Actin cytoskeleton-regulatory complex protein PAN1 - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

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P32521 (PAN1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 125. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Actin cytoskeleton-regulatory complex protein PAN1

Alternative name(s):
Mitochondrial distribution of proteins protein 3

Gene names

Name:	PAN1
Synonyms:	DIM2, MDP3, MIP3
Ordered Locus Names:	YIR006C
ORF Names:	YIB6C

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces ›

Protein attributes

Sequence length	1480 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.5 Ref.6 Ref.7 Ref.8 Ref.10 Ref.12 Ref.13 Ref.14 Ref.15 Ref.19 Ref.20 Ref.21 Ref.25
Subunit structure	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. Ref.8 Ref.10 Ref.11 Ref.13 Ref.14 Ref.18 Ref.19 Ref.22 Ref.25 Ref.26
Subcellular location	Cell membrane; Peripheral membrane protein; Cytoplasmic side. Endosome membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasm › cytoskeleton › actin patch. Note: Cytoplasmic and cortical actin patches. Ref.7 Ref.8 Ref.14 Ref.17 Ref.19
Post-translational modification	The N-terminus is blocked.
Sequence similarities	Belongs to the PAN1 family. Contains 2 EH domains.
Caution	Was originally (Ref.1) thought to be a subunit of PAB-dependent poly(A)-specific ribonuclease.

Ontologies

Keywords
Biological process	Endocytosis
Cellular component	Cell membrane Cytoplasm Cytoskeleton Endosome Membrane
Domain	Coiled coil Repeat
Ligand	Actin-binding
PTM	Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	actin cortical patch assembly Inferred from mutant phenotype PubMed 18177206. Source: SGD axial cellular bud site selection Inferred from mutant phenotype Ref.7. Source: SGD bipolar cellular bud site selection Inferred from mutant phenotype Ref.7. Source: SGD endocytosis Inferred from mutant phenotype Ref.6. Source: SGD
Cellular_component	actin cortical patch Inferred from direct assay Ref.17. Source: SGD endosome membrane Inferred from electronic annotation. Source: UniProtKB-SubCell mating projection tip Inferred from direct assay PubMed 19053807. Source: SGD nucleus Inferred from direct assay PubMed 17967424. Source: SGD plasma membrane Inferred from direct assay PubMed 11914276. Source: SGD
Molecular_function	calcium ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct
END3	P39013	9	EBI-12875,EBI-6460
SLA1	P32790	5	EBI-12875,EBI-17313
YAP1801	P38856	4	EBI-12875,EBI-24811

