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Actin cytoskeleton-regulatory complex protein PAN1 (Mitochondrial distribution of proteins protein 3)

 PAN1_YEAST              Reviewed;        1480 AA.
P32521; D6VVT6;
01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
01-FEB-1995, sequence version 2.
26-FEB-2020, entry version 185.
RecName: Full=Actin cytoskeleton-regulatory complex protein PAN1;
AltName: Full=Mitochondrial distribution of proteins protein 3;
Name=PAN1; Synonyms=DIM2, MDP3, MIP3; OrderedLocusNames=YIR006C;
ORFNames=YIB6C;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 320-344; 352-375
AND 899-906.
PubMed=1339314; DOI=10.1016/0092-8674(92)90246-9;
Sachs A.B., Deardorff J.A.;
"Translation initiation requires the PAB-dependent poly(A) ribonuclease in
yeast.";
Cell 70:961-973(1992).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=7762303; DOI=10.1002/yea.320110109;
Voss H., Tamames J., Teodoru C., Valencia A., Sensen C., Wiemann S.,
Schwager C., Zimmermann J., Sander C., Ansorge W.;
"Nucleotide sequence and analysis of the centromeric region of yeast
chromosome IX.";
Yeast 11:61-78(1995).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169870;
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.,
Pearson D., Rajandream M.A., Rice P., Rowley N., Skelton J., Smith V.,
Walsh S.V., Whitehead S., Barrell B.G.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome IX.";
Nature 387:84-87(1997).
[4]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
G3 (Bethesda) 4:389-398(2014).
[5]
FUNCTION.
PubMed=8524255; DOI=10.1128/mcb.15.12.6884;
Zoladek T., Vaduva G., Hunter L.A., Boguta M., Go B.D., Martin N.C.,
Hopper A.K.;
"Mutations altering the mitochondrial-cytoplasmic distribution of Mod5p
implicate the actin cytoskeleton and mRNA 3' ends and/or protein synthesis
in mitochondrial delivery.";
Mol. Cell. Biol. 15:6884-6894(1995).
[6]
FUNCTION, AND DOMAIN.
PubMed=8978817; DOI=10.1083/jcb.135.6.1485;
Wendland B., McCaffery J.M., Xiao Q., Emr S.D.;
"A novel fluorescence-activated cell sorter-based screen for yeast
endocytosis mutants identifies a yeast homologue of mammalian eps15.";
J. Cell Biol. 135:1485-1500(1996).
[7]
FUNCTION, SUBCELLULAR LOCATION, AND DOMAIN.
PubMed=8756649; DOI=10.1128/mcb.16.9.4897;
Tang H.-Y., Cai M.;
"The EH-domain-containing protein Pan1 is required for normal organization
of the actin cytoskeleton in Saccharomyces cerevisiae.";
Mol. Cell. Biol. 16:4897-4914(1996).
[8]
IDENTIFICATION IN THE PAN1 COMPLEX, FUNCTION OF THE PAN1 COMPLEX, AND
SUBCELLULAR LOCATION.
PubMed=9234686; DOI=10.1128/mcb.17.8.4294;
Tang H.-Y., Munn A., Cai M.;
"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.";
Mol. Cell. Biol. 17:4294-4304(1997).
[9]
EH DOMAINS.
PubMed=9822599; DOI=10.1093/emboj/17.22.6541;
Paoluzi S., Castagnoli L., Lauro I., Salcini A.E., Coda L., Fre' S.,
Confalonieri S., Pelicci P.G., Di Fiore P.P., Cesareni G.;
"Recognition specificity of individual EH domains of mammals and yeast.";
EMBO J. 17:6541-6550(1998).
[10]
FUNCTION, AND INTERACTION WITH YAP1801 AND YAP1802.
PubMed=9531549; DOI=10.1083/jcb.141.1.71;
Wendland B., Emr S.D.;
"Pan1p, yeast eps15, functions as a multivalent adaptor that coordinates
protein-protein interactions essential for endocytosis.";
J. Cell Biol. 141:71-84(1998).
[11]
PHOSPHORYLATION BY PRK1, AND INTERACTION WITH END3.
PubMed=9885245; DOI=10.1083/jcb.144.1.71;
Zeng G., Cai M.;
"Regulation of the actin cytoskeleton organization in yeast by a novel
serine/threonine kinase Prk1p.";
J. Cell Biol. 144:71-82(1999).
[12]
FUNCTION.
PubMed=10954428;
Gagny B., Wiederkehr A., Dumoulin P., Winsor B., Riezman H.,
Haguenauer-Tsapis R.;
"A novel EH domain protein of Saccharomyces cerevisiae, Ede1p, involved in
endocytosis.";
J. Cell Sci. 113:3309-3319(2000).
[13]
FUNCTION, AND IDENTIFICATION IN THE PAN1 COMPLEX.
