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Protein purity of essence (Interaction calmodulin and colossal molecular mass protein) (Protein Calossin) (Protein pushover)

 POE_DROME               Reviewed;        5322 AA.
Q9VLT5; O96958; Q8MS98; Q9XYD1; Q9XYD2;
11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
18-JUL-2018, entry version 137.
RecName: Full=Protein purity of essence;
AltName: Full=Interaction calmodulin and colossal molecular mass protein;
AltName: Full=Protein Calossin;
AltName: Full=Protein pushover;
Name=poe {ECO:0000312|EMBL:AAF52598.1,
ECO:0000312|FlyBase:FBgn0011230};
Synonyms=calo {ECO:0000312|EMBL:CAA76940.1},
push {ECO:0000312|EMBL:AAD20450.1}; ORFNames=CG14472;
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227;
[1] {ECO:0000305, ECO:0000312|EMBL:AAD20450.1}
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS A AND B), FUNCTION,
TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
PubMed=11517334; DOI=10.1073/pnas.191107698;
Yager J., Richards S., Hekmat-Scafe D.S., Hurd D.D., Sundaresan V.,
Caprette D.R., Saxton W.M., Carlson J.R., Stern M.;
"Control of Drosophila perineurial glial growth by interacting
neurotransmitter-mediated signaling pathways.";
Proc. Natl. Acad. Sci. U.S.A. 98:10445-10450(2001).
[2] {ECO:0000312|EMBL:AAF52598.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley {ECO:0000269|PubMed:10731132};
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[3] {ECO:0000305, ECO:0000312|EMBL:AAF52598.1}
GENOME REANNOTATION.
STRAIN=Berkeley;
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a
systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[4] {ECO:0000305, ECO:0000312|EMBL:CAA76940.1}
NUCLEOTIDE SEQUENCE [MRNA] OF 1207-5322 (ISOFORM A), PUTATIVE
FUNCTION, AND INTERACTION WITH CALMODULIN.
TISSUE=Retina {ECO:0000312|EMBL:CAA76940.1};
PubMed=9813038; DOI=10.1074/jbc.273.47.31297;
Xu X.-Z.S., Wes P.D., Chen H., Li H.-S., Yu M., Morgan S., Liu Y.,
Montell C.;
"Retinal targets for calmodulin include proteins implicated in
synaptic transmission.";
J. Biol. Chem. 273:31297-31307(1998).
[5] {ECO:0000305, ECO:0000312|EMBL:AAM50858.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 5019-5322 (ISOFORM A).
STRAIN=Berkeley {ECO:0000312|EMBL:AAM50858.1};
TISSUE=Embryo {ECO:0000269|PubMed:12537569};
PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M.,
George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H.,
Rubin G.M., Celniker S.E.;
"A Drosophila full-length cDNA resource.";
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
[6] {ECO:0000305}
IDENTIFICATION, AND PUTATIVE FUNCTION.
PubMed=8244010;
Castrillon D.H., Gonczy P., Alexander S., Rawson R., Eberhart C.G.,
Viswanathan S., DiNardo S., Wasserman S.A.;
"Toward a molecular genetic analysis of spermatogenesis in Drosophila
melanogaster: characterization of male-sterile mutants generated by
single P element mutagenesis.";
Genetics 135:489-505(1993).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1894, AND IDENTIFICATION
BY MASS SPECTROMETRY.
PubMed=17372656; DOI=10.1039/b617545g;
Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D.,
Juenger M.A., Eng J.K., Aebersold R., Tao W.A.;
"An integrated chemical, mass spectrometric and computational strategy
for (quantitative) phosphoproteomics: application to Drosophila
melanogaster Kc167 cells.";
Mol. Biosyst. 3:275-286(2007).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-167; THR-599; SER-600;
SER-1167; SER-1168; SER-1171; SER-1894; THR-3013; SER-3014; SER-3051;
SER-3057 AND SER-3510, AND IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Embryo;
PubMed=18327897; DOI=10.1021/pr700696a;
Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
"Phosphoproteome analysis of Drosophila melanogaster embryos.";
J. Proteome Res. 7:1675-1682(2008).
[9]
FUNCTION.