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1480

1480

Actin cytoskeleton-regulatory complex protein PAN1

PRO_0000058221

Regions

Repeat

142 – 153

1-1

Repeat

164 – 175

1-2

Repeat

188 – 199

1-3

Repeat

215 – 226

1-4

Repeat

235 – 246

1-5

Domain

270 – 359

EH 1

Repeat

328 – 350

2-1

Repeat

392 – 403

1-6

Repeat

409 – 420

1-7

Repeat

422 – 433

1-8

Repeat

446 – 457

1-9

Repeat

467 – 478

1-10

Repeat

498 – 509

1-11

Repeat

510 – 518

1-12

Repeat

538 – 548

1-13

Repeat

549 – 556

1-14

Repeat

564 – 575

1-15

Domain

600 – 689

EH 2

Repeat

658 – 680

2-2

Repeat

1084 – 1089

3-1

Repeat

1090 – 1095

3-2

Repeat

1096 – 1101

3-3

Repeat

1102 – 1107

3-4

Repeat

1108 – 1113

3-5

Repeat

1114 – 1119

3-6

Repeat

1120 – 1125

3-7

Repeat

1315 – 1320

4-1

Repeat

1321 – 1326

4-2

Repeat

1327 – 1332

4-3

Repeat

1340 – 1345

4-4

Repeat

1346 – 1350

4-5

Repeat

1355 – 1360

4-6

Repeat

1361 – 1366

4-7

Repeat

1372 – 1377

4-8

Region

142 – 575

434

15 X 12 AA tandem repeats of [SPNAG]-[IL]-[QKNGT]-[PSA]-[QT]-[GQAPISTLYK]-T-G-[YFGML]-[YVMGAQL]-[QVLNPAG]-[ASQPN]

Region

328 – 680

353

2 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]-S

Region

1084 – 1125

7 X 6 AA tandem repeats of Q-[PS]-T-Q-P-V

Region

1315 – 1377

8 X 6 AA repeats of [ATVSP]-P-[LVI]-P-[SPQILA]-[VAS]

Coiled coil

1131 – 1190

Potential

Compositional bias

13 – 22

Poly-Gln

Compositional bias

29 – 34

Poly-Gln

Compositional bias

98 – 106

Poly-Gln

Compositional bias

1400 – 1406

Poly-Pro

Compositional bias

1452 – 1455

Poly-Glu

Compositional bias

1474 – 1480

Poly-Pro

Amino acid modifications

Modified residue

241

Phosphothreonine Ref.29

Modified residue

246

Phosphoserine Ref.29

Modified residue

566

Phosphothreonine Ref.29

Modified residue

570

Phosphothreonine Ref.29

Modified residue

747

Phosphoserine Ref.29

Modified residue

757

Phosphoserine Ref.29

Modified residue

758

Phosphoserine Ref.29

Modified residue

986

Phosphoserine Ref.29

Modified residue

991

Phosphoserine Ref.29

Modified residue

995

Phosphothreonine Ref.24 Ref.29

Modified residue

1003

Phosphoserine Ref.16 Ref.23 Ref.24 Ref.29

Modified residue

1007

Phosphoserine Ref.29

Modified residue

1135

Phosphoserine Ref.27 Ref.29

Modified residue

1180

Phosphoserine Ref.29

Modified residue

1250

Phosphoserine Ref.29

Modified residue

1252

Phosphoserine Ref.16 Ref.29

Modified residue

1253

Phosphoserine Ref.29

Modified residue

1256

Phosphothreonine Ref.16 Ref.29

Modified residue

1281

Phosphoserine Ref.24

Modified residue

1321

Phosphothreonine Ref.29

Experimental info

Sequence conflict

235

P → T in AAA34841. Ref.1

Sequence conflict

266 – 273

ITAQDQAK → YYCPRSGKN in AAA34841. Ref.1

Sequence conflict

474 – 487

Missing AA sequence Ref.1

Sequence conflict

653 – 657

Missing in AAA34841. Ref.1

Sequence conflict

1291

A → R in AAA34841. Ref.1

Sequence conflict

1396 – 1480

GGVLP…PPPLP → EAFCLHPHLYQLNKLPLQNL LSLTLITTMVLKKARAHMDP ILMMTFYRFLNQLVQMKRKK GHNQFLLQVSHQFHLQVFLH PHPFHEDLICFL in AAA34841. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

P32521 [UniParc].

Last modified February 1, 1995. Version 2.
Checksum: F3518495FF759553
Show »

FASTA

1,480

160,267

        10         20         30         40         50         60 
MYNPYQQQGM GYQQQQQQQQ QQPNGFYPQQ QQGQSSNQPQ GQPQPQQQMA FNQPQATGIG 

        70         80         90        100        110        120 
GMPQSFGNSF SSMPQQPQTG YNNNGNNGSV YGNGNFGQQP QQQQQQAKPQ HTGYVPNSSM 

       130        140        150        160        170        180 
PMMNTTGTMP PPNPAQQPQL QSIQPQGTGY YQAANTANVH SVQPLQSQGT GYYVSTPNLI 

       190        200        210        220        230        240 
SSNQTQQPLQ AQGTGYYQSQ PQQVPPPQQA QSLQPLKPQQ TGFYLQPQNQ APLEPLKPTA 

       250        260        270        280        290        300 
TGFVNSFANN GLNNDIKIPA IRLSFITAQD QAKFETLFRS IVTNGSNTVS GANCRKILMR 

       310        320        330        340        350        360 
SGLPPSQLAR IWTLCDTSKA GELLFPEFAL AMHLINDVLQ GDTIPYELDS KTKNEVSSFI 

       370        380        390        400        410        420 
DAINLSIANQ DSSANDAPKT PFDEFITAGV QNLQPQPTGY MPQTSFGIPL QSQITGGGVA 

       430        440        450        460        470        480 
SALNPQSTGF MAPTTFNMSM NTGTPGLNPQ ITGGAPASMQ PNITGNALQP QTTGMMPQTT 

       490        500        510        520        530        540 
GMMPQTTGMM PQTSFGVNLG PQLTGGALQS QYTGGYGSVM PQQSGPASMP NLSFNQQGLQ 

       550        560        570        580        590        600 
SQLTGLQPQP TGFLPPSNFS ATMPLTAQKT GFGNNEIYTK SNFNNNLIDN SSQDKISTEE 

       610        620        630        640        650        660 
KSLFYKIFET FDTQNKGLLD SPTAVEIFRK SGLNRADLEQ IWNLCDINNT GQLNKQEFAL 

       670        680        690        700        710        720 
GMHLVYGKLN GKPIPNVLPS SLIPSSTKLL DNLKNQLKTE PTTTKEKPSF GKIDALSYKN 

       730        740        750        760        770        780 
NDDDVLPNYR NRRKVYSAKN EEQSSFSSPS AKSVNHSSST LQTDDISVDK TVEKKTAKPK 

       790        800        810        820        830        840 
YAGFSREINL KNIASLENEI KNISNPENCY DSSIPSDLTS RFDAIIAKLP NLFNEISTID 

       850        860        870        880        890        900 
NEITNAKIQL YRKKNPSSII GSGPNGEITE NDRKKAKSRA LLRARMSALT GKSTESEDSL 

       910        920        930        940        950        960 
SMEDEQQSAE IKRIQQENGK NQEIIKDIRS SISDISASLK STMTGSNMIS NQEFERWEFG 

       970        980        990       1000       1010       1020 
IGLEDGVREF LDDLKSNSNK SVTESSPFVP SSTPTPVDDR SSSPSYSQFK TAEERAAYLK 

      1030       1040       1050       1060       1070       1080 
EQAKKRMKEK LAKFDKNRRN VTQSSRSISS ENSREQPQQI AGSSNLVEPR ATPFQEEKYV 

      1090       1100       1110       1120       1130       1140 
EVAQPTQPVQ STQPVQPTQP VQPTQPVQPT QPVQPTQPVQ PTQPVQNVYN AKQESDDEDE 

      1150       1160       1170       1180       1190       1200 
DDEEKRLQEE LKRLKLKKKA DKEKRLAALR KQIEDAQNES DEEETNGKDN FGGHVNVPQA 

      1210       1220       1230       1240       1250       1260 
APVAPSAAFS QNSTNAPRSV HAAVTPAAGK NSTGLPSTTM GHNPYFKDAS ASSTSTFDAR 

      1270       1280       1290       1300       1310       1320 
AAEMQRRIQR GLDEDEDDGW SDEDESNNRV AVDNKVEEAK IGHPDHARAP PVTAAPLPSV 

      1330       1340       1350       1360       1370       1380 
TPVPPAVPVP QANTSNEKSS PIPIAPIPPS VTQEPPVPLA PPLPAVDGFQ EPPIPSAPAI 

      1390       1400       1410       1420       1430       1440 
ATAVQKSGSS TPALAGGVLP PPPPLPTQQA STSEPIIAHV DNYNGAEKGT GAYGSDSDDD 

