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P32521

- PAN1_YEAST

UniProt

P32521 - PAN1_YEAST

Protein

Actin cytoskeleton-regulatory complex protein PAN1

Gene

PAN1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 137 (01 Oct 2014)
      Sequence version 2 (01 Feb 1995)
      Previous versions | rss
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    Functioni

    Component of the PAN1 actin cytoskeleton-regulatory complex required for the internalization of endosomes during actin-coupled endocytosis. The complex links the site of endocytosis to the cell membrane-associated actin cytoskeleton. Mediates uptake of external molecules and vacuolar degradation of plasma membrane proteins. Plays a role in the proper organization of the cell membrane-associated actin cytoskeleton and promotes its destabilization. Required for the bipolar budding of diploid cells and the correct distribution of chitin at the cell surface.13 Publications

    GO - Molecular functioni

    1. calcium ion binding Source: InterPro
    2. protein binding Source: IntAct
    3. protein binding, bridging Source: SGD

    GO - Biological processi

    1. actin cortical patch assembly Source: SGD
    2. axial cellular bud site selection Source: SGD
    3. bipolar cellular bud site selection Source: SGD
    4. endocytosis Source: SGD

    Keywords - Biological processi

    Endocytosis

    Keywords - Ligandi

    Actin-binding

    Enzyme and pathway databases

    BioCyciYEAST:G3O-31427-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Actin cytoskeleton-regulatory complex protein PAN1
    Alternative name(s):
    Mitochondrial distribution of proteins protein 3
    Gene namesi
    Name:PAN1
    Synonyms:DIM2, MDP3, MIP3
    Ordered Locus Names:YIR006C
    ORF Names:YIB6C
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome IX

    Organism-specific databases

    CYGDiYIR006c.
    SGDiS000001445. PAN1.

    Subcellular locationi

    GO - Cellular componenti

    1. actin cortical patch Source: SGD
    2. cytoplasm Source: SGD
    3. endosome membrane Source: UniProtKB-SubCell
    4. nucleus Source: SGD
    5. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Cytoskeleton, Endosome, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 14801480Actin cytoskeleton-regulatory complex protein PAN1PRO_0000058221Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei241 – 2411Phosphothreonine1 Publication
    Modified residuei570 – 5701Phosphothreonine2 Publications
    Modified residuei747 – 7471Phosphoserine1 Publication
    Modified residuei757 – 7571Phosphoserine2 Publications
    Modified residuei993 – 9931Phosphothreonine1 Publication
    Modified residuei995 – 9951Phosphothreonine3 Publications
    Modified residuei1003 – 10031Phosphoserine2 Publications
    Modified residuei1180 – 11801Phosphoserine1 Publication
    Modified residuei1250 – 12501Phosphoserine2 Publications
    Modified residuei1253 – 12531Phosphoserine1 Publication
    Modified residuei1281 – 12811Phosphoserine2 Publications
    Modified residuei1321 – 13211Phosphothreonine1 Publication

    Post-translational modificationi

    The N-terminus is blocked.

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP32521.
    PaxDbiP32521.
    PeptideAtlasiP32521.

    Expressioni

    Gene expression databases

    GenevestigatoriP32521.

    Interactioni

    Subunit structurei

    Forms homooligomers. Component of the PAN1 actin cytoskeleton-regulatory complex composed of at least END3, PAN1, and SLA1. Interacts directly with END3, and with ENT1, SCD5, SLA2, YAP1801 and YAP1802.10 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    END3P390139EBI-12875,EBI-6460
    MYO5Q044392EBI-12875,EBI-11687
    SLA1P327905EBI-12875,EBI-17313
    YAP1801P388564EBI-12875,EBI-24811

    Protein-protein interaction databases

    BioGridi34997. 60 interactions.
    DIPiDIP-1340N.
    IntActiP32521. 22 interactions.
    MINTiMINT-398969.
    STRINGi4932.YIR006C.