PubMed=27552662; DOI=10.1371/journal.pbio.1002539;
Ashton-Beaucage D., Lemieux C., Udell C.M., Sahmi M., Rochette S.,
Therrien M.;
"The Deubiquitinase USP47 Stabilizes MAPK by Counteracting the
Function of the N-end Rule ligase POE/UBR4 in Drosophila.";
PLoS Biol. 14:E1002539-E1002539(2016).
-!- FUNCTION: Has a role in growth of the perineurial glial layer of
the larval peripheral nerve (PubMed:27552662). May have a role in
male fertility and eye development or function (PubMed:27552662).
Involved in the negative regulation of the Ras/MAPK signaling
pathway in the wing by acting with the E2 enzyme Unc6 and the
putative E3 ligases Kcmf1 and Ufd4 to mediate the ubiquitination
and proteasomal degradation of rl/MAPK (PubMed:27552662).
{ECO:0000269|PubMed:11517334, ECO:0000269|PubMed:27552662}.
-!- SUBUNIT: May bind calmodulin (PubMed:9813038). Interacts with
Kcmf1 (PubMed:27552662). {ECO:0000269|PubMed:27552662,
ECO:0000269|PubMed:9813038}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=A {ECO:0000269|PubMed:11517334};
IsoId=Q9VLT5-1; Sequence=Displayed;
Name=B {ECO:0000269|PubMed:11517334};
IsoId=Q9VLT5-2; Sequence=VSP_052089, VSP_052090;
-!- TISSUE SPECIFICITY: Expressed in embryonic central nervous system
and adult testes. {ECO:0000269|PubMed:11517334}.
-!- DISRUPTION PHENOTYPE: Flies increase the growth of the perineurial
glial layer of the larval peripheral nerve and exhibit male
sterility due to the inhibition of sperm individualisation.
{ECO:0000269|PubMed:11517334}.
-!- SIMILARITY: Belongs to the UBR4 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAM50858.1; Type=Erroneous translation; Note=Wrong choice of frame.; Evidence={ECO:0000305};
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EMBL; AF096896; AAD20449.1; -; Genomic_DNA.
EMBL; AF096897; AAD20450.1; -; mRNA.
EMBL; AE014134; AAF52598.1; -; Genomic_DNA.
EMBL; Y17920; CAA76940.1; -; mRNA.
EMBL; AY118998; AAM50858.1; ALT_SEQ; mRNA.
PIR; T13719; T13719.
RefSeq; NP_001260222.1; NM_001273293.1. [Q9VLT5-1]
RefSeq; NP_476986.1; NM_057638.4. [Q9VLT5-1]
UniGene; Dm.7936; -.
BioGrid; 70146; 19.
IntAct; Q9VLT5; 13.
STRING; 7227.FBpp0079167; -.
iPTMnet; Q9VLT5; -.
PaxDb; Q9VLT5; -.
PRIDE; Q9VLT5; -.
EnsemblMetazoa; FBtr0079545; FBpp0079167; FBgn0011230. [Q9VLT5-1]
EnsemblMetazoa; FBtr0333088; FBpp0305301; FBgn0011230. [Q9VLT5-1]
GeneID; 46243; -.
KEGG; dme:Dmel_CG14472; -.
CTD; 46243; -.
FlyBase; FBgn0011230; poe.
eggNOG; KOG1776; Eukaryota.
eggNOG; ENOG410XPP8; LUCA.
GeneTree; ENSGT00600000084471; -.
InParanoid; Q9VLT5; -.
KO; K10691; -.
OMA; AFEMKEL; -.
OrthoDB; EOG091G000I; -.
PhylomeDB; Q9VLT5; -.
Reactome; R-DME-6798695; Neutrophil degranulation.
Reactome; R-DME-983168; Antigen processing: Ubiquitination & Proteasome degradation.
GenomeRNAi; 46243; -.
PRO; PR:Q9VLT5; -.
Proteomes; UP000000803; Chromosome 2L.
Bgee; FBgn0011230; -.
ExpressionAtlas; Q9VLT5; baseline and differential.
Genevisible; Q9VLT5; DM.
GO; GO:0043186; C:P granule; IPI:FlyBase.