      1450       1460       1470       1480 
VLSIPESVGT DEEEEGAQPV STAGIPSIPP AGIPPPPPLP

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome IX." Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D., Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N., Harris D.E., Horsnell T., Hunt S., Jagels K., Jones M., Lye G., Moule S., Odell C. Barrell B.G. Nature 387:84-87(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[4]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases 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]	"Recognition specificity of individual EH domains of mammals and yeast." Paoluzi S., Castagnoli L., Lauro I., Salcini A.E., Coda L., Fre' S., Confalonieri S., Pelicci P.G., Di Fiore P.P., Cesareni G. EMBO J. 17:6541-6550(1998) [PubMed] [Europe PMC] [Abstract] 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]	"Phosphoproteome analysis by mass spectrometry and its application to Saccharomyces cerevisiae." Ficarro S.B., McCleland M.L., Stukenberg P.T., Burke D.J., Ross M.M., Shabanowitz J., Hunt D.F., White F.M. Nat. Biotechnol. 20:301-305(2002) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1003; SER-1252 AND THR-1256, MASS SPECTROMETRY. Strain: 2124.
[17]	"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.
[18]	"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.
[19]	"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.
[20]	"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.
[21]	"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.
[22]	"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, MASS SPECTROMETRY.
[23]	"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-1003, MASS SPECTROMETRY. Strain: YAL6B.
[24]	"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, MASS SPECTROMETRY. Strain: ADR376.
[25]	"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.
[26]	"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.
[27]	"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1135, MASS SPECTROMETRY.
[28]	"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.
[29]	"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; SER-246; THR-566; THR-570; SER-747; SER-757; SER-758; SER-986; SER-991; THR-995; SER-1003; SER-1007; SER-1135; SER-1180; SER-1250; SER-1252; SER-1253; THR-1256 AND THR-1321, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Z38062 Genomic DNA. Translation: CAA86208.1. X79743 Genomic DNA. Translation: CAB38097.1. M90688 Genomic DNA. Translation: AAA34841.1. BK006942 Genomic DNA. Translation: DAA08552.1.
PIR	S48440.
RefSeq	NP_012271.3. NM_001179528.3.
3D structure databases
ProteinModelPortal	P32521.
SMR	P32521. Positions 273-345, 604-686.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-1340N.
IntAct	P32521. 20 interactions.
MINT	MINT-398969.
STRING	4932.YIR006C.
Proteomic databases
PaxDb	P32521.
PeptideAtlas	P32521.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YIR006C; YIR006C; YIR006C.
GeneID	854822.
KEGG	sce:YIR006C. sce:YIR013C.
Organism-specific databases
CYGD	YIR006c.
SGD	S000001445. PAN1.
Phylogenomic databases
eggNOG	NOG253201.
GeneTree	ENSGT00680000101300.
OMA	VAMHLIY.
OrthoDB	EOG4V9Z04.
Gene expression databases
Genevestigator	P32521.
GermOnline	YIR006C. Saccharomyces cerevisiae.
Family and domain databases
Gene3D	1.10.238.10. 2 hits.
InterPro	IPR013182. DUF1720. IPR011992. EF-hand-like_dom. IPR018247. EF_Hand_1_Ca_BS. IPR002048. EF_hand_dom. IPR000261. EPS15_homology. IPR026812. Pan1. [Graphical view]
PANTHER	PTHR11216:SF35. PTHR11216:SF35. 1 hit.
Pfam	PF08226. DUF1720. 3 hits. [Graphical view]
SMART	SM00054. EFh. 3 hits. SM00027. EH. 2 hits. [Graphical view]
PROSITE	PS50222. EF_HAND_2. 3 hits. PS50031. EH. 2 hits. [Graphical view]
ProtoNet	Search...
Other
NextBio	977672.

Entry information

Entry name

PAN1_YEAST

Accession

Primary (citable) accession number: P32521
Secondary accession number(s): D6VVT6

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1993
Last sequence update:	February 1, 1995
Last modified:	May 1, 2013
This is version 125 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Yeast chromosome IX

Yeast (Saccharomyces cerevisiae) chromosome IX: entries and gene names

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

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