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Regulator of microtubule dynamics protein 3 (RMD-3) (hRMD-3) (Cerebral protein 10) (Protein FAM82A2) (Protein FAM82C) (Protein tyrosine phosphatase-interacting protein 51) (TCPTP-interacting protein 51)

 RMD3_HUMAN              Reviewed;         470 AA.
Q96TC7; A9UMZ9; B3KRR3; Q6ZWE9; Q96H23; Q96SD6; Q9H6G1; Q9NVQ6;
15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
15-MAY-2007, sequence version 2.
22-NOV-2017, entry version 121.
RecName: Full=Regulator of microtubule dynamics protein 3;
Short=RMD-3;
Short=hRMD-3;
AltName: Full=Cerebral protein 10;
AltName: Full=Protein FAM82A2;
AltName: Full=Protein FAM82C;
AltName: Full=Protein tyrosine phosphatase-interacting protein 51;
AltName: Full=TCPTP-interacting protein 51;
Name=RMDN3; Synonyms=FAM82A2, FAM82C, PTPIP51;
ORFNames=hucep-10, UNQ3122/PRO10274;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Brain;
Yoshimoto M., Yazaki M., Matsumoto K., Takayama K.;
"Molecular cloning of a novel gene expressed in human cerebral
cortex.";
Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
PubMed=12975309; DOI=10.1101/gr.1293003;
Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S.,
Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J.,
Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J.,
Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A.,
Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H.,
Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D.,
Wood W.I., Godowski P.J., Gray A.M.;
"The secreted protein discovery initiative (SPDI), a large-scale
effort to identify novel human secreted and transmembrane proteins: a
bioinformatics assessment.";
Genome Res. 13:2265-2270(2003).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Amygdala, and Teratocarcinoma;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain, and Uterus;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 78-470.
Porsche A., Hofer W.H.;
"A protein interacting with T-cell tyrosine phosphatase.";
Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
[7]
IDENTIFICATION, INTERACTION WITH MICROTUBULES, AND SUBCELLULAR
LOCATION.
PubMed=18070910; DOI=10.1083/jcb.200705108;
Oishi K., Okano H., Sawa H.;
"RMD-1, a novel microtubule-associated protein, functions in
chromosome segregation in Caenorhabditis elegans.";
J. Cell Biol. 179:1149-1162(2007).
[8]
TISSUE SPECIFICITY, AND INTERACTION WITH PTPN2.
PubMed=15609043; DOI=10.1007/s00418-004-0732-7;
Stenzinger A., Kajosch T., Tag C., Porsche A., Welte I., Hofer H.W.,
Steger K., Wimmer M.;
"The novel protein PTPIP51 exhibits tissue- and cell-specific
expression.";
Histochem. Cell Biol. 123:19-28(2005).
[9]
FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=16820967; DOI=10.1007/s10495-006-8882-9;
Lv B.F., Yu C.F., Chen Y.Y., Lu Y., Guo J.H., Song Q.S., Ma D.L.,
Shi T.P., Wang L.;
"Protein tyrosine phosphatase interacting protein 51 (PTPIP51) is a
novel mitochondria protein with an N-terminal mitochondrial targeting
sequence and induces apoptosis.";
Apoptosis 11:1489-1501(2006).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[11]
INDUCTION, AND SUBCELLULAR LOCATION.
PubMed=17361080; DOI=10.1159/000098949;
Stenzinger A., Schreiner D., Pfeiffer T., Tag C., Hofer H.W.,
Wimmer M.;
"Epidermal growth factor-, transforming growth factor-beta-, retinoic
acid-and 1,25-dihydroxyvitamin D(3)-regulated expression of the novel
protein PTPIP51 in keratinocytes.";
Cells Tissues Organs 184:76-87(2006).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18220336; DOI=10.1021/pr0705441;
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
Yates J.R. III;
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
efficient phosphoproteomic analysis.";
J. Proteome Res. 7:1346-1351(2008).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-44 AND SER-212, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-46, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[18]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[19]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[20]
FUNCTION IN CELLULAR CALCIUM HOMEOSTASIS REGULATION, SUBCELLULAR
LOCATION, AND INTERACTION WITH VAPB.