GO; GO:0005516; F:calmodulin binding; IDA:FlyBase.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0042065; P:glial cell growth; IMP:UniProtKB.
GO; GO:0042066; P:perineurial glial growth; IMP:FlyBase.
GO; GO:0050896; P:response to stimulus; IEA:UniProtKB-KW.
GO; GO:0007291; P:sperm individualization; IMP:FlyBase.
GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
InterPro; IPR025704; E3_Ub_ligase_UBR4.
InterPro; IPR036322; WD40_repeat_dom_sf.
InterPro; IPR003126; Znf_UBR.
Pfam; PF13764; E3_UbLigase_R4; 1.
Pfam; PF02207; zf-UBR; 1.
SMART; SM00396; ZnF_UBR1; 1.
SUPFAM; SSF50978; SSF50978; 2.
PROSITE; PS51157; ZF_UBR; 1.
1: Evidence at protein level;
Alternative splicing; Calmodulin-binding; Complete proteome;
Developmental protein; Differentiation; Metal-binding; Neurogenesis;
Phosphoprotein; Reference proteome; Sensory transduction; Vision;
Zinc; Zinc-finger.
CHAIN 1 5322 Protein purity of essence.
/FTId=PRO_0000245794.
ZN_FING 1794 1863 UBR-type. {ECO:0000255|PROSITE-
ProRule:PRU00508}.
MOD_RES 167 167 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 599 599 Phosphothreonine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 600 600 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 1167 1167 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 1168 1168 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 1171 1171 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 1894 1894 Phosphoserine.
{ECO:0000269|PubMed:17372656,
ECO:0000269|PubMed:18327897}.
MOD_RES 3013 3013 Phosphothreonine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 3014 3014 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 3051 3051 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 3057 3057 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 3510 3510 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
VAR_SEQ 4119 4120 LP -> TL (in isoform B).
{ECO:0000303|PubMed:11517334}.
/FTId=VSP_052089.
VAR_SEQ 4121 5322 Missing (in isoform B).
{ECO:0000303|PubMed:11517334}.
/FTId=VSP_052090.
CONFLICT 675 675 S -> T (in Ref. 1; AAD20449/AAD20450).
{ECO:0000305}.
CONFLICT 947 947 I -> T (in Ref. 1; AAD20449).
{ECO:0000305}.
CONFLICT 1405 1405 S -> A (in Ref. 1; AAD20449/AAD20450).
{ECO:0000305}.
CONFLICT 1621 1621 N -> D (in Ref. 1; AAD20449/AAD20450).
{ECO:0000305}.
CONFLICT 2965 2965 L -> P (in Ref. 4; CAA76940).
{ECO:0000305}.
CONFLICT 3105 3105 A -> T (in Ref. 1; AAD20450).
{ECO:0000305}.
CONFLICT 3159 3164 DYVEIG -> GLCGNW (in Ref. 1; AAD20450).
{ECO:0000305}.
CONFLICT 3257 3257 G -> A (in Ref. 4; CAA76940).
{ECO:0000305}.
CONFLICT 4011 4011 D -> H (in Ref. 1; AAD20449).
{ECO:0000305}.
CONFLICT 4812 4812 V -> G (in Ref. 4; CAA76940).
{ECO:0000305}.
SEQUENCE 5322 AA; 590702 MW; 3890824E00F2DB50 CRC64;
MSAHSGGTDW NSVVKALILN RTGALNKNEV VNLLKAITRC EHDFFEEESN FTQFYTAFAA
LAADKLMQIK TICQTQICQL HDATAVLIRF IIYRLPRVSV YETKWLLGAL KMLCEGRECP
ASASSSMFDY NAVANVLKSC KHPESTTKSI MPSSSSSGSG ASNDKESPKS EIKRSRSDLS
SVILQQLIAP LEPGKMTWVP LSEEVTDCTE QILAANVEYF QEQNGVDTLL DVCVSLPILN
RYRSKYMETI NGGKSLYLPL TQVEATAVKS SMNHMLTDLT ILSQAQALIE MQPLTPSRIE
RLSMCGIAAL YNAVLTSIAT SVLGMSQASS SQKQTASTSQ GSGVGGSSGG QSNKDHDDFE
DQACSIVNKA LEIYSNIGHM FKTSARIHVY QNHLCYGSWL LISGIQGAMG ASGSGGSSSD
SASKSASKAT KSGSEAGTAP TTPIARVNLF KVQQGFGELN AAIANHSIKL LSELIEDLKV
EAACGQSLES TELPEPAQFD ILQNYSSLER IVRVLNTATL HQLFTFLATV AYRKACTLKR
ASAKDRTECE PISYSDSTTY FNDSLSCSDN SEEDDSESYL GHWFKETLSP ETHDDNANTS
TQERAEQKSA LVPKLDEPHE YLDLAADIFC FLDQFLANRH AYMQRYVKAG VSDQQMLLMA
NIIKDFDRDV MRNESDQGSG NAPAASAGAG TSAGASTKWQ TSMIRFSGAA GRYIHNLIST
SLLSEQLQSN LLQHLSISPW STDTNTWPLQ VYPSTLSVLV QILLLKPTQE KEAACLSVWH
RLINTLVEGV CSSNTASDSD YEDLNIEHAQ LLLFLFHSLN LMQKKSILLL TAGGVIRCAE
VCRGISEDRP VKNSQIMLLS RLLLFLEYLM KHLYNAPPEL LDQVRWNLFS VSSMPDTQKI
TDLLNCRTKL NSYCRHDIEE NFRKSAGEYG SSIRPTFYSL VMGDPEISYW AQEFKLDGLA
WNFILCTPDK LKYPLLVDAL TDILSITDMS MYSKEKDKEA SMHNLCAIQY CFTIAWKLNL
GLPPSTSHVE SLKAERSPNL HSLMWSIRLP LASSHYLVVS SLIKQGMYTQ YAETLWTHVG
DIGADIKYSL KQTILGVEAF NSQMNGNGTP RLSDLILFDS LVAHMQAVAW ANKEGLKWPR
KESEDAAGEQ SAGTSLTSSS NDPELYSSNE SIDDQKLKQD DDGKLSSDLQ KYNQLVNELM
VKLMNSYQLL SVIVRGQMLK QLSSSTPEKA LNLIVPIVSD KPAIMLELHA AFLKLLPNED
KQLIANEWPK CLMVNDFAFN GKQHPVEPYI LNVIDAHIIE LTRGSNYSTL HTLKHCLKSI
LQLFELLLPH RTANAEVETQ LKQLLISSML DMRTDYLQGH SEHCLREILS GLTQEAQKLL
LYEHMVGYCY RMLKEFAADL RQPQSAGPSG GAPLDQDRAM FNESMLFAVL KTMFKMLEKP
VAVQAMRQFF KDQRSGSLTT LLLSFTGTSL PVSYARKMLQ FVNRLFQLSL QADSQFQHED
LVECFSELAT VDVARLKQWL GHIIYGPNVS TDVSTSEALD TTCRMLTSIL QPSSSSSSNA
QTPTNMATVS AMPSISDQLD PMEIEYDCGT AAGGGESNPG TGGAAANTSQ ILSLWQAAQP
NPSEESSQAC DHSDSERNGA LLLSFVKSLV KDQSKASQIA PPLFQALLQL GQTLISPPQE
GCDFADVLQI MITLADASPA RGHVALFNTT LLWLELAKLQ LPDKHLKHAE NVSAQLRYLS
ELLQSIGFRG SRQHNPPWDD ELQTDIDELY DELAEEGEQD SLLDDSDEDT LNNKLCTFSQ
TQKEFMNQHW YHCHTCNMIN TVGVCSVCAR VCHKGHDVSY AKYGNFFCDC GAKEDGSCQA
LSRRIGSNEV RDSAGIGSYL PSHMSLLAGK KRSSLPVGQP VLTRKDSLTN ERIAVLTKLL
EPYRETLQHQ DQWLLVVRCI LEYFDLLLPS INENCMLYSI VGCHKRATAA LERLHLLEQS
FQVTDQLMFA TLGSQEGAFE NVRMNYSGDQ GQTIKHLLSS GVVRRVAFCC LSSPHGRRQQ
LAVSHEKGKV TILQLSALLK QADASKRKLT LTQLSSAPIA CTVISLAANP CNEDCLAVCG
LKECHILTFS SSGSTNEHIV VNPQLENGNY IKKAVWLPGS QTLLAVVTSD YVKIYDLAVD
TYSPKYYYLV AVGKIRDCTF VYQDGNYNML TFASSGYIYT QQLDQQSLAV HGDFYVTNTL
ELSHQHIKDI AGHIGGGGVS IYYSHTLQLL FYSYSCGRSF FSPLTNVSEG VKGIYHLDTN
