NAP1/YKR048C Protein Information

Standard Name	Nap1p 1
Systematic Name	Ykr048cp
ORF Classification	Verified
Description	Protein that interacts with mitotic cyclin Clb2p; required for the regulation of microtubule dynamics during mitosis; controls bud morphogenesis; involved in the transport of H2A and H2B histones to the nucleus; phosphorylated by CK2; protein abundance increases in response to DNA replication stress (2, 3, 4, 5, 6)
Name Description	Nucleosome Assembly Protein 1

Experimental Data
Molecules/cell	8070 7

Predicted Sequence	Formatted Sequence or sequence in FASTA format
Length (a.a.)	417
Molecular Weight (Da)	47,884
Isoelectric Point (pI)	4.06

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 Nap1p (InterPro)
Physical Interactions	There are 253 total physical interactions (BioGRID)
Homologs	PDB Homologs \| BLASTP \| BLASTP v. fungi \| Fungal Alignment \| Synteny Viewer
External Sequence Databases	EBI: UPI000005321D \| P25293 MIPS: YKR048C NCBI: 169791784 \| 169791785 \| 172034 \| 486499 \| 51013005 \| 5262962 \| 547995 \| 6322901 \| 90108772 \| NP_012974.1 GenBank/EMBL/DDBJ: DAA09199.1 \| AY692777 \| M63555 \| Z28272 \| Z28273

Amino Acid Sequence (or in FASTA format)
1 MSDPIRTKPK SSMQIDNAPT PHNTPASVLN PSYLKNGNPV RAQAQEQDDK 51 IGTINEEDIL ANQPLLLQSI QDRLGSLVGQ DSGYVGGLPK NVKEKLLSLK 101 TLQSELFEVE KEFQVEMFEL ENKFLQKYKP IWEQRSRIIS GQEQPKPEQI 151 AKGQEIVESL NETELLVDEE EKAQNDSEEE QVKGIPSFWL TALENLPIVC 201 DTITDRDAEV LEYLQDIGLE YLTDGRPGFK LLFRFDSSAN PFFTNDILCK 251 TYFYQKELGY SGDFIYDHAE GCEISWKDNA HNVTVDLEMR KQRNKTTKQV 301 RTIEKITPIE SFFNFFDPPK IQNEDQDEEL EEDLEERLAL DYSIGEQLKD 351 KLIPRAVDWF TGAALEFEFE EDEEEADEDE DEEEDDDHGL EDDDGESAEE 401 QDDFAGRPEQ APECKQS*

Amino Acid Sequence (or in FASTA format)

       1  MSDPIRTKPK SSMQIDNAPT PHNTPASVLN PSYLKNGNPV RAQAQEQDDK
      51  IGTINEEDIL ANQPLLLQSI QDRLGSLVGQ DSGYVGGLPK NVKEKLLSLK
     101  TLQSELFEVE KEFQVEMFEL ENKFLQKYKP IWEQRSRIIS GQEQPKPEQI
     151  AKGQEIVESL NETELLVDEE EKAQNDSEEE QVKGIPSFWL TALENLPIVC
     201  DTITDRDAEV LEYLQDIGLE YLTDGRPGFK LLFRFDSSAN PFFTNDILCK
     251  TYFYQKELGY SGDFIYDHAE GCEISWKDNA HNVTVDLEMR KQRNKTTKQV
     301  RTIEKITPIE SFFNFFDPPK IQNEDQDEEL EEDLEERLAL DYSIGEQLKD
     351  KLIPRAVDWF TGAALEFEFE EDEEEADEDE DEEEDDDHGL EDDDGESAEE
     401  QDDFAGRPEQ APECKQS*

external links for Nap1p

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 Nap1p

1)	Ishimi Y and Kikuchi A (1991) Identification and molecular cloning of yeast homolog of nucleosome assembly protein I which facilitates nucleosome assembly in vitro. J Biol Chem 266(11):7025-9
2)	Kellogg DR and Murray AW (1995) NAP1 acts with Clb1 to perform mitotic functions and to suppress polar bud growth in budding yeast. J Cell Biol 130(3):675-85
3)	Fujii-Nakata T, et al. (1992) Functional analysis of nucleosome assembly protein, NAP-1. The negatively charged COOH-terminal region is not necessary for the intrinsic assembly activity. J Biol Chem 267(29):20980-6
4)	Mosammaparast N, et al. (2002) A role for nucleosome assembly protein 1 in the nuclear transport of histones H2A and H2B. EMBO J 21(23):6527-38
5)	Calvert ME, et al. (2008) Phosphorylation by casein kinase 2 regulates Nap1 localization and function. Mol Cell Biol 28(4):1313-25
6)	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
7)	Ghaemmaghami S, et al. (2003) Global analysis of protein expression in yeast. Nature 425(6959):737-41