PubMed=10594004; DOI=10.1128/mcb.20.1.12-25.2000;
Tang H.-Y., Xu J., Cai M.;
"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.";
Mol. Cell. Biol. 20:12-25(2000).
[14]
IDENTIFICATION IN THE PAN1 COMPLEX, FUNCTION OF THE PAN1 COMPLEX,
SUBCELLULAR LOCATION, AND PHOSPHORYLATION BY PRK1.
PubMed=11739778; DOI=10.1091/mbc.12.12.3759;
Zeng G., Yu X., Cai M.;
"Regulation of yeast actin cytoskeleton-regulatory complex
Pan1p/Sla1p/End3p by serine/threonine kinase Prk1p.";
Mol. Biol. Cell 12:3759-3772(2001).
[15]
FUNCTION.
PubMed=11957109; DOI=10.1007/s10142-001-0043-1;
Bidlingmaier S., Snyder M.A.;
"Large-scale identification of genes important for apical growth in
Saccharomyces cerevisiae by directed allele replacement technology (DART)
screening.";
Funct. Integr. Genomics 1:345-356(2002).
[16]
SUBCELLULAR LOCATION.
PubMed=14622601; DOI=10.1016/s0092-8674(03)00883-3;
Kaksonen M., Sun Y., Drubin D.G.;
"A pathway for association of receptors, adaptors, and actin during
endocytic internalization.";
Cell 115:475-487(2003).
[17]
INTERACTION WITH ENT1.
PubMed=12529323; DOI=10.1074/jbc.m211622200;
Aguilar R.C., Watson H.A., Wendland B.;
"The yeast Epsin Ent1 is recruited to membranes through multiple
independent interactions.";
J. Biol. Chem. 278:10737-10743(2003).
[18]
FUNCTION, SUBCELLULAR LOCATION, DOMAINS, AND SUBUNIT.
PubMed=15522098; DOI=10.1111/j.1600-0854.2004.00238.x;
Miliaras N.B., Park J.-H., Wendland B.;
"The function of the endocytic scaffold protein Pan1p depends on multiple
domains.";
Traffic 5:963-978(2004).
[19]
FUNCTION.
PubMed=16171804; DOI=10.1016/j.yexcr.2005.08.018;
Kaminska J., Wysocka-Kapcinska M., Smaczynska-de Rooij I., Rytka J.,
Zoladek T.;
"Pan1p, an actin cytoskeleton-associated protein, is required for growth of
yeast on oleate medium.";
Exp. Cell Res. 310:482-492(2005).
[20]
FUNCTION.
PubMed=16183906; DOI=10.1534/genetics.105.040634;
D'Agostino J.L., Goode B.L.;
"Dissection of Arp2/3 complex actin nucleation mechanism and distinct roles
for its nucleation-promoting factors in Saccharomyces cerevisiae.";
Genetics 171:35-47(2005).
[21]
INTERACTION WITH SPA2, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=16030260; DOI=10.1091/mbc.e05-02-0108;
Shih J.L., Reck-Peterson S.L., Newitt R., Mooseker M.S., Aebersold R.,
Herskowitz I.;
"Cell polarity protein Spa2P associates with proteins involved in actin
function in Saccharomyces cerevisiae.";
Mol. Biol. Cell 16:4595-4608(2005).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-995; SER-1003 AND SER-1281,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=ADR376;
PubMed=17330950; DOI=10.1021/pr060559j;
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
Elias J.E., Gygi S.P.;
"Large-scale phosphorylation analysis of alpha-factor-arrested
Saccharomyces cerevisiae.";
J. Proteome Res. 6:1190-1197(2007).
[23]
IDENTIFICATION IN THE PAN1 COMPLEX, INTERACTION WITH SLA2, AND FUNCTION.
PubMed=17151356; DOI=10.1091/mbc.e06-09-0788;
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.;
"Negative regulation of yeast Eps15-like Arp2/3 complex activator, Pan1p,
by the Hip1R-related protein, Sla2p, during endocytosis.";
Mol. Biol. Cell 18:658-668(2007).
[24]
INTERACTION WITH SCD5.
PubMed=17898076; DOI=10.1091/mbc.e07-06-0607;
Zeng G., Huang B., Neo S.P., Wang J., Cai M.;
"Scd5p mediates phosphoregulation of actin and endocytosis by the type 1
phosphatase Glc7p in yeast.";
Mol. Biol. Cell 18:4885-4898(2007).
[25]
PHOSPHORYLATION BY ARK1.
PubMed=17978096; DOI=10.1091/mbc.e07-06-0530;
Jin M., Cai M.;
"A novel function of Arp2p in mediating Prk1p-specific regulation of actin
and endocytosis in yeast.";
Mol. Biol. Cell 19:297-307(2008).