PubMed=22131369; DOI=10.1093/hmg/ddr559;
De Vos K.J., Morotz G.M., Stoica R., Tudor E.L., Lau K.F.,
Ackerley S., Warley A., Shaw C.E., Miller C.C.;
"VAPB interacts with the mitochondrial protein PTPIP51 to regulate
calcium homeostasis.";
Hum. Mol. Genet. 21:1299-1311(2012).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-44 AND SER-46, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50; SER-183; SER-193;
SER-212 AND SER-232, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[23]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
-!- FUNCTION: Involved in cellular calcium homeostasis regulation. May
participate in differentiation and apoptosis of keratinocytes.
Overexpression induces apoptosis. {ECO:0000269|PubMed:16820967,
ECO:0000269|PubMed:22131369}.
-!- SUBUNIT: Interacts with PTPN2. Interacts with microtubules.
Interacts with VAPB. {ECO:0000269|PubMed:15609043,
ECO:0000269|PubMed:18070910, ECO:0000269|PubMed:22131369}.
-!- INTERACTION:
P18031:PTPN1; NbExp=4; IntAct=EBI-1056589, EBI-968788;
P31946:YWHAB; NbExp=5; IntAct=EBI-1056589, EBI-359815;
-!- SUBCELLULAR LOCATION: Mitochondrion membrane; Single-pass membrane
protein. Mitochondrion outer membrane. Cytoplasm. Nucleus.
Cytoplasm, cytoskeleton, spindle. Cytoplasm, cytoskeleton, spindle
pole. Note=In interphase localizes in the cytoplasm, and during
mitosis localizes to the spindle microtubules and spindle poles.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q96TC7-1; Sequence=Displayed;
Name=2;
IsoId=Q96TC7-2; Sequence=VSP_025531;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Present at high level in epidermis and
seminiferous epithelium: while basal cells in the epidermis and
spermatogonia show no perceptible amount, keratinocytes of
suprabasal layers and differentiating first-order spermatocytes up
to spermatids exhibit high expression. In skeletal muscle, its
presence is restricted to fibers of the fast twitch type. In
surface epithelia containing ciliated cells, it is associated with
the microtubular structures responsible for ciliary movement. Also
present in specific structures of the central nervous system such
as neurons of the hippocampal region, ganglion cells of the
autonomic nervous system, and axons of the peripheral nervous
system (at protein level). Widely expressed.
{ECO:0000269|PubMed:15609043, ECO:0000269|PubMed:16820967}.
-!- INDUCTION: By EGF, TGFB1, retinoic acid-and 1,25-dihydroxyvitamin
D(3). {ECO:0000269|PubMed:17361080}.
-!- DOMAIN: The transmembrane region is required for mitochondrial
localization.
-!- SIMILARITY: Belongs to the RMDN family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAB15298.1; Type=Erroneous termination; Positions=453; Note=Translated as Glu.; Evidence={ECO:0000305};
Sequence=BAC85554.1; Type=Frameshift; Positions=383; Evidence={ECO:0000305};
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EMBL; AB000782; BAB46923.1; -; mRNA.
EMBL; AY358793; AAQ89153.1; -; mRNA.
EMBL; AK001441; BAA91693.1; -; mRNA.
EMBL; AK025963; BAB15298.1; ALT_SEQ; mRNA.
EMBL; AK092058; BAG52475.1; -; mRNA.
EMBL; AK123282; BAG53885.1; -; mRNA.
EMBL; AK123192; BAC85554.1; ALT_FRAME; mRNA.
EMBL; CH471125; EAW92436.1; -; Genomic_DNA.
EMBL; BC008970; AAH08970.2; -; mRNA.
EMBL; BC063844; AAH63844.1; -; mRNA.
EMBL; AJ242719; CAC39480.1; -; Genomic_DNA.
EMBL; BR000691; FAA00416.1; -; mRNA.