    Structurei

    3D structure databases

    ProteinModelPortaliP32521.
    SMRiP32521. Positions 273-345, 604-686.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati142 – 153121-1Add
    BLAST
    Repeati164 – 175121-2Add
    BLAST
    Repeati188 – 199121-3Add
    BLAST
    Repeati215 – 226121-4Add
    BLAST
    Repeati235 – 246121-5Add
    BLAST
    Domaini270 – 35990EH 1PROSITE-ProRule annotationAdd
    BLAST
    Repeati328 – 350232-1Add
    BLAST
    Repeati392 – 403121-6Add
    BLAST
    Repeati409 – 420121-7Add
    BLAST
    Repeati422 – 433121-8Add
    BLAST
    Repeati446 – 457121-9Add
    BLAST
    Repeati467 – 478121-10Add
    BLAST
    Repeati498 – 509121-11Add
    BLAST
    Repeati510 – 51891-12
    Repeati538 – 548111-13Add
    BLAST
    Repeati549 – 55681-14
    Repeati564 – 575121-15Add
    BLAST
    Domaini600 – 68990EH 2PROSITE-ProRule annotationAdd
    BLAST
    Repeati658 – 680232-2Add
    BLAST
    Repeati1084 – 108963-1
    Repeati1090 – 109563-2
    Repeati1096 – 110163-3
    Repeati1102 – 110763-4
    Repeati1108 – 111363-5
    Repeati1114 – 111963-6
    Repeati1120 – 112563-7
    Repeati1315 – 132064-1
    Repeati1321 – 132664-2
    Repeati1327 – 133264-3
    Repeati1340 – 134564-4
    Repeati1346 – 135054-5
    Repeati1355 – 136064-6
    Repeati1361 – 136664-7
    Repeati1372 – 137764-8

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni142 – 57543415 X 12 AA tandem repeats of [SPNAG]-[IL]-[QKNGT]-[PSA]-[QT]-[GQAPISTLYK]-T-G-[YFGML]-[YVMGAQL]-[QVLNPAG]-[ASQPN]Add
    BLAST
    Regioni328 – 6803532 X 23 AA repeats of F-A-L-[AG]-M-H-L-[IV]-[NY]-[DG]-[VK]-L-[QN]-G-[DK]-[TP]-I-P-[YN]-[EV]-L-[DP]-SAdd
    BLAST
    Regioni1084 – 1125427 X 6 AA tandem repeats of Q-[PS]-T-Q-P-VAdd
    BLAST
    Regioni1315 – 1377638 X 6 AA repeats of [ATVSP]-P-[LVI]-P-[SPQILA]-[VAS]Add
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili1131 – 119060Sequence AnalysisAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi13 – 2210Poly-Gln
    Compositional biasi29 – 346Poly-Gln
    Compositional biasi98 – 1069Poly-Gln
    Compositional biasi1400 – 14067Poly-Pro
    Compositional biasi1452 – 14554Poly-Glu
    Compositional biasi1474 – 14807Poly-Pro

    Sequence similaritiesi

    Belongs to the PAN1 family.Curated
    Contains 2 EH domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil, Repeat

    Phylogenomic databases

    eggNOGiNOG253201.
    GeneTreeiENSGT00730000114400.
    OMAiWGLVNAP.
    OrthoDBiEOG7P2Z1C.

    Family and domain databases

    Gene3Di1.10.238.10. 2 hits.
    InterProiIPR013182. DUF1720.
    IPR011992. EF-hand-dom_pair.
    IPR018247. EF_Hand_1_Ca_BS.
    IPR002048. EF_hand_dom.
    IPR000261. EPS15_homology.
    IPR026812. Pan1_fungal.
    [Graphical view]
    PANTHERiPTHR11216:SF35. PTHR11216:SF35. 1 hit.
    PfamiPF08226. DUF1720. 2 hits.
    [Graphical view]
    SMARTiSM00054. EFh. 3 hits.
    SM00027. EH. 2 hits.
    [Graphical view]
    PROSITEiPS50222. EF_HAND_2. 3 hits.
    PS50031. EH. 2 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P32521-1 [UniParc]FASTAAdd to Basket