[26]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-241; THR-570; SER-747;
SER-757; THR-995; SER-1250 AND THR-1321, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth phosphoproteome
analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
[27]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-570; SER-757; THR-993;
THR-995; SER-1003; SER-1180; SER-1250; SER-1253 AND SER-1281, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19779198; DOI=10.1126/science.1172867;
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
"Global analysis of Cdk1 substrate phosphorylation sites provides insights
into evolution.";
Science 325:1682-1686(2009).
-!- 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. {ECO:0000269|PubMed:10594004,
ECO:0000269|PubMed:10954428, ECO:0000269|PubMed:11739778,
ECO:0000269|PubMed:11957109, ECO:0000269|PubMed:15522098,
ECO:0000269|PubMed:16171804, ECO:0000269|PubMed:16183906,
ECO:0000269|PubMed:17151356, ECO:0000269|PubMed:8524255,
ECO:0000269|PubMed:8756649, ECO:0000269|PubMed:8978817,
ECO:0000269|PubMed:9234686, ECO:0000269|PubMed:9531549}.
-!- SUBUNIT: 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.
{ECO:0000269|PubMed:10594004, ECO:0000269|PubMed:11739778,
ECO:0000269|PubMed:12529323, ECO:0000269|PubMed:15522098,
ECO:0000269|PubMed:16030260, ECO:0000269|PubMed:17151356,
ECO:0000269|PubMed:17898076, ECO:0000269|PubMed:9234686,
ECO:0000269|PubMed:9531549, ECO:0000269|PubMed:9885245}.
-!- INTERACTION:
P39013:END3; NbExp=9; IntAct=EBI-12875, EBI-6460;
Q04439:MYO5; NbExp=2; IntAct=EBI-12875, EBI-11687;
P32790:SLA1; NbExp=5; IntAct=EBI-12875, EBI-17313;
P38856:YAP1801; NbExp=4; IntAct=EBI-12875, EBI-24811;
-!- 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.
-!- PTM: The N-terminus is blocked.
-!- SIMILARITY: Belongs to the PAN1 family. {ECO:0000305}.
-!- CAUTION: Was originally thought to be a subunit of PAB-dependent
poly(A)-specific ribonuclease. {ECO:0000305|PubMed:1339314}.
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EMBL; Z38062; CAA86208.1; -; Genomic_DNA.
EMBL; X79743; CAB38097.1; -; Genomic_DNA.
EMBL; M90688; AAA34841.1; -; Genomic_DNA.
EMBL; BK006942; DAA08552.1; -; Genomic_DNA.
PIR; S48440; S48440.
RefSeq; NP_012271.3; NM_001179528.3.
SMR; P32521; -.
BioGrid; 34997; 648.
ComplexPortal; CPX-426; PAN1 actin cytoskeleton-regulatory complex.
DIP; DIP-1340N; -.
IntAct; P32521; 22.
MINT; P32521; -.
STRING; 4932.YIR006C; -.
iPTMnet; P32521; -.
MaxQB; P32521; -.
PaxDb; P32521; -.
PRIDE; P32521; -.
TopDownProteomics; P32521; -.
EnsemblFungi; YIR006C_mRNA; YIR006C; YIR006C.
GeneID; 854822; -.
KEGG; sce:YIR006C; -.
EuPathDB; FungiDB:YIR006C; -.
SGD; S000001445; PAN1.
HOGENOM; CLU_006042_0_0_1; -.
InParanoid; P32521; -.
KO; K20047; -.
OMA; PQRTGMQ; -.
BioCyc; YEAST:G3O-31427-MONOMER; -.
Reactome; R-SCE-194840; Rho GTPase cycle.
Reactome; R-SCE-416482; G alpha (12/13) signalling events.
Reactome; R-SCE-8856825; Cargo recognition for clathrin-mediated endocytosis.
Reactome; R-SCE-8856828; Clathrin-mediated endocytosis.
PRO; PR:P32521; -.
Proteomes; UP000002311; Chromosome IX.
RNAct; P32521; protein.
GO; GO:0030479; C:actin cortical patch; IDA:SGD.
GO; GO:1990964; C:actin cytoskeleton-regulatory complex; IDA:SGD.
GO; GO:0005935; C:cellular bud neck; HDA:SGD.
GO; GO:0005737; C:cytoplasm; IDA:SGD.
GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
GO; GO:0043332; C:mating projection tip; HDA:SGD.
GO; GO:0005634; C:nucleus; IDA:SGD.
GO; GO:0005886; C:plasma membrane; HDA:SGD.
GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
GO; GO:0071933; F:Arp2/3 complex binding; IDA:SGD.
GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
GO; GO:0000147; P:actin cortical patch assembly; IMP:SGD.
GO; GO:0007120; P:axial cellular bud site selection; IMP:SGD.
GO; GO:0007121; P:bipolar cellular bud site selection; IMP:SGD.