CCDS; CCDS10063.1; -. [Q96TC7-1]
RefSeq; NP_001291731.1; NM_001304802.1. [Q96TC7-1]
RefSeq; NP_001310823.1; NM_001323894.1. [Q96TC7-1]
RefSeq; NP_001310824.1; NM_001323895.1. [Q96TC7-2]
RefSeq; NP_060615.1; NM_018145.2. [Q96TC7-1]
UniGene; Hs.511067; -.
UniGene; Hs.632944; -.
ProteinModelPortal; Q96TC7; -.
SMR; Q96TC7; -.
BioGrid; 120476; 42.
IntAct; Q96TC7; 21.
MINT; MINT-1631442; -.
STRING; 9606.ENSP00000260385; -.
iPTMnet; Q96TC7; -.
PhosphoSitePlus; Q96TC7; -.
SwissPalm; Q96TC7; -.
BioMuta; RMDN3; -.
DMDM; 147643203; -.
EPD; Q96TC7; -.
MaxQB; Q96TC7; -.
PaxDb; Q96TC7; -.
PeptideAtlas; Q96TC7; -.
PRIDE; Q96TC7; -.
TopDownProteomics; Q96TC7-1; -. [Q96TC7-1]
TopDownProteomics; Q96TC7-2; -. [Q96TC7-2]
DNASU; 55177; -.
Ensembl; ENST00000260385; ENSP00000260385; ENSG00000137824. [Q96TC7-1]
Ensembl; ENST00000338376; ENSP00000342493; ENSG00000137824. [Q96TC7-1]
GeneID; 55177; -.
KEGG; hsa:55177; -.
UCSC; uc001zmp.1; human. [Q96TC7-1]
CTD; 55177; -.
DisGeNET; 55177; -.
EuPathDB; HostDB:ENSG00000137824.15; -.
GeneCards; RMDN3; -.
HGNC; HGNC:25550; RMDN3.
HPA; HPA009975; -.
MIM; 611873; gene.
neXtProt; NX_Q96TC7; -.
OpenTargets; ENSG00000137824; -.
PharmGKB; PA162387926; -.
eggNOG; ENOG410IIGM; Eukaryota.
eggNOG; ENOG41101S6; LUCA.
GeneTree; ENSGT00530000063162; -.
HOVERGEN; HBG072518; -.
InParanoid; Q96TC7; -.
OMA; EVRSHME; -.
OrthoDB; EOG091G0F3V; -.
PhylomeDB; Q96TC7; -.
TreeFam; TF315854; -.
GenomeRNAi; 55177; -.
PRO; PR:Q96TC7; -.
Proteomes; UP000005640; Chromosome 15.
Bgee; ENSG00000137824; -.
CleanEx; HS_FAM82A2; -.
ExpressionAtlas; Q96TC7; baseline and differential.
Genevisible; Q96TC7; HS.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
GO; GO:0005741; C:mitochondrial outer membrane; IDA:UniProtKB.
GO; GO:0005739; C:mitochondrion; IDA:HPA.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
GO; GO:0006874; P:cellular calcium ion homeostasis; IMP:UniProtKB.
Gene3D; 1.25.40.10; -; 3.
InterPro; IPR011990; TPR-like_helical_dom_sf.
SUPFAM; SSF48452; SSF48452; 1.
1: Evidence at protein level;
Alternative splicing; Apoptosis; Coiled coil; Complete proteome;
Cytoplasm; Cytoskeleton; Differentiation; Membrane; Microtubule;
Mitochondrion; Mitochondrion outer membrane; Nucleus; Phosphoprotein;
Polymorphism; Reference proteome; Transmembrane; Transmembrane helix.
CHAIN 1 470 Regulator of microtubule dynamics protein
3.
/FTId=PRO_0000287510.
TRANSMEM 13 35 Helical. {ECO:0000255}.
COILED 92 124 {ECO:0000255}.
MOD_RES 44 44 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 46 46 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163}.
MOD_RES 50 50 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 57 57 Phosphoserine.
{ECO:0000250|UniProtKB:Q3UJU9}.
MOD_RES 183 183 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 193 193 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 212 212 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:24275569}.
MOD_RES 232 232 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
VAR_SEQ 1 129 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_025531.
