Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P32521 (PAN1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 134. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length1480 AA.
Sequence statusComplete.
Protein existenceEvidence 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.18 Ref.19 Ref.20 Ref.23

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.17 Ref.18 Ref.21 Ref.23 Ref.24

Subcellular location

Cell membrane; Peripheral membrane protein; Cytoplasmic side. Endosome membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasmcytoskeletonactin patch. Note: Cytoplasmic and cortical actin patches. Ref.7 Ref.8 Ref.14 Ref.16 Ref.18

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.

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 14801480Actin cytoskeleton-regulatory complex protein PAN1
PRO_0000058221

Regions

Repeat142 – 153121-1
Repeat164 – 175121-2
Repeat188 – 199121-3
Repeat215 – 226121-4
Repeat235 – 246121-5
Domain270 – 35990EH 1
Repeat328 – 350232-1
Repeat392 – 403121-6
Repeat409 – 420121-7
Repeat422 – 433121-8
Repeat446 – 457121-9
Repeat467 – 478121-10
Repeat498 – 509121-11
Repeat510 – 51891-12
Repeat538 – 548111-13
Repeat549 – 55681-14
Repeat564 – 575121-15
Domain600 – 68990EH 2
Repeat658 – 680232-2
Repeat1084 – 108963-1
Repeat1090 – 109563-2
Repeat1096 – 110163-3
Repeat1102 – 110763-4
Repeat1108 – 111363-5
Repeat1114 – 111963-6
Repeat1120 – 112563-7
Repeat1315 – 132064-1
Repeat1321 – 132664-2
Repeat1327 – 133264-3
Repeat1340 – 134564-4
Repeat1346 – 135054-5
Repeat1355 – 136064-6
Repeat1361 – 136664-7
Repeat1372 – 137764-8
Region142 – 57543415 X 12 AA tandem repeats of [SPNAG]-[IL]-[QKNGT]-[PSA]-[QT]-[GQAPISTLYK]-T-G-[YFGML]-[YVMGAQL]-[QVLNPAG]-[ASQPN]
Region328 – 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]-S
Region1084 – 1125427 X 6 AA tandem repeats of Q-[PS]-T-Q-P-V
Region1315 – 1377638 X 6 AA repeats of [ATVSP]-P-[LVI]-P-[SPQILA]-[VAS]
Coiled coil1131 – 119060 Potential
Compositional bias13 – 2210Poly-Gln
Compositional bias29 – 346Poly-Gln
Compositional bias98 – 1069Poly-Gln
Compositional bias1400 – 14067Poly-Pro
Compositional bias1452 – 14554Poly-Glu
Compositional bias1474 – 14807Poly-Pro

Amino acid modifications

Modified residue2411Phosphothreonine Ref.26
Modified residue5701Phosphothreonine Ref.26 Ref.27
Modified residue7471Phosphoserine Ref.26
Modified residue7571Phosphoserine Ref.26 Ref.27
Modified residue9931Phosphothreonine Ref.27
Modified residue9951Phosphothreonine Ref.22 Ref.26 Ref.27
Modified residue10031Phosphoserine Ref.22 Ref.27
Modified residue11801Phosphoserine Ref.27
Modified residue12501Phosphoserine Ref.26 Ref.27
Modified residue12531Phosphoserine Ref.27
Modified residue12811Phosphoserine Ref.22 Ref.27
Modified residue13211Phosphothreonine Ref.26

Experimental info

Sequence conflict2351P → T in AAA34841. Ref.1
Sequence conflict266 – 2738ITAQDQAK → YYCPRSGKN in AAA34841. Ref.1
Sequence conflict474 – 48714Missing AA sequence Ref.1
Sequence conflict653 – 6575Missing in AAA34841. Ref.1
Sequence conflict12911A → R in AAA34841. Ref.1
Sequence conflict1396 – 148085GGVLP…PPPLP → EAFCLHPHLYQLNKLPLQNL LSLTLITTMVLKKARAHMDP ILMMTFYRFLNQLVQMKRKK GHNQFLLQVSHQFHLQVFLH PHPFHEDLICFL in AAA34841. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P32521 [UniParc].

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

FASTA1,480160,267
        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' 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. expand/collapse author list , Pearson D., Rajandream M.A., Rice P., Rowley N., Skelton J., Smith V., Walsh S.V., Whitehead S., Barrell B.G.
Nature 387:84-87(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[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]"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].
+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.
PIRS48440.
RefSeqNP_012271.3. NM_001179528.3.

3D structure databases

ProteinModelPortalP32521.
SMRP32521. Positions 273-345, 604-686.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid34997. 60 interactions.
DIPDIP-1340N.
IntActP32521. 22 interactions.
MINTMINT-398969.
STRING4932.YIR006C.

Proteomic databases

PaxDbP32521.
PeptideAtlasP32521.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYIR006C; YIR006C; YIR006C.
GeneID854822.
KEGGsce:YIR006C.

Organism-specific databases

CYGDYIR006c.
SGDS000001445. PAN1.

Phylogenomic databases

eggNOGNOG253201.
GeneTreeENSGT00730000114400.
OMAWGLVNAP.
OrthoDBEOG7P2Z1C.

Enzyme and pathway databases

BioCycYEAST:G3O-31427-MONOMER.

Gene expression databases

GenevestigatorP32521.

Family and domain databases

Gene3D1.10.238.10. 2 hits.
InterProIPR013182. DUF1720.
IPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
IPR000261. EPS15_homology.
IPR026812. Pan1_fungal.
[Graphical view]
PANTHERPTHR11216:SF35. PTHR11216:SF35. 1 hit.
PfamPF08226. DUF1720. 2 hits.
[Graphical view]
SMARTSM00054. EFh. 3 hits.
SM00027. EH. 2 hits.
[Graphical view]
PROSITEPS50222. EF_HAND_2. 3 hits.
PS50031. EH. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio977672.
PROP32521.

Entry information

Entry namePAN1_YEAST
AccessionPrimary (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: April 16, 2014
This is version 134 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome IX

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

Yeast

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

SIMILARITY comments

Index of protein domains and families