GO; GO:0006897; P:endocytosis; IMP:SGD.
GO; GO:2000601; P:positive regulation of Arp2/3 complex-mediated actin nucleation; IDA:SGD.
CDD; cd00052; EH; 2.
DisProt; DP02220; -.
InterPro; IPR013182; DUF1720.
InterPro; IPR011992; EF-hand-dom_pair.
InterPro; IPR018247; EF_Hand_1_Ca_BS.
InterPro; IPR002048; EF_hand_dom.
InterPro; IPR000261; EH_dom.
Pfam; PF08226; DUF1720; 3.
Pfam; PF12763; EF-hand_4; 2.
SMART; SM00054; EFh; 3.
SMART; SM00027; EH; 2.
SUPFAM; SSF47473; SSF47473; 2.
PROSITE; PS50222; EF_HAND_2; 3.
PROSITE; PS50031; EH; 2.
1: Evidence at protein level;
Actin-binding; Cell membrane; Coiled coil; Cytoplasm; Cytoskeleton;
Direct protein sequencing; Endocytosis; Endosome; Membrane; Phosphoprotein;
Reference proteome; Repeat.
CHAIN 1..1480
/note="Actin cytoskeleton-regulatory complex protein PAN1"
/id="PRO_0000058221"
REPEAT 142..153
/note="1-1"
REPEAT 164..175
/note="1-2"
REPEAT 188..199
/note="1-3"
REPEAT 215..226
/note="1-4"
REPEAT 235..246
/note="1-5"
DOMAIN 270..359
/note="EH 1"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00077"
REPEAT 328..350
/note="2-1"
REPEAT 392..403
/note="1-6"
REPEAT 409..420
/note="1-7"
REPEAT 422..433
/note="1-8"
REPEAT 446..457
/note="1-9"
REPEAT 467..478
/note="1-10"
REPEAT 498..509
/note="1-11"
REPEAT 510..518
/note="1-12"
REPEAT 538..548
/note="1-13"
REPEAT 549..556
/note="1-14"
REPEAT 564..575
/note="1-15"
DOMAIN 600..689
/note="EH 2"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00077"
REPEAT 658..680
/note="2-2"
REPEAT 1084..1089
/note="3-1"
REPEAT 1090..1095
/note="3-2"
REPEAT 1096..1101
/note="3-3"
REPEAT 1102..1107
/note="3-4"
REPEAT 1108..1113
/note="3-5"
REPEAT 1114..1119
/note="3-6"
REPEAT 1120..1125
/note="3-7"
REPEAT 1315..1320
/note="4-1"
REPEAT 1321..1326
/note="4-2"
REPEAT 1327..1332
/note="4-3"
REPEAT 1340..1345
/note="4-4"
REPEAT 1346..1350
/note="4-5"
REPEAT 1355..1360
/note="4-6"
REPEAT 1361..1366
/note="4-7"
REPEAT 1372..1377
/note="4-8"
REGION 142..575
/note="15 X 12 AA tandem repeats of [SPNAG]-[IL]-[QKNGT]-
[PSA]-[QT]-[GQAPISTLYK]-T-G-[YFGML]-[YVMGAQL]-[QVLNPAG]-
[ASQPN]"
REGION 328..680
/note="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
/note="7 X 6 AA tandem repeats of Q-[PS]-T-Q-P-V"
REGION 1315..1377
/note="8 X 6 AA repeats of [ATVSP]-P-[LVI]-P-[SPQILA]-
[VAS]"
COILED 1131..1190
/evidence="ECO:0000255"
COMPBIAS 13..22
/note="Poly-Gln"
COMPBIAS 29..34
/note="Poly-Gln"
COMPBIAS 98..106
/note="Poly-Gln"
COMPBIAS 1400..1406
/note="Poly-Pro"
COMPBIAS 1452..1455
/note="Poly-Glu"
COMPBIAS 1474..1480
/note="Poly-Pro"
MOD_RES 241
/note="Phosphothreonine"
/evidence="ECO:0000244|PubMed:18407956"
MOD_RES 570
/note="Phosphothreonine"
/evidence="ECO:0000244|PubMed:18407956,
ECO:0000244|PubMed:19779198"
MOD_RES 747
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:18407956"
MOD_RES 757
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:18407956,
ECO:0000244|PubMed:19779198"
MOD_RES 993
/note="Phosphothreonine"
/evidence="ECO:0000244|PubMed:19779198"
MOD_RES 995
/note="Phosphothreonine"
/evidence="ECO:0000244|PubMed:17330950,
ECO:0000244|PubMed:18407956, ECO:0000244|PubMed:19779198"
MOD_RES 1003
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:17330950,
ECO:0000244|PubMed:19779198"
MOD_RES 1180
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:19779198"
MOD_RES 1250
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:18407956,
ECO:0000244|PubMed:19779198"
MOD_RES 1253
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:19779198"