VARIANT 33 33 Q -> H (in dbSNP:rs11558807).
/FTId=VAR_049029.
CONFLICT 416 416 F -> V (in Ref. 1; BAB46923).
{ECO:0000305}.
CONFLICT 469 469 R -> Q (in Ref. 3; BAC85554).
{ECO:0000305}.
SEQUENCE 470 AA; 52118 MW; 1C8D1022E6CF7B6A CRC64;
MSRLGALGGA RAGLGLLLGT AAGLGFLCLL YSQRWKRTQR HGRSQSLPNS LDYTQTSDPG
RHVMLLRAVP GGAGDASVLP SLPREGQEKV LDRLDFVLTS LVALRREVEE LRSSLRGLAG
EIVGEVRCHM EENQRVARRR RFPFVRERSD STGSSSVYFT ASSGATFTDA ESEGGYTTAN
AESDNERDSD KESEDGEDEV SCETVKMGRK DSLDLEEEAA SGASSALEAG GSSGLEDVLP
LLQQADELHR GDEQGKREGF QLLLNNKLVY GSRQDFLWRL ARAYSDMCEL TEEVSEKKSY
ALDGKEEAEA ALEKGDESAD CHLWYAVLCG QLAEHESIQR RIQSGFSFKE HVDKAIALQP
ENPMAHFLLG RWCYQVSHLS WLEKKTATAL LESPLSATVE DALQSFLKAE ELQPGFSKAG
RVYISKCYRE LGKNSEARWW MKLALELPDV TKEDLAIQKD LEELEVILRD


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EIAAB35350 Fam82a2,Fam82c,Protein FAM82A2,Protein FAM82C,Rat,Rattus norvegicus,Regulator of microtubule dynamics protein 3,RMD-3
EIAAB35343 CGI-90,FAM82B,Homo sapiens,hRMD-1,Human,Protein FAM82B,Regulator of microtubule dynamics protein 1,RMD-1
EIAAB35348 BLOCK18,FAM82A,FAM82A1,Homo sapiens,hRMD-2,Human,Protein FAM82A1,Regulator of microtubule dynamics protein 2,RMD-2,UNQ9371_PRO34163
15-288-21471 Liprin-alpha-1 - Protein tyrosine phosphatase receptor type f polypeptide-interacting protein alpha-1; PTPRF-interacting protein alpha-1; LAR-interacting protein 1; LIP.1 Polyclonal 0.1 mg
15-288-21470 Liprin-alpha-1 - Protein tyrosine phosphatase receptor type f polypeptide-interacting protein alpha-1; PTPRF-interacting protein alpha-1; LAR-interacting protein 1; LIP.1 Polyclonal 0.1 mg
15-288-21471 Liprin-alpha-1 - Protein tyrosine phosphatase receptor type f polypeptide-interacting protein alpha-1; PTPRF-interacting protein alpha-1; LAR-interacting protein 1; LIP.1 Polyclonal 0.05 mg
15-288-21470 Liprin-alpha-1 - Protein tyrosine phosphatase receptor type f polypeptide-interacting protein alpha-1; PTPRF-interacting protein alpha-1; LAR-interacting protein 1; LIP.1 Polyclonal 0.05 mg
EIAAB32049 Macrophage actin-associated tyrosine-phosphorylated protein,Mayp,Mouse,Mus musculus,PEST phosphatase-interacting protein 2,pp37,Proline-serine-threonine phosphatase-interacting protein 2,Pstpip2
EIAAB44014 CEV14,Clonal evolution-related gene on chromosome 14 protein,GMAP-210,Golgi-associated microtubule-binding protein 210,Homo sapiens,Human,Thyroid receptor-interacting protein 11,TR-interacting protein
EIAAB40512 Mouse,Mus musculus,Phosphoserine_threonine_tyrosine interaction protein,Protein tyrosine phosphatase-like protein,Serine_threonine_tyrosine-interacting protein,Styx
EIAAB31218 Homo sapiens,hPIP1,Human,p21-activated protein kinase-interacting protein 1,PAK_PLