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P32521

- PAN1_YEAST

UniProt

P32521 - PAN1_YEAST

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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

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, 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
Complete GO annotation...

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 Source: UniProtKB-KW
  4. nucleus Source: SGD
  5. plasma membrane Source: UniProtKB-KW
Complete GO annotation...

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. 61 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.
InParanoidiP32521.
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

        10         20         30         40         50
MYNPYQQQGM GYQQQQQQQQ QQPNGFYPQQ QQGQSSNQPQ GQPQPQQQMA
60 70 80 90 100
FNQPQATGIG GMPQSFGNSF SSMPQQPQTG YNNNGNNGSV YGNGNFGQQP
110 120 130 140 150
QQQQQQAKPQ HTGYVPNSSM PMMNTTGTMP PPNPAQQPQL QSIQPQGTGY
160 170 180 190 200
YQAANTANVH SVQPLQSQGT GYYVSTPNLI SSNQTQQPLQ AQGTGYYQSQ
210 220 230 240 250
PQQVPPPQQA QSLQPLKPQQ TGFYLQPQNQ APLEPLKPTA TGFVNSFANN
260 270 280 290 300
GLNNDIKIPA IRLSFITAQD QAKFETLFRS IVTNGSNTVS GANCRKILMR
310 320 330 340 350
SGLPPSQLAR IWTLCDTSKA GELLFPEFAL AMHLINDVLQ GDTIPYELDS
360 370 380 390 400
KTKNEVSSFI DAINLSIANQ DSSANDAPKT PFDEFITAGV QNLQPQPTGY
410 420 430 440 450
MPQTSFGIPL QSQITGGGVA SALNPQSTGF MAPTTFNMSM NTGTPGLNPQ
460 470 480 490 500
ITGGAPASMQ PNITGNALQP QTTGMMPQTT GMMPQTTGMM PQTSFGVNLG
510 520 530 540 550
PQLTGGALQS QYTGGYGSVM PQQSGPASMP NLSFNQQGLQ SQLTGLQPQP
560 570 580 590 600
TGFLPPSNFS ATMPLTAQKT GFGNNEIYTK SNFNNNLIDN SSQDKISTEE
610 620 630 640 650
KSLFYKIFET FDTQNKGLLD SPTAVEIFRK SGLNRADLEQ IWNLCDINNT
660 670 680 690 700
GQLNKQEFAL GMHLVYGKLN GKPIPNVLPS SLIPSSTKLL DNLKNQLKTE
710 720 730 740 750
PTTTKEKPSF GKIDALSYKN NDDDVLPNYR NRRKVYSAKN EEQSSFSSPS
760 770 780 790 800
AKSVNHSSST LQTDDISVDK TVEKKTAKPK YAGFSREINL KNIASLENEI
810 820 830 840 850
KNISNPENCY DSSIPSDLTS RFDAIIAKLP NLFNEISTID NEITNAKIQL
860 870 880 890 900
YRKKNPSSII GSGPNGEITE NDRKKAKSRA LLRARMSALT GKSTESEDSL
910 920 930 940 950
SMEDEQQSAE IKRIQQENGK NQEIIKDIRS SISDISASLK STMTGSNMIS
960 970 980 990 1000
NQEFERWEFG IGLEDGVREF LDDLKSNSNK SVTESSPFVP SSTPTPVDDR
1010 1020 1030 1040 1050
SSSPSYSQFK TAEERAAYLK EQAKKRMKEK LAKFDKNRRN VTQSSRSISS
1060 1070 1080 1090 1100
ENSREQPQQI AGSSNLVEPR ATPFQEEKYV EVAQPTQPVQ STQPVQPTQP
1110 1120 1130 1140 1150
VQPTQPVQPT QPVQPTQPVQ PTQPVQNVYN AKQESDDEDE DDEEKRLQEE
1160 1170 1180 1190 1200
LKRLKLKKKA DKEKRLAALR KQIEDAQNES DEEETNGKDN FGGHVNVPQA
1210 1220 1230 1240 1250
APVAPSAAFS QNSTNAPRSV HAAVTPAAGK NSTGLPSTTM GHNPYFKDAS
1260 1270 1280 1290 1300
ASSTSTFDAR AAEMQRRIQR GLDEDEDDGW SDEDESNNRV AVDNKVEEAK
1310 1320 1330 1340 1350
IGHPDHARAP PVTAAPLPSV TPVPPAVPVP QANTSNEKSS PIPIAPIPPS
1360 1370 1380 1390 1400
VTQEPPVPLA PPLPAVDGFQ EPPIPSAPAI ATAVQKSGSS TPALAGGVLP
1410 1420 1430 1440 1450
PPPPLPTQQA STSEPIIAHV DNYNGAEKGT GAYGSDSDDD VLSIPESVGT
1460 1470 1480
DEEEEGAQPV STAGIPSIPP AGIPPPPPLP
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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. 61 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.
InParanoidi P32521.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 139 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