MOD_RES 1281
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:17330950,
ECO:0000244|PubMed:19779198"
MOD_RES 1321
/note="Phosphothreonine"
/evidence="ECO:0000244|PubMed:18407956"
CONFLICT 235
/note="P -> T (in Ref. 1; AAA34841)"
/evidence="ECO:0000305"
CONFLICT 266..273
/note="ITAQDQAK -> YYCPRSGKN (in Ref. 1; AAA34841)"
/evidence="ECO:0000305"
CONFLICT 474..487
/note="Missing (in Ref. 1; AA sequence)"
/evidence="ECO:0000305"
CONFLICT 653..657
/note="Missing (in Ref. 1; AAA34841)"
/evidence="ECO:0000305"
CONFLICT 1291
/note="A -> R (in Ref. 1; AAA34841)"
/evidence="ECO:0000305"
CONFLICT 1396..1480
/note="GGVLPPPPPLPTQQASTSEPIIAHVDNYNGAEKGTGAYGSDSDDDVLSIPES
VGTDEEEEGAQPVSTAGIPSIPPAGIPPPPPLP -> EAFCLHPHLYQLNKLPLQNLLS
LTLITTMVLKKARAHMDPILMMTFYRFLNQLVQMKRKKGHNQFLLQVSHQFHLQVFLHP
HPFHEDLICFL (in Ref. 1; AAA34841)"
/evidence="ECO:0000305"
SEQUENCE 1480 AA; 160267 MW; F3518495FF759553 CRC64;
MYNPYQQQGM GYQQQQQQQQ QQPNGFYPQQ QQGQSSNQPQ GQPQPQQQMA FNQPQATGIG
GMPQSFGNSF SSMPQQPQTG YNNNGNNGSV YGNGNFGQQP QQQQQQAKPQ HTGYVPNSSM
PMMNTTGTMP PPNPAQQPQL QSIQPQGTGY YQAANTANVH SVQPLQSQGT GYYVSTPNLI
SSNQTQQPLQ AQGTGYYQSQ PQQVPPPQQA QSLQPLKPQQ TGFYLQPQNQ APLEPLKPTA
TGFVNSFANN GLNNDIKIPA IRLSFITAQD QAKFETLFRS IVTNGSNTVS GANCRKILMR
SGLPPSQLAR IWTLCDTSKA GELLFPEFAL AMHLINDVLQ GDTIPYELDS KTKNEVSSFI
DAINLSIANQ DSSANDAPKT PFDEFITAGV QNLQPQPTGY MPQTSFGIPL QSQITGGGVA
SALNPQSTGF MAPTTFNMSM NTGTPGLNPQ ITGGAPASMQ PNITGNALQP QTTGMMPQTT
GMMPQTTGMM PQTSFGVNLG PQLTGGALQS QYTGGYGSVM PQQSGPASMP NLSFNQQGLQ
SQLTGLQPQP TGFLPPSNFS ATMPLTAQKT GFGNNEIYTK SNFNNNLIDN SSQDKISTEE
KSLFYKIFET FDTQNKGLLD SPTAVEIFRK SGLNRADLEQ IWNLCDINNT GQLNKQEFAL
GMHLVYGKLN GKPIPNVLPS SLIPSSTKLL DNLKNQLKTE PTTTKEKPSF GKIDALSYKN
NDDDVLPNYR NRRKVYSAKN EEQSSFSSPS AKSVNHSSST LQTDDISVDK TVEKKTAKPK
YAGFSREINL KNIASLENEI KNISNPENCY DSSIPSDLTS RFDAIIAKLP NLFNEISTID
NEITNAKIQL YRKKNPSSII GSGPNGEITE NDRKKAKSRA LLRARMSALT GKSTESEDSL
SMEDEQQSAE IKRIQQENGK NQEIIKDIRS SISDISASLK STMTGSNMIS NQEFERWEFG
IGLEDGVREF LDDLKSNSNK SVTESSPFVP SSTPTPVDDR SSSPSYSQFK TAEERAAYLK
EQAKKRMKEK LAKFDKNRRN VTQSSRSISS ENSREQPQQI AGSSNLVEPR ATPFQEEKYV
EVAQPTQPVQ STQPVQPTQP VQPTQPVQPT QPVQPTQPVQ PTQPVQNVYN AKQESDDEDE
DDEEKRLQEE LKRLKLKKKA DKEKRLAALR KQIEDAQNES DEEETNGKDN FGGHVNVPQA
APVAPSAAFS QNSTNAPRSV HAAVTPAAGK NSTGLPSTTM GHNPYFKDAS ASSTSTFDAR
AAEMQRRIQR GLDEDEDDGW SDEDESNNRV AVDNKVEEAK IGHPDHARAP PVTAAPLPSV
TPVPPAVPVP QANTSNEKSS PIPIAPIPPS VTQEPPVPLA PPLPAVDGFQ EPPIPSAPAI
ATAVQKSGSS TPALAGGVLP PPPPLPTQQA STSEPIIAHV DNYNGAEKGT GAYGSDSDDD
VLSIPESVGT DEEEEGAQPV STAGIPSIPP AGIPPPPPLP


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Catalog number Product name Quantity
28-124 EPLIN is a cytoskeleton-associated protein that inhibits actin filament depolymerization and cross-links filaments in bundles. EPLIN is a cytoskeleton-associated protein that inhibits actin filament d 0.05 mg
25-452 AVIL is a member of the gelsolin_villin family of actin regulatory proteins. This protein has structural similarity to villin. It binds actin and may play a role in the development of neuronal cells t 0.05 mg
25-094 AVIL is a member of the gelsolin_villin family of actin regulatory proteins. This protein has structural similarity to villin. It binds actin and may play a role in the development of neuronal cells t 0.05 mg
EIAAB26211 Liver regeneration-related protein LRRGT00164,Mdm20,Mitochondrial distribution and morphology protein 20,Naa25,N-alpha-acetyltransferase 25, NatB auxiliary subunit,NatB complex subunit MDM20,N-termina