SASKSASKGP LQPLVQWTEV TGHPGLVYAS MQTSNNPIIL MITPERIYLQ EIKAQSAKSR
IMDVVGIRHA VAGVEKTTLL LLCEDGSLRI FSAQPEYTSF WLSPQVQPFG NQLYSSTLMA
KGGGSGSTSK SKSNTASGKM TSRKASQQQK QPTAGGQPVF PIDFFEHCNM LADVEFGGND
LLQIYNKQKL KTRLFSTGMF VASTRSNGFT LEVINNDPNV VIVGIRVLIG TQDVQRAPQS
VTILGRTIPT PVRRARWFDI PLTREEMLQS DKLLKVVFAK APDPEHVTLL DCIEVYGKSK
ELVGWPDESE DVTVPGSSAP AVSSSQASSA NFGEGFNCIT QLDRMANHLL EVMDCALHLL
GSGVPASMRQ KAVKTASALL LLPTPNPVQT QARYVLATLY GTRALYHNYK DGVLLQFVNR
ELQSMQPKLE KLETLREIDP EAFYRLVLMV RGIANARPQS LAKICVENNY DIVPTLMGIV
LELHKVTPTL DEPVNIVKRG LCQPETIVHC LVEIMYGFAL ADPGQVGRMT KYFIDLLKHD
ASVISHSAKE ALILLLSPRM KRRKVAIVTP PACSTPTPST STMQALQAAA SSAASDIIEE
AAGVVVDGSV GGGGLPEPNA DAEGAAVGVG GVGQQQMLNL EAFMGGGFPR LLGLPEDADD
EAIMDIAIAL SLQQHGGDAN ALQSLQQGLA NLQGIRQATA MAAAVNAAAN VSLGGSDDDE
GSNVATDGST LRTSPAEPAG SGGSESGGSG VESIGGTSAR SSNFGDHANA SPPRQGSTKD
DQEQPGPSGV AGSGGVAVLS AMSSSEDNEA NEDDKLSKLH DLRIAVLESI IQHLGTFDLC
NGLQAIPLIQ VILMLTTDLN GNNERDQQVL HDLLTALVDY VEIGKRGAAA RMETKCPGNE
VRLALLSLFG VLMGKTKSKQ TGTTSPPHQF KDNSSFVAST TANVLSKSGA FVYALEALNT
LLVHWKNVLG DPYAAGGGLA SQSAQASGGA SGPGVQLLKP IKHGPKPDIS ILIPHNYLKN
YPDIFESYDG LLTEIIVRLP YQILRLSSAH PDNYDSGFCE AMTFTLCEYM MLNLNTLLRR
QVRKLLMYIC GSKEKFRMYR DGHSLDAHFR VVKRVCNIVS SKTGAPYNAN PPMLSYDALV
ELTEHLRTCQ EISQMRTGNW QKFCVVHEDA LAMLMEIACY QLDDGVSPII IQLLQAAVCN
LPPPSGSKQA QPQPSTSSAS GKLRTDREKS EDTDAYYSKF DPAQCGTFVH QIFRYACDAL
IIRFVRIFLL ENNITQLRWQ AHSFMTGLFE HANERQREKL LNIFWNLWPL VPTYGRRTAQ
FVDLLGYLTL STRSITERLP EFVSRAVDVL RQQNELLCKH PNAPIYTTLE SILQVNGYYL
ESEPCLVCNN PEVPMANIKL PSVKSDSKYT TTTMIYKLVQ CHTISKLIVR IADLKRTKMV
RTINVYYNNR SVQAVVELKN RPALWHKARS VSLQSAQTEL KIDFPLPITA CNLMIEFADF
FETVSGSSEN LQCPRCSAAV PAYPGVCGNC GENVFQCHKC RAINYDEKDP FLCHSCGFCK
YAKFDFSMYA RVCCAVDPIE SAEDRVKTVS LIHSSLERAD RNYRQLLTNK QMLELLIQKV
AEHRSSDRMV EDNMASVHST SQVNKIIQLL AQKYCVESRT SFEELSKIVQ KVKACRSELV
AYDRQQQDQP PVNPGSTTGA ENPTTNRCYG CALASTEQCL TLLRAMAYNY DCRVCLYSQG
LVSELAEHNL RRGTPLIQEE VRNLLVVLTK DNAEACMHLL QLVTTRVKNA LMGSIPLISL
EAAVHQEMTL LEVLLGQDDI CWEYKLKVIF ELFISNCRLP RGPVTAVLHP CLRIMQNLIC
PVLPGSKPNQ KVATTDLCSM KMFEGNTVDY RAWLNSDRNH EYAAWSKRMP SNNQAKLKNA
KDQNVAASGG SDAPPKSRRE VRVAFLSEKY GKRWRERVLD KQRVIKPLVF NAKWIQPLLF
NANSRFGRQL ACSLLSSLSR TNERRQQALN MLTSFLKHVG EAGEASAEYL MLYKNMATEQ
PWLQYLVLKG VLSQISQLLA IEISKVHRME EYSLSSDLSL GYALRQYVEL LWLLLECPNI
RRTYKTRMLG PVLESYLALR SLVVQRTRLI DDAQEKLLEM LEDMTSGTEE ETRAFMEILI
DTVEKTRMND IKTPVFVFER LYSIIHPEEH DESEFYMTLE KDPQQEDFLQ GRMLGNPYPS
SEMGLGPLMR DVKNKICTDC ELIALLEDDN GMELLVNNKI ISLDLPVKDV YKKVWLAEGG
DRDAMRIVYR MRGLLGDATE EFVETLNNKS QEQVDTEQLY RMANVLADCN GLRVMLERIG
SLQRISRNRE LIQVLLKLFL ICVKVRRCQE VLCQPEIGAI NTLLKVLQMC LQSENDSIQS
AVTEQLLEIM ETILSKAASD TLDSFLQFSL TFGGPEYVSA LISCTDCPNV RNNPSVLRHL
IRVLAALVYG NEVKMALLCE HFKDTLNFNR FDNERTPEEE FKLELFCVLT NQIEHNCIGG
TLKDYIVSLG IVERSLAYIT EHAPCVKPTL LRTDSDELKE FISRPSLKYI LRFLTGLSNH
HEATQVAISK DIIPIIHRLE QVSSDEHVGS LAENLLEALS TDSATAARVQ QVRDFTRAEK
KRLAMATREK QLDALGMRTN EKGQVTAKGS ILQKIEKLRD ETGLTCFICR EGYACQPDKV
LGIYTFTKRC NVEEFELKSR KTIGYTTVTH FNVVHVDCHT SAIRLTRGRD EWERASLQNA
NTRCNGLLPL WGPAVGEAAF SACMTRHSSY MQESTQRCDI SYTSSVHDLK LLLVRFAWER
SFHDDAGGGG PQSNMHFVPY LLFYSVYLLL SSRSAARDSK TLLTYLQAPP SEKWLECGYE
VDGPLFMATI SLSLHSRELW NKHKLAHLKR MIAVAQGRHV SPAVLCKALL APADRQVKDY
TVYKPFLMMW ALVDLIYDNL FKTVSTPKEE DWPISLFDYL RKNDEALLKS TDSILQTLTE
EFLPCTSFVE FCDVAGLLHL IEHPDNFIEE ILAALPSTSS SN


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orb80987 Human Calmodulin protein Calmodulin Human Recombinant full length protein expressed in E.coli, having Molecular Weight of approximately 16 kDa, the Accession number is NP_001734. For research use only 10
orb81384 Staphylococcal Protein 434 a.a protein Recombinant Staphylococcal Protein produced in E.coli is non-glycosylated, Polypeptide chain containing 434 amino acids (37-469 a.a.) and having a molecular mass 10
orb80853 Human Protein Kinase beta 1 protein PKC-bI Human Recombinant produced in Sf9 is glycosylated, polypeptide chain containing amino acids 2-671 and having a molecular mass of 80 KD. This protein is the f 2
orb80854 Human Protein Kinase beta 2 protein PKC-bII Human Recombinant produced in Sf9 is glycosylated, polypeptide chain containing amino acids 2-673 and having a molecular mass of 80 KD. This protein is the 2
orb80858 Human Protein Kinase q protein PKC-q Human Recombinant produced in Sf9 is glycosylated, polypeptide chain containing amino acids 2-706 and having a molecular mass of 86 KD. This protein is the full-le 2
orb80857 Human Protein Kinase gamma protein PKC-g Human Recombinant produced in Sf9 is glycosylated, polypeptide chain containing amino acids 2-676 and having a molecular mass of 80 KD. This protein is the ful 2
orb80855 Human Protein Kinase delta protein PKC-d Human Recombinant produced in Sf9 is glycosylated, polypeptide chain containing amino acids 2-676 and having a molecular mass of 80 KD. This protein is the ful 2
orb80784 C-JUN protein C-JUN amino acids 1-81 produced in E.coli, is non-glycosylated, polypeptide chain having a molecular mass of 52 kDa.C-JUN is maltose binding protein (MBP) fusion protein with an amino-te 2