    « Hide

    MYNPYQQQGM GYQQQQQQQQ QQPNGFYPQQ QQGQSSNQPQ GQPQPQQQMA     50
    FNQPQATGIG GMPQSFGNSF SSMPQQPQTG YNNNGNNGSV YGNGNFGQQP 100
    QQQQQQAKPQ HTGYVPNSSM PMMNTTGTMP PPNPAQQPQL QSIQPQGTGY 150
    YQAANTANVH SVQPLQSQGT GYYVSTPNLI SSNQTQQPLQ AQGTGYYQSQ 200
    PQQVPPPQQA QSLQPLKPQQ TGFYLQPQNQ APLEPLKPTA TGFVNSFANN 250
    GLNNDIKIPA IRLSFITAQD QAKFETLFRS IVTNGSNTVS GANCRKILMR 300
    SGLPPSQLAR IWTLCDTSKA GELLFPEFAL AMHLINDVLQ GDTIPYELDS 350
    KTKNEVSSFI DAINLSIANQ DSSANDAPKT PFDEFITAGV QNLQPQPTGY 400
    MPQTSFGIPL QSQITGGGVA SALNPQSTGF MAPTTFNMSM NTGTPGLNPQ 450
    ITGGAPASMQ PNITGNALQP QTTGMMPQTT GMMPQTTGMM PQTSFGVNLG 500
    PQLTGGALQS QYTGGYGSVM PQQSGPASMP NLSFNQQGLQ SQLTGLQPQP 550
    TGFLPPSNFS ATMPLTAQKT GFGNNEIYTK SNFNNNLIDN SSQDKISTEE 600
    KSLFYKIFET FDTQNKGLLD SPTAVEIFRK SGLNRADLEQ IWNLCDINNT 650
    GQLNKQEFAL GMHLVYGKLN GKPIPNVLPS SLIPSSTKLL DNLKNQLKTE 700
    PTTTKEKPSF GKIDALSYKN NDDDVLPNYR NRRKVYSAKN EEQSSFSSPS 750
    AKSVNHSSST LQTDDISVDK TVEKKTAKPK YAGFSREINL KNIASLENEI 800
    KNISNPENCY DSSIPSDLTS RFDAIIAKLP NLFNEISTID NEITNAKIQL 850
    YRKKNPSSII GSGPNGEITE NDRKKAKSRA LLRARMSALT GKSTESEDSL 900
    SMEDEQQSAE IKRIQQENGK NQEIIKDIRS SISDISASLK STMTGSNMIS 950
    NQEFERWEFG IGLEDGVREF LDDLKSNSNK SVTESSPFVP SSTPTPVDDR 1000
    SSSPSYSQFK TAEERAAYLK EQAKKRMKEK LAKFDKNRRN VTQSSRSISS 1050
    ENSREQPQQI AGSSNLVEPR ATPFQEEKYV EVAQPTQPVQ STQPVQPTQP 1100
    VQPTQPVQPT QPVQPTQPVQ PTQPVQNVYN AKQESDDEDE DDEEKRLQEE 1150
    LKRLKLKKKA DKEKRLAALR KQIEDAQNES DEEETNGKDN FGGHVNVPQA 1200
    APVAPSAAFS QNSTNAPRSV HAAVTPAAGK NSTGLPSTTM GHNPYFKDAS 1250
    ASSTSTFDAR AAEMQRRIQR GLDEDEDDGW SDEDESNNRV AVDNKVEEAK 1300
    IGHPDHARAP PVTAAPLPSV TPVPPAVPVP QANTSNEKSS PIPIAPIPPS 1350
    VTQEPPVPLA PPLPAVDGFQ EPPIPSAPAI ATAVQKSGSS TPALAGGVLP 1400
    PPPPLPTQQA STSEPIIAHV DNYNGAEKGT GAYGSDSDDD VLSIPESVGT 1450
    DEEEEGAQPV STAGIPSIPP AGIPPPPPLP 1480
    Length:1,480
    Mass (Da):160,267
    Last modified:February 1, 1995 - v2
    Checksum:iF3518495FF759553
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti235 – 2351P → T in AAA34841. (PubMed:1339314)Curated
    Sequence conflicti266 – 2738ITAQDQAK → YYCPRSGKN in AAA34841. (PubMed:1339314)Curated
    Sequence conflicti474 – 48714Missing AA sequence (PubMed:1339314)CuratedAdd
    BLAST
    Sequence conflicti653 – 6575Missing in AAA34841. (PubMed:1339314)Curated
    Sequence conflicti1291 – 12911A → R in AAA34841. (PubMed:1339314)Curated
    Sequence conflicti1396 – 148085GGVLP…PPPLP → EAFCLHPHLYQLNKLPLQNL LSLTLITTMVLKKARAHMDP ILMMTFYRFLNQLVQMKRKK GHNQFLLQVSHQFHLQVFLH PHPFHEDLICFL in AAA34841. (PubMed:1339314)CuratedAdd
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z38062 Genomic DNA. Translation: CAA86208.1.
    X79743 Genomic DNA. Translation: CAB38097.1.
    M90688 Genomic DNA. Translation: AAA34841.1.
    BK006942 Genomic DNA. Translation: DAA08552.1.
    PIRiS48440.
    RefSeqiNP_012271.3. NM_001179528.3.

