast. Nature 425(6959):737-41