SPT14/YPL175W Protein Information

Standard Name	Spt14p
Systematic Name	Ypl175wp
Alias	Cwh6p , Gpi3p 1
ORF Classification	Verified
Description	UDP-GlcNAc-binding and catalytic subunit of the enzyme that mediates the first step in glycosylphosphatidylinositol (GPI) biosynthesis, mutations cause defects in transcription and in biogenesis of cell wall proteins (2, 3)
Name Description	SuPpressor of Ty 4

Experimental Data
Molecules/cell	1480 5

Predicted Sequence	Formatted Sequence or sequence in FASTA format
Length (a.a.)	452
Molecular Weight (Da)	51,242
Isoelectric Point (pI)	7.25

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 Spt14p (InterPro)
Physical Interactions	There are 2 total physical interactions (BioGRID)
Homologs	PDB Homologs \| BLASTP \| BLASTP v. fungi \| Fungal Alignment \| Synteny Viewer
External Sequence Databases	EBI: UPI0000168426 \| P32363 MIPS: YPL175W NCBI: 1370369 \| 19858447 \| 239938921 \| 441475 \| 9755344 \| NP_015150.2 GenBank/EMBL/DDBJ: DAA11259.1 \| X63290 \| Z73531
External Classifications	EC: 2.4.1.198 [Phosphatidylinositol N-acetylglucosaminyltransferase]

Amino Acid Sequence (or in FASTA format)
1 MGFNIAMLCD FFYPQLGGVE FHIYHLSQKL IDLGHSVVII THAYKDRVGV 51 RHLTNGLKVY HVPFFVIFRE TTFPTVFSTF PIIRNILLRE QIQIVHSHGS 101 ASTFAHEGIL HANTMGLRTV FTDHSLYGFN NLTSIWVNKL LTFTLTNIDR 151 VICVSNTCKE NMIVRTELSP DIISVIPNAV VSEDFKPRDP TGGTKRKQSR 201 DKIVIVVIGR LFPNKGSDLL TRIIPKVCSS HEDVEFIVAG DGPKFIDFQQ 251 MIESHRLQKR VQLLGSVPHE KVRDVLCQGD IYLHASLTEA FGTILVEAAS 301 CNLLIVTTQV GGIPEVLPNE MTVYAEQTSV SDLVQATNKA INIIRSKALD 351 TSSFHDSVSK MYDWMDVAKR TVEIYTNISS TSSADDKDWM KMVANLYKRD 401 GIWAKHLYLL CGIVEYMLFF LLEWLYPRDE IDLAPKWPKK TVSNETKEAR 451 ET*

Amino Acid Sequence (or in FASTA format)

       1  MGFNIAMLCD FFYPQLGGVE FHIYHLSQKL IDLGHSVVII THAYKDRVGV
      51  RHLTNGLKVY HVPFFVIFRE TTFPTVFSTF PIIRNILLRE QIQIVHSHGS
     101  ASTFAHEGIL HANTMGLRTV FTDHSLYGFN NLTSIWVNKL LTFTLTNIDR
     151  VICVSNTCKE NMIVRTELSP DIISVIPNAV VSEDFKPRDP TGGTKRKQSR
     201  DKIVIVVIGR LFPNKGSDLL TRIIPKVCSS HEDVEFIVAG DGPKFIDFQQ
     251  MIESHRLQKR VQLLGSVPHE KVRDVLCQGD IYLHASLTEA FGTILVEAAS
     301  CNLLIVTTQV GGIPEVLPNE MTVYAEQTSV SDLVQATNKA INIIRSKALD
     351  TSSFHDSVSK MYDWMDVAKR TVEIYTNISS TSSADDKDWM KMVANLYKRD
     401  GIWAKHLYLL CGIVEYMLFF LLEWLYPRDE IDLAPKWPKK TVSNETKEAR
     451  ET*

external links for Spt14p

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

References cited on this page View Complete Literature Guide for Spt14p

1)	Leidich SD, et al. (1995) Temperature-sensitive yeast GPI anchoring mutants gpi2 and gpi3 are defective in the synthesis of N-acetylglucosaminyl phosphatidylinositol. Cloning of the GPI2 gene. J Biol Chem 270(22):13029-35
2)	Vossen JH, et al. (1995) Identification of SPT14/CWH6 as the yeast homologue of hPIG-A, a gene involved in the biosynthesis of GPI anchors. Biochim Biophys Acta 1243(3):549-51
3)	Kostova Z, et al. (2000) Photoaffinity labelling with P3-(4-azidoanilido)uridine 5'-triphosphate identifies gpi3p as the UDP-GlcNAc-binding subunit of the enzyme that catalyses formation of GlcNAc-phosphatidylinositol, the first glycolipid intermediate in glycosylphosphatidylinositol synthesis. Biochem J 350 Pt 3():815-22
4)	Fassler JS and Winston F (1988) Isolation and analysis of a novel class of suppressor of Ty insertion mutations in Saccharomyces cerevisiae. Genetics 118(2):203-12
5)	Ghaemmaghami S, et al. (2003) Global analysis of protein expression in yeast. Nature 425(6959):737-41