Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Polyphosphatidylinositol phosphatase INP52

Gene

INP52

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Dephosphorylates a number of phosphatidylinositols (PIs) like phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2), but also phosphatidylinositol 3-phosphate (PtdIns3P), phosphatidylinositol 4-phosphate (PtdIns4P), and phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2). Controls the cellular levels and subcellular distribution of phosphatidylinositol 3-phosphate and phosphatidylinositol 4,5-bisphosphate. Specifically functions within the early endocytic pathway and actin organization.13 Publications

Catalytic activityi

1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O = 1-phosphatidyl-1D-myo-inositol 4-phosphate + phosphate.

GO - Molecular functioni

  • phosphatidylinositol-3,5-bisphosphate 5-phosphatase activity Source: SGD
  • phosphatidylinositol-3-phosphatase activity Source: SGD
  • phosphatidylinositol-4,5-bisphosphate 5-phosphatase activity Source: SGD
  • phosphatidylinositol-4-phosphate phosphatase activity Source: SGD

GO - Biological processi

  • endocytosis Source: UniProtKB-KW
  • phosphatidylinositol-3-phosphate biosynthetic process Source: GOC
  • phosphatidylinositol dephosphorylation Source: SGD
  • protein transport Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Endocytosis, Lipid metabolism, Protein transport, Transport

Enzyme and pathway databases

BioCyciYEAST:MONOMER3O-69.
YEAST:YNL106C-MONOMER.
ReactomeiR-SCE-1660499. Synthesis of PIPs at the plasma membrane.
R-SCE-1660514. Synthesis of PIPs at the Golgi membrane.
R-SCE-1855183. Synthesis of IP2, IP, and Ins in the cytosol.
R-SCE-1855204. Synthesis of IP3 and IP4 in the cytosol.
R-SCE-194840. Rho GTPase cycle.
R-SCE-202424. Downstream TCR signaling.

Names & Taxonomyi

Protein namesi
Recommended name:
Polyphosphatidylinositol phosphatase INP52
Alternative name(s):
Synaptojanin-like protein 2
Including the following 2 domains:
SAC1-like phosphoinositide phosphatase (EC:3.1.3.-)
Phosphatidylinositol 4,5-bisphosphate 5-phosphatase (EC:3.1.3.36)
Gene namesi
Name:INP52
Synonyms:SJL2
Ordered Locus Names:YNL106C
ORF Names:N2160
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XIV

Organism-specific databases

EuPathDBiFungiDB:YNL106C.
SGDiS000005050. INP52.

Subcellular locationi

GO - Cellular componenti

  • actin cortical patch Source: SGD
  • cytoplasm Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi631 – 6311E → A: Impairs completely enzyme activity. 1 Publication
Mutagenesisi730 – 7301H → A: Impairs completely enzyme activity. 1 Publication
Mutagenesisi771 – 7711D → A: Impairs completely enzyme activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11831183Polyphosphatidylinositol phosphatase INP52PRO_0000209745Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei152 – 1521PhosphoserineCombined sources
Modified residuei522 – 5221PhosphoserineCombined sources
Modified residuei1005 – 10051PhosphoserineCombined sources
Modified residuei1016 – 10161PhosphoserineCombined sources
Modified residuei1032 – 10321PhosphothreonineCombined sources
Modified residuei1095 – 10951PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP50942.
PeptideAtlasiP50942.

PTM databases

iPTMnetiP50942.

Interactioni

Subunit structurei

Interacts with ABP1 and BSP1.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ABP1P158912EBI-28834,EBI-2036
BSP1Q066044EBI-28834,EBI-37047
SLA1P327903EBI-28834,EBI-17313

Protein-protein interaction databases

BioGridi35718. 125 interactions.
DIPiDIP-2764N.
IntActiP50942. 12 interactions.
MINTiMINT-593552.

Structurei

3D structure databases

ProteinModelPortaliP50942.
SMRiP50942. Positions 171-502, 567-905.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini167 – 507341SACPROSITE-ProRule annotationAdd
BLAST

Domaini

The SAC1 domain is capable of hydrolyzing phosphatidylinositol 3-phosphate (PtdIns3P), phosphatidylinositol 4-phosphate (PtdIns4P), and phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2).1 Publication

Sequence similaritiesi

Belongs to the synaptojanin family.Curated
In the central section; belongs to the inositol 1,4,5-trisphosphate 5-phosphatase family.Curated
Contains 1 SAC domain.PROSITE-ProRule annotation

Phylogenomic databases

GeneTreeiENSGT00760000119075.
HOGENOMiHOG000179717.
InParanoidiP50942.
KOiK01106.
OMAiGIMGIAG.
OrthoDBiEOG7DRJBN.