orb80856 Human Protein Kinase e protein PRKCE Human Recombinant produced in Sf9 is glycosylated, polypeptide chain containing amino acids 2-737 and having a molecular mass of 87 KD. This protein is the full-le 2
orb81389 Human Stromal Interaction Molecule 1 protein Recombinant STIM1 produced in E.coli is a single, non-glycosylated polypeptide chain containing 343 amino acids and having a molecular mass of 38 kDa. STIM 5
orb80986 Human Calmodulin-2 protein Recombinant CALM2 produced in E.coli is a single, non-glycosylated polypeptide chain containing 149 amino acids and having a molecular mass of 16 kDa. CALM2 is purified by c 5
orb81750 Epstein-Barr Virus (HHV-4) EBNA1 His tag protein The E.coli derived recombinant protein contains the HHV-4 EBNA1 regions 408-641 amino acids having a molecular mass of 24.8kDa. The EBNA1 protein is fu 100
orb81382 Staphylococcal Protein-A protein Recombinant Staphylococcal Protein produced in E.coli is non-glycosylated, Polypeptide chain having a molecular mass of 45 kDa. Recombinant Staphylococcal Protein is p 10 mg
orb80849 Human Protein Kinase Akt1_PKB alpha Active Enzyme protein Recombinant Human Protein Kinase is glycosylated polypeptide having a molecular mass of 59.1 kDa. Recombinant Protein Kinase is purified by pr 5
orb81253 Human Proliferation-associated protein 2G4 protein PA2G4 produced in E.coli is a single, non-glycosylated polypeptide chain containing 402 amino acids (1-394 a.a.) and having a molecular mass of 44.8k 5
orb81753 Epstein-Barr Virus (HHV-4) p18 GST protein The E.coli derived recombinant protein contains the HHV-4 p18 regions, having a molecular mass of 35.4kDa which includes GST tag at N-terminus. For research 100
orb81462 Human Vesicle-Associated Membrane Protein 4 protein VAMP4 produced in E.coli is a single, non-glycosylated polypeptide chain containing 123 amino acids (1-115 a.a.) and having a molecular mass of 14.5 2
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orb81054 Human C-Terminal Binding Protein 1 protein CTBP1 produced in E.coli is a single,non-glycosylated polypeptide chain containing 440 amino acids (1-400 a.a.) and having a molecular mass of 47.5 kDa. CTBP 5
orb81354 Protein Export Protein SecB protein Recombinant E.coli SecB produced in E.coli is a single, non-glycosylated polypeptide chain containing 155 amino acids and having a molecular mass of 17.2 kDa. SecB 5
PAH-G1-2 Protein Arrays containing 234 Human Protein for simultaneous detection of Protein function, including Protein-protein interaction, Protein modification, antibody specificity, auto-antibody and small m 1 glass slide with 2 sub-arrays
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