DAM1/YGR113W Protein Information Help

Standard Name Dam1p
Systematic Name Ygr113wp
ORF Classification Verified
Description Essential subunit of the Dam1 complex (aka DASH complex), couples kinetochores to the force produced by MT depolymerization thereby aiding in chromosome segregation; Ipl1p target for regulating kinetochore-MT attachments (1, 2, 3, 4, 5, 6)
Name Description Duo1 And Mps1 interacting
Predicted Sequence Formatted Sequence or sequence in FASTA format
Length (a.a.) 343
Molecular Weight (Da) 38,422
Isoelectric Point (pI) 9.97

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Post-translational Modifications PhosphoGRID | PhosphoPep Database
Domains/motifs See the graphical view and list of proteins that share domains/motifs in common with Dam1p (InterPro)
Physical Interactions There are 105 total physical interactions (BioGRID)
Homologs PDB Homologs | BLASTP | BLASTP v. fungi | Fungal Alignment | Synteny Viewer
External Sequence Databases EBI: UPI0000052FE3 | P53267
MIPS: YGR113W
NCBI: 1323183 | 398365747 | 67476766 | 8927583 | NP_011628.4
GenBank/EMBL/DDBJ: DAA08207.1 | AF280542 | Z72898
Amino Acid Sequence (or in FASTA format)
       1  MSEDKAKLGT TRSATEYRLS IGSAPTSRRS SMGESSSLMK FADQEGLTSS
      51  VGEYNENTIQ QLLLPKIREL SDSIITLDSN FTRLNFIHES LADLNESLGS
     101  LLYGIMSNSW CVEFSQAPHD IQDDLIAIKQ LKSLEDEKNN LVMELSNMER
     151  GIKRKKDEQG ENDLAKASQN KQFNQPLFPS SQVRKYRSYD NRDKRKPSKI
     201  GNNLQVENEE DYEDDTSSEA SFVLNPTNIG MSKSSQGHVT KTTRLNNNTN
     251  SKLRRKSILH TIRNSIASGA DLPIENDNVV NLGDLHPNNR ISLGSGAARV
     301  VNGPVTKNRN SMFSGRAERK PTESRHSVAK KTEKKINTRP PFR*      

external links for Dam1p
Homologs Interaction Resources Protein databases/Other Localization Resources
BLASTP (NCBI) BioGRID SCOP Superfamily YPL+
Ashbya (AGD) BOND GPMdb (Mass Spec.) YeastGFP
YGOB BioPIXIE MIPS YeastRC Public Image Repository
YOGY CYC2008 (complexes) Pfam domains

Complexome


DIP


GeneMANIA


YeastRC Mass Spec (Seattle)

References cited on this page View Complete Literature Guide for Dam1p
1) Li Y, et al.  (2002) The mitotic spindle is required for loading of the DASH complex onto the kinetochore. Genes Dev 16(2):183-97
2) Cheeseman IM, et al.  (2002) Phospho-regulation of kinetochore-microtubule attachments by the Aurora kinase Ipl1p. Cell 111(2):163-72
3) Courtwright AM and He X  (2002) Dam1 is the right one: phosphoregulation of kinetochore biorientation. Dev Cell 3(5):610-1
4) Miranda JJ, et al.  (2005) The yeast DASH complex forms closed rings on microtubules. Nat Struct Mol Biol 12(2):138-43
5) Westermann S, et al.  (2005) Formation of a dynamic kinetochore- microtubule interface through assembly of the Dam1 ring complex. Mol Cell 17(2):277-90
6) Westermann S, et al.  (2006) The Dam1 kinetochore ring complex moves processively on depolymerizing microtubule ends. Nature 440(7083):565-9