30-394 DSTN belongs to the actin-binding proteins ADF family. This family of proteins is responsible for enhancing the turnover rate of actin in vivo. It is the actin depolymerizing protein that severs actin 0.05 mg
EIAAB05289 Actin regulatory protein CAP-G,Actin-capping protein GCAP39,Capg,Macrophage-capping protein,Mbh1,Mouse,Mus musculus,Myc basic motif homolog 1
EIAAB33305 Complex III subunit 6,Complex III subunit VIII,Cytochrome b-c1 complex subunit 6, mitochondrial,Cytochrome c1 non-heme 11 kDa protein,Homo sapiens,Human,Mitochondrial hinge protein,Ubiquinol-cytochrom
EIAAB33308 Complex III subunit 6,Complex III subunit VIII,Cytochrome b-c1 complex subunit 6, mitochondrial,Cytochrome c1 non-heme 11 kDa protein,Mitochondrial hinge protein,Mouse,Mus musculus,Ubiquinol-cytochrom
EIAAB33306 Complex III subunit 6,Complex III subunit VIII,Cytochrome b-c1 complex subunit 6, mitochondrial,Cytochrome c1 non-heme 11 kDa protein,Mitochondrial hinge protein,Rat,Rattus norvegicus,Ubiquinol-cytoch
EIAAB26209 C12orf30,Homo sapiens,Human,MDM20,Mitochondrial distribution and morphology protein 20,NAA25,N-alpha-acetyltransferase 25, NatB auxiliary subunit,NAP1,NatB complex subunit MDM20,N-terminal acetyltrans
27-647 HS1 which is hematopoietic lineage cell-specific protein 1, is a substrate of protein tyrosine kinases in lymphocytes, it binds to F-actin, and promotes Arp2_3 complex-mediated actin polymerization. H 0.1 mg
30-801 WASF3 is a member of the Wiskott-Aldrich syndrome protein family. It is a protein that forms a multiprotein complex that links receptor kinases and actin. Binding to actin occurs through a C-terminal 0.05 mg
30-802 WASF3 is a member of the Wiskott-Aldrich syndrome protein family. It is a protein that forms a multiprotein complex that links receptor kinases and actin. Binding to actin occurs through a C-terminal 0.05 mg
EIAAB33307 Bos taurus,Bovine,Complex III subunit 6,Complex III subunit VIII,Cytochrome b-c1 complex subunit 6, mitochondrial,Cytochrome c1 non-heme 11 kDa protein,Mitochondrial hinge protein,Ubiquinol-cytochrome
EIAAB26210 Mdm20,Mitochondrial distribution and morphology protein 20,Mouse,Mus musculus,Naa25,N-alpha-acetyltransferase 25, NatB auxiliary subunit,NatB complex subunit MDM20,N-terminal acetyltransferase B compl
27-993 Regulator of G protein signaling (RGS) proteins are regulatory and structural components of G protein-coupled receptor complexes. RGS proteins are GTPase-activating proteins for Gi and Gq class G-alph 0.1 mg
29-775 Ankyrins are a family of proteins that are believed to link the integral membrane proteins to the underlying spectrin-actin cytoskeleton and play key roles in activities such as cell motility, activat 0.1 mg
27-992 Regulator of G protein signaling (RGS) proteins are regulatory and structural components of G protein-coupled receptor complexes. RGS proteins are GTPase-activating proteins for Gi class G-alpha prote 0.1 mg
pro-145 Recombinant Human Actin Related Protein 2_3 Complex Subunit 5 RECOMBINANT & NATURAL PROTEINS 5
pro-145 Recombinant Human Actin Related Protein 2_3 Complex Subunit 5 RECOMBINANT & NATURAL PROTEINS 1mg
pro-145 Recombinant Human Actin Related Protein 2_3 Complex Subunit 5 RECOMBINANT & NATURAL PROTEINS 20
27-191 ARPC2 is one of seven subunits of the human Arp2_3 protein complex. The Arp2_3 protein complex has been implicated in the control of actin polymerization in cells and has been conserved through evolut 0.05 mg
30-793 ARPC3 is one of seven subunits of the human Arp2_3 protein complex. The Arp2_3 protein complex has been implicated in the control of actin polymerization in cells and has been conserved through evolut 0.05 mg
30-191 Proteins that contain formin homology (FH) domains, such as FHOD3, play a role in regulation of the actin cytoskeleton. 0.05 mg
26-936 CDC42EP4 is a member of the CDC42-binding protein family. Members of this family interact with Rho family GTPases and regulate the organization of the actin cytoskeleton. The protein has been shown to 0.05 mg
Pathways :
WP2272: Pathogenic Escherichia coli infection
WP2292: Chemokine signaling pathway
WP525: Mitochondrial Unfolded-Protein Response
WP1909: Signal regulatory protein (SIRP) family interactions
WP1493: Carbon assimilation C4 pathway
WP210: Cytoplasmic Ribosomal Proteins
WP731: Sterol regulatory element binding protein related
WP1502: Mitochondrial biogenesis
WP1673: Naphthalene and anthracene degradation
WP1678: Nucleotide excision repair
WP211: BMP signaling pathway
WP51: Regulation of Actin Cytoskeleton
WP1062: Regulation of Actin Cytoskeleton
WP1616: ABC transporters
WP1888: Post-translational protein modification
WP1690: Propanoate metabolism
WP2218: sGC
WP1371: G Protein Signaling Pathways
WP1694: Pyrimidine metabolism
WP232: G Protein Signaling Pathways
WP1165: G Protein Signaling Pathways
WP1654: gamma-Hexachlorocyclohexane degradation
WP351: Regulation of Actin Cytoskeleton
WP1661: Glyoxylate and dicarboxylate metabolism
WP944: Regulation of Actin Cytoskeleton

Related Genes :
[PAN1 DIM2 MDP3 MIP3 YIR006C YIB6C] Actin cytoskeleton-regulatory complex protein PAN1 (Mitochondrial distribution of proteins protein 3)
[pan1 panA HVO_0850] Proteasome-activating nucleotidase 1 (PAN 1) (Proteasomal ATPase 1) (Proteasome regulatory ATPase 1) (Proteasome regulatory particle 1)
[HSD17B11 DHRS8 PAN1B SDR16C2 PSEC0029 UNQ207/PRO233] Estradiol 17-beta-dehydrogenase 11 (EC 1.1.1.62) (17-beta-hydroxysteroid dehydrogenase 11) (17-beta-HSD 11) (17bHSD11) (17betaHSD11) (17-beta-hydroxysteroid dehydrogenase XI) (17-beta-HSD XI) (17betaHSDXI) (Cutaneous T-cell lymphoma-associated antigen HD-CL-03) (CTCL-associated antigen HD-CL-03) (Dehydrogenase/reductase SDR family member 8) (Retinal short-chain dehydrogenase/reductase 2) (retSDR2) (Short chain dehydrogenase/reductase family 16C member 2)
[mamK amb0965] Actin-like protein MamK (EC 3.6.1.3) (Magnetosome cytoskeleton protein MamK)
[mamK MGMSRv2__2377 mgI489 MGR_4093] Actin-like protein MamK (EC 3.6.1.3) (Magnetosome cytoskeleton protein MamK)
[pan-1 NCU06171] Actin cytoskeleton-regulatory complex protein pan-1
[MDM10 YAL010C FUN37] Mitochondrial distribution and morphology protein 10 (Mitochondrial inheritance component MDM10)
[pep NCU02549] Mitochondrial-processing peptidase subunit beta (EC 3.4.24.64) (Beta-MPP) (Complex III subunit I) (Core protein I) (Cytochrome b-c1 complex subunit 1, mitochondrial) (Processing enhancing protein) (Ubiquinol-cytochrome c oxidoreductase core protein 1) (Ubiquinol-cytochrome c reductase complex 50 kDa protein)
[arcB Arc35 arpE DDB_G0282813] Actin-related protein 2/3 complex subunit 2 (Arp2/3 complex 34 kDa subunit) (p34-ARC)
[arcC Arc18 arpF DDB_G0292804] Actin-related protein 2/3 complex subunit 3 (Arp2/3 complex 21 kDa subunit) (p21-ARC)
[MDM12 YOL009C] Mitochondrial distribution and morphology protein 12 (Mitochondrial inheritance component MDM12)
[Ppp1r9b Spino] Neurabin-2 (Neurabin-II) (Neural tissue-specific F-actin-binding protein II) (PP1bp134) (Protein phosphatase 1 regulatory subunit 9B) (Spinophilin) (p130)
[asp1 vip1 SPCC1672.06c] Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase (EC 2.7.4.21) (EC 2.7.4.24) (Cortical actin cytoskeleton protein asp1) (InsP6 and PP-IP5 kinase)
[fes-1 NCU06606] Cytochrome b-c1 complex subunit Rieske, mitochondrial (EC 7.1.1.8) (Complex III subunit 5) (Complex III subunit V) (Rieske iron-sulfur protein) (RISP) (Ubiquinol-cytochrome c oxidoreductase iron-sulfur subunit) (Ubiquinol-cytochrome c reductase complex 25 kDa protein)
[arcA Arc40 arpD DDB_G0277825] Actin-related protein 2/3 complex subunit 1 (Arp2/3 complex 41 kDa subunit) (p41-Arc)
[arcD Arc19 arpG DDB_G0269102] Actin-related protein 2/3 complex subunit 4 (Arp2/3 complex 20 kDa subunit) (p20-ARC)
[arcE Arc15 arpH DDB_G0288319] Actin-related protein 2/3 complex subunit 5 (Arp2/3 complex 16 kDa subunit) (p16-ARC)
[Hsd17b11 Dhrs8 Pan1b] Estradiol 17-beta-dehydrogenase 11 (EC 1.1.1.62) (17-beta-hydroxysteroid dehydrogenase 11) (17-beta-HSD 11) (17bHSD11) (17betaHSD11) (17-beta-hydroxysteroid dehydrogenase XI) (17-beta-HSD XI) (17betaHSDXI) (Dehydrogenase/reductase SDR family member 8)
[Flna Fln Fln1] Filamin-A (FLN-A) (Actin-binding protein 280) (ABP-280) (Alpha-filamin) (Endothelial actin-binding protein) (Filamin-1) (Non-muscle filamin)
[arpC aclA act DDB_G0283755] Actin-related protein 3 (Actin-like protein 3) (Actin-related protein C)
[MDM20 DEC1 YOL076W] N-terminal acetyltransferase B complex subunit MDM20 (NatB complex subunit MDM20) (Dislikes extra CIN8 protein 1) (Mitochondrial distribution and morphology protein 20)
[ARP7 SWP61 YPR034W YP9367.14] Actin-related protein 7 (Actin-like protein ARP7) (Chromatin structure-remodeling complex protein ARP7) (SWI/SNF complex component ARP7)
[FLNB FLN1L FLN3 TABP TAP] Filamin-B (FLN-B) (ABP-278) (ABP-280 homolog) (Actin-binding-like protein) (Beta-filamin) (Filamin homolog 1) (Fh1) (Filamin-3) (Thyroid autoantigen) (Truncated actin-binding protein) (Truncated ABP)
[MDM35 YKL053C-A] Mitochondrial distribution and morphology protein 35
[Dst Bpag1 Macf2] Dystonin (Bullous pemphigoid antigen 1) (BPA) (Dystonia musculorum protein) (Hemidesmosomal plaque protein) (Microtubule actin cross-linking factor 2)
[MACF1 ABP620 ACF7 KIAA0465 KIAA1251] Microtubule-actin cross-linking factor 1, isoforms 1/2/3/5 (620 kDa actin-binding protein) (ABP620) (Actin cross-linking family protein 7) (Macrophin-1) (Trabeculin-alpha)
[ARP9 SWP59 YMR033W YM9973.07] Actin-like protein ARP9 (Chromatin structure-remodeling complex protein ARP9) (SWI/SNF complex component ARP9)
[cyt-1 NCU09816] Cytochrome c1, heme protein, mitochondrial (EC 7.1.1.8) (Complex III subunit 4) (Complex III subunit IV) (Cytochrome b-c1 complex subunit 4) (Ubiquinol-cytochrome c oxidoreductase complex cytochrome c1 subunit) (Cytochrome c-1) (Ubiquinol-cytochrome c reductase complex 31 kDa protein)
[MPPbeta At3g02090 F1C9.12] Probable mitochondrial-processing peptidase subunit beta, mitochondrial (EC 3.4.24.64) (Beta-MPP) (Complex III subunit I) (Core protein I) (Cytochrome b-c1 complex subunit 1, mitochondrial) (Ubiquinol-cytochrome c oxidoreductase core protein 1)
[FLNA FLN FLN1] Filamin-A (FLN-A) (Actin-binding protein 280) (ABP-280) (Alpha-filamin) (Endothelial actin-binding protein) (Filamin-1) (Non-muscle filamin)

Bibliography :