    Genome annotation databases

    EnsemblFungiiYIR006C; YIR006C; YIR006C.
    GeneIDi854822.
    KEGGisce:YIR006C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z38062 Genomic DNA. Translation: CAA86208.1 .
    X79743 Genomic DNA. Translation: CAB38097.1 .
    M90688 Genomic DNA. Translation: AAA34841.1 .
    BK006942 Genomic DNA. Translation: DAA08552.1 .
    PIRi S48440.
    RefSeqi NP_012271.3. NM_001179528.3.

    3D structure databases

    ProteinModelPortali P32521.
    SMRi P32521. Positions 273-345, 604-686.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 34997. 60 interactions.
    DIPi DIP-1340N.
    IntActi P32521. 22 interactions.
    MINTi MINT-398969.
    STRINGi 4932.YIR006C.

    Proteomic databases

    MaxQBi P32521.
    PaxDbi P32521.
    PeptideAtlasi P32521.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YIR006C ; YIR006C ; YIR006C .
    GeneIDi 854822.
    KEGGi sce:YIR006C.

    Organism-specific databases

    CYGDi YIR006c.
    SGDi S000001445. PAN1.

    Phylogenomic databases

    eggNOGi NOG253201.
    GeneTreei ENSGT00730000114400.
    OMAi WGLVNAP.
    OrthoDBi EOG7P2Z1C.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-31427-MONOMER.

    Miscellaneous databases

    NextBioi 977672.
    PROi P32521.

    Gene expression databases

    Genevestigatori P32521.