Family and domain databases

Gene3Di3.60.10.10. 1 hit.
InterProiIPR005135. Endo/exonuclease/phosphatase.
IPR000300. IPPc.
IPR002013. SAC_dom.
[Graphical view]
PfamiPF03372. Exo_endo_phos. 1 hit.
PF02383. Syja_N. 1 hit.
[Graphical view]
SMARTiSM00128. IPPc. 1 hit.
[Graphical view]
SUPFAMiSSF56219. SSF56219. 1 hit.
PROSITEiPS50275. SAC. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P50942-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKILLSKQQT RKIAIVSETH GLVFRPINSK NSRRSTCAVE LVPKAELNGN
60 70 80 90 100
GFRRLSNHEI YGFIGLIEIE GLMFIATITG KSKVAQPIPN KTVNKIYAVD
110 120 130 140 150
FFCLNNSKWD FMDIDSSGYP IVTNDGDFAI SSPPSISTHS SRSSLRSSSS
160 170 180 190 200
RSLNAQEQAP KHPCHELRKL LSNGSFYYST DFDLTCTLQK RGFTEHSLSF
210 220 230 240 250
DDFDREFMWN SFLMDEIITY RDRLDVTAKE LLDQRGFLTT VIRGFAETIF
260 270 280 290 300
SYINRLKVGL TIISRQSWKR AGTRFNARGI DDDGHVANFV ETEMIMYSSQ
310 320 330 340 350
YCYAFTQIRG SLPIFWEQDT SLISPKIQIT RSVEATQPTF DEHFIRLFKK
360 370 380 390 400
YGPVHIINLL STKSSEIQLS RRYKEQLKNS EKMKIGRDVF LTSFDFHRET
410 420 430 440 450
SQDGFAAASR IIPKIRNTIL DAGYFSYDVK EGRLISEQDG VFRTNCLDCL
460 470 480 490 500
DRTNLIQQTI SLAVFKLFLE DFRLVKPSSF IDDNEFVQKV NALWADNGDQ
510 520 530 540 550
ISQIYTGTNA LKSSYSRKGK MSFSGALSDA TKSVSRMYIN NFVDKGKQQN
560 570 580 590 600
IDTLLGKLPH QQVVELYDPI CEYVNERLLE SEEKFTTHSN INLFVGTFNV
610 620 630 640 650
NGNSRRADLS KWLFPIGDKF KPDVVVLGLQ EVIELTAGSI LNADYTKSSF
660 670 680 690 700
WETMVTDCLN QYEEKYLLLR VEQMSSLLIL FFARSDRAYN IKEVGGSTKK
710 720 730 740 750
TGFGGITGNK GAVAIRFDYG ATSFCFVNTH LSAGASNIDE RRNDYNNIYR
760 770 780 790 800
NITFPRSKTI PHHDSLFWLG DLNYRITLTN DEVRRELRAQ KDGYIDRLLQ
810 820 830 840 850
YDQLTQEINE GVVFQGFKEP TLQFRPTYKY DYGTDNYDTS EKARTPSWTD
860 870 880 890 900
RIIYKGENLH PLAYSDAPLK ISDHKPVYAA YRANVKFVDE KEKLNLVEKL
910 920 930 940 950
YAEYKNTHPE ALTTGPDELS HARMEKQKES IPLDATVQSA GIKLIDLDDT
960 970 980 990 1000
SSCVSPLLSG PSPQPSVVGP GGLSNVSPDK SKLNVLPPPP PTSRHNKEPS
1010 1020 1030 1040 1050
SKLLSPTKEI SIVSVSPRKG ESNLPALERH STPKPLPPVP ALSLSKPVSL
1060 1070 1080 1090 1100
QKSSSELQHA KETIDNGKIV PRPCPPIRRK SSTAPDEIST STKNSGVSTT
1110 1120 1130 1140 1150
EDPEPAKAST KPEKPPVVKK PHYLSVAANK LNTSQEHSIK VSPSNSKSEE
1160 1170 1180
ELPCKKKSKP KVPAKNPELE KLSVHPLKPC DPN
Length:1,183
Mass (Da):133,331
Last modified:October 1, 1996 - v1
Checksum:i97B279870DFE6F65
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z71382 Genomic DNA. Translation: CAA95982.1.
Z69382 Genomic DNA. Translation: CAA93402.1.
Z50161 Genomic DNA. Translation: CAA90520.1.
BK006947 Genomic DNA. Translation: DAA10440.1.
PIRiS63046.
RefSeqiNP_014293.1. NM_001182944.1.

Genome annotation databases

EnsemblFungiiYNL106C; YNL106C; YNL106C.
GeneIDi855618.
KEGGisce:YNL106C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z71382 Genomic DNA. Translation: CAA95982.1.
Z69382 Genomic DNA. Translation: CAA93402.1.
Z50161 Genomic DNA. Translation: CAA90520.1.
BK006947 Genomic DNA. Translation: DAA10440.1.
PIRiS63046.
RefSeqiNP_014293.1. NM_001182944.1.

3D structure databases

ProteinModelPortaliP50942.
SMRiP50942. Positions 171-502, 567-905.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi35718. 125 interactions.
DIPiDIP-2764N.
IntActiP50942. 12 interactions.
MINTiMINT-593552.

PTM databases

iPTMnetiP50942.

Proteomic databases

MaxQBiP50942.
PeptideAtlasiP50942.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYNL106C; YNL106C; YNL106C.
GeneIDi855618.
KEGGisce:YNL106C.

Organism-specific databases

EuPathDBiFungiDB:YNL106C.
SGDiS000005050. INP52.

Phylogenomic databases

GeneTreeiENSGT00760000119075.
HOGENOMiHOG000179717.
InParanoidiP50942.
KOiK01106.
OMAiGIMGIAG.
OrthoDBiEOG7DRJBN.

Enzyme and pathway databases

BioCyciYEAST:MONOMER3O-69.
YEAST:YNL106C-MONOMER.
ReactomeiR-SCE-1660499. Synthesis of PIPs at the plasma membrane.
R-SCE-1660514. Synthesis of PIPs at the Golgi membrane.
R-SCE-1855183. Synthesis of IP2, IP, and Ins in the cytosol.
R-SCE-1855204. Synthesis of IP3 and IP4 in the cytosol.
R-SCE-194840. Rho GTPase cycle.
R-SCE-202424. Downstream TCR signaling.

Miscellaneous databases

NextBioi979804.
PROiP50942.

Family and domain databases

Gene3Di3.60.10.10. 1 hit.
InterProiIPR005135. Endo/exonuclease/phosphatase.
IPR000300. IPPc.
IPR002013. SAC_dom.
[Graphical view]
PfamiPF03372. Exo_endo_phos. 1 hit.
PF02383. Syja_N. 1 hit.
[Graphical view]
SMARTiSM00128. IPPc. 1 hit.
[Graphical view]
SUPFAMiSSF56219. SSF56219. 1 hit.
PROSITEiPS50275. SAC. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its evolutionary implications."
    Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K., Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K., Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M., Beinhauer J.D., Boskovic J., Buitrago M.J.
    , Bussereau F., Coster F., Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F., Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C., Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A., Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H., Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L., Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R., Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D., Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A., Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C., Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F., Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G., Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M., Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.
    Nature 387:93-98(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  3. "The sequence of a 21.3 kb DNA fragment from the left arm of yeast chromosome XIV reveals LEU4, MET4, POL1, RAS2, and six new open reading frames."
    Saiz J.E., Buitrago M.J., Soler A., del Rey F., Revuelta J.L.
    Yeast 12:403-409(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-1102.
    Strain: ATCC 96604 / S288c / FY1679.
  4. "The DNA sequence of cosmid 14-13b from chromosome XIV of Saccharomyces cerevisiae reveals an unusually high number of overlapping open reading frames."
    de Antoni A., D'Angelo M., Dal Pero F., Sartorello F., Pandolfo D., Pallavicini A., Lanfranchi G., Valle G.
    Yeast 13:261-266(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 880-1183.
  5. "Novel genes involved in endosomal traffic in yeast revealed by suppression of a targeting-defective plasma membrane ATPase mutant."
    Luo W.-J., Chang A.
    J. Cell Biol. 138:731-746(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  6. "Identification and characterization of an essential family of inositol polyphosphate 5-phosphatases (INP51, INP52 and INP53 gene products) in the yeast Saccharomyces cerevisiae."
    Stolz L.E., Huynh C.V., Thorner J., York J.D.
    Genetics 148:1715-1729(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  7. "Synaptojanin family members are implicated in endocytic membrane traffic in yeast."
    Singer-Krueger B., Nemoto Y., Daniell L., Ferro-Novick S., De Camilli P.
    J. Cell Sci. 111:3347-3356(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. "SAC1-like domains of yeast SAC1, INP52, and INP53 and of human synaptojanin encode polyphosphoinositide phosphatases."
    Guo S., Stolz L.E., Lemrow S.M., York J.D.
    J. Biol. Chem. 274:12990-12995(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DOMAIN.
  9. "SAC1 encodes a regulated lipid phosphoinositide phosphatase, defects in which can be suppressed by the homologous Inp52p and Inp53p phosphatases."
    Hughes W.E., Woscholski R., Cooke F.T., Patrick R.S., Dove S.K., McDonald N.Q., Parker P.J.
    J. Biol. Chem. 275:801-808(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  10. "The inositol polyphosphate 5-phosphatases and the apurinic/apyrimidinic base excision repair endonucleases share a common mechanism for catalysis."
    Whisstock J.C., Romero S., Gurung R., Nandurkar H., Ooms L.M., Bottomley S.P., Mitchell C.A.
    J. Biol. Chem. 275:37055-37061(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF GLU-631; HIS-730 AND ASP-771.
  11. "The yeast inositol polyphosphate 5-phosphatases inp52p and inp53p translocate to actin patches following hyperosmotic stress: mechanism for regulating phosphatidylinositol 4,5-bisphosphate at plasma membrane invaginations."
    Ooms L.M., McColl B.K., Wiradjaja F., Wijayaratnam A.P.W., Gleeson P., Gething M.J., Sambrook J.F., Mitchell C.A.
    Mol. Cell. Biol. 20:9376-9390(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  12. "Mammalian inositol polyphosphate 5-phosphatase II can compensate for the absence of all three yeast Sac1-like-domain-containing 5-phosphatases."
    O'Malley C.J., McColl B.K., Kong A.M., Ellis S.L., Wijayaratnam A.P.W., Sambrook J., Mitchell C.A.
    Biochem. J. 355:805-817(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  13. "Bsp1p/Ypr171p is an adapter that directly links some synaptojanin family members to the cortical actin cytoskeleton in yeast."
    Wicky S., Frischmuth S., Singer-Krueger B.
    FEBS Lett. 537:35-41(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH BSP1.
  14. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  15. "Essential role for the myotubularin-related phosphatase Ymr1p and the synaptojanin-like phosphatases Sjl2p and Sjl3p in regulation of phosphatidylinositol 3-phosphate in yeast."
    Parrish W.R., Stefan C.J., Emr S.D.
    Mol. Biol. Cell 15:3567-3579(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  16. "Interaction of Pik1p and Sjl proteins in membrane trafficking."
    Nguyen P.H., Hasek J., Kohlwein S.D., Romero C., Choi J.H., Vancura A.
    FEMS Yeast Res. 5:363-371(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  17. "The phosphoinositide phosphatase Sjl2 is recruited to cortical actin patches in the control of vesicle formation and fission during endocytosis."
    Stefan C.J., Padilla S.M., Audhya A., Emr S.D.
    Mol. Cell. Biol. 25:2910-2923(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH ABP1.
  18. "Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway."
    Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N.
    Mol. Cell. Proteomics 4:310-327(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1005, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: YAL6B.
  19. "Sjl2p is specifically involved in early steps of endocytosis intimately linked to actin dynamics via the Ark1p/Prk1p kinases."
    Boettcher C., Wicky S., Schwarz H., Singer-Krueger B.
    FEBS Lett. 580:633-641(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  20. "PtdIns(4,5)P2 turnover is required for multiple stages during clathrin-and actin-dependent endocytic internalization."
    Sun Y., Carroll S., Kaksonen M., Toshima J.Y., Drubin D.G.
    J. Cell Biol. 177:355-367(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  21. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
    Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
    J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1032, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  22. "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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-152, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  23. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-522; SER-1005 AND SER-1016, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiINP52_YEAST
AccessioniPrimary (citable) accession number: P50942
Secondary accession number(s): D6W174
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: May 11, 2016
This is version 137 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome XIV
    Yeast (Saccharomyces cerevisiae) chromosome XIV: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.