    Family and domain databases

    Gene3Di 1.10.238.10. 2 hits.
    InterProi IPR013182. DUF1720.
    IPR011992. EF-hand-dom_pair.
    IPR018247. EF_Hand_1_Ca_BS.
    IPR002048. EF_hand_dom.
    IPR000261. EPS15_homology.
    IPR026812. Pan1_fungal.
    [Graphical view ]
    PANTHERi PTHR11216:SF35. PTHR11216:SF35. 1 hit.
    Pfami PF08226. DUF1720. 2 hits.
    [Graphical view ]
    SMARTi SM00054. EFh. 3 hits.
    SM00027. EH. 2 hits.
    [Graphical view ]
    PROSITEi PS50222. EF_HAND_2. 3 hits.
    PS50031. EH. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Translation initiation requires the PAB-dependent poly(A) ribonuclease in yeast."
      Sachs A.B., Deardorff J.A.
      Cell 70:961-973(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 320-344; 352-375 AND 899-906.
    2. "Nucleotide sequence and analysis of the centromeric region of yeast chromosome IX."
      Voss H., Tamames J., Teodoru C., Valencia A., Sensen C., Wiemann S., Schwager C., Zimmermann J., Sander C., Ansorge W.
      Yeast 11:61-78(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    4. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    5. "Mutations altering the mitochondrial-cytoplasmic distribution of Mod5p implicate the actin cytoskeleton and mRNA 3' ends and/or protein synthesis in mitochondrial delivery."
      Zoladek T., Vaduva G., Hunter L.A., Boguta M., Go B.D., Martin N.C., Hopper A.K.
      Mol. Cell. Biol. 15:6884-6894(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    6. "A novel fluorescence-activated cell sorter-based screen for yeast endocytosis mutants identifies a yeast homologue of mammalian eps15."
      Wendland B., McCaffery J.M., Xiao Q., Emr S.D.
      J. Cell Biol. 135:1485-1500(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DOMAIN.
    7. "The EH-domain-containing protein Pan1 is required for normal organization of the actin cytoskeleton in Saccharomyces cerevisiae."
      Tang H.-Y., Cai M.
      Mol. Cell. Biol. 16:4897-4914(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, DOMAIN.
    8. "EH domain proteins Pan1p and End3p are components of a complex that plays a dual role in organization of the cortical actin cytoskeleton and endocytosis in Saccharomyces cerevisiae."
      Tang H.-Y., Munn A., Cai M.
      Mol. Cell. Biol. 17:4294-4304(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE PAN1 COMPLEX, FUNCTION OF THE PAN1 COMPLEX, SUBCELLULAR LOCATION.
    9. Cited for: EH DOMAINS.
    10. "Pan1p, yeast eps15, functions as a multivalent adaptor that coordinates protein-protein interactions essential for endocytosis."
      Wendland B., Emr S.D.
      J. Cell Biol. 141:71-84(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH YAP1801 AND YAP1802.
    11. "Regulation of the actin cytoskeleton organization in yeast by a novel serine/threonine kinase Prk1p."
      Zeng G., Cai M.
      J. Cell Biol. 144:71-82(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION BY PRK1, INTERACTION WITH END3.
    12. "A novel EH domain protein of Saccharomyces cerevisiae, Ede1p, involved in endocytosis."
      Gagny B., Wiederkehr A., Dumoulin P., Winsor B., Riezman H., Haguenauer-Tsapis R.
      J. Cell Sci. 113:3309-3319(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    13. "Pan1p, End3p, and Sla1p, three yeast proteins required for normal cortical actin cytoskeleton organization, associate with each other and play essential roles in cell wall morphogenesis."
      Tang H.-Y., Xu J., Cai M.
      Mol. Cell. Biol. 20:12-25(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, IDENTIFICATION IN THE PAN1 COMPLEX.
    14. "Regulation of yeast actin cytoskeleton-regulatory complex Pan1p/Sla1p/End3p by serine/threonine kinase Prk1p."
      Zeng G., Yu X., Cai M.
      Mol. Biol. Cell 12:3759-3772(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE PAN1 COMPLEX, FUNCTION OF THE PAN1 COMPLEX, SUBCELLULAR LOCATION, PHOSPHORYLATION BY PRK1.
    15. "Large-scale identification of genes important for apical growth in Saccharomyces cerevisiae by directed allele replacement technology (DART) screening."
      Bidlingmaier S., Snyder M.A.
      Funct. Integr. Genomics 1:345-356(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    16. "A pathway for association of receptors, adaptors, and actin during endocytic internalization."
      Kaksonen M., Sun Y., Drubin D.G.
      Cell 115:475-487(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    17. "The yeast Epsin Ent1 is recruited to membranes through multiple independent interactions."
      Aguilar R.C., Watson H.A., Wendland B.
      J. Biol. Chem. 278:10737-10743(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ENT1.
    18. "The function of the endocytic scaffold protein Pan1p depends on multiple domains."
      Miliaras N.B., Park J.-H., Wendland B.
      Traffic 5:963-978(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, DOMAINS, SUBUNIT.
    19. "Pan1p, an actin cytoskeleton-associated protein, is required for growth of yeast on oleate medium."
      Kaminska J., Wysocka-Kapcinska M., Smaczynska-de Rooij I., Rytka J., Zoladek T.
      Exp. Cell Res. 310:482-492(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    20. "Dissection of Arp2/3 complex actin nucleation mechanism and distinct roles for its nucleation-promoting factors in Saccharomyces cerevisiae."
      D'Agostino J.L., Goode B.L.
      Genetics 171:35-47(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    21. "Cell polarity protein Spa2P associates with proteins involved in actin function in Saccharomyces cerevisiae."
      Shih J.L., Reck-Peterson S.L., Newitt R., Mooseker M.S., Aebersold R., Herskowitz I.
      Mol. Biol. Cell 16:4595-4608(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SPA2, IDENTIFICATION BY MASS SPECTROMETRY.
    22. "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-995; SER-1003 AND SER-1281, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: ADR376.
    23. "Negative regulation of yeast Eps15-like Arp2/3 complex activator, Pan1p, by the Hip1R-related protein, Sla2p, during endocytosis."
      Toshima J., Toshima J.Y., Duncan M.C., Cope M.J.T.V., Sun Y., Martin A.C., Anderson S., Yates J.R. III, Mizuno K., Drubin D.G.
      Mol. Biol. Cell 18:658-668(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE PAN1 COMPLEX, INTERACTION WITH SLA2, FUNCTION.
    24. "Scd5p mediates phosphoregulation of actin and endocytosis by the type 1 phosphatase Glc7p in yeast."
      Zeng G., Huang B., Neo S.P., Wang J., Cai M.
      Mol. Biol. Cell 18:4885-4898(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SCD5.
    25. "A novel function of Arp2p in mediating Prk1p-specific regulation of actin and endocytosis in yeast."
      Jin M., Cai M.
      Mol. Biol. Cell 19:297-307(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION BY ARK1.
    26. "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 THR-241; THR-570; SER-747; SER-757; THR-995; SER-1250 AND THR-1321, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    27. "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 THR-570; SER-757; THR-993; THR-995; SER-1003; SER-1180; SER-1250; SER-1253 AND SER-1281, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiPAN1_YEAST
    AccessioniPrimary (citable) accession number: P32521
    Secondary accession number(s): D6VVT6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1993
    Last sequence update: February 1, 1995
    Last modified: October 1, 2014
    This is version 137 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Caution

    Was originally thought to be a subunit of PAB-dependent poly(A)-specific ribonuclease.1 Publication

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, 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 IX
      Yeast (Saccharomyces cerevisiae) chromosome IX: entries and gene names

    External Data

    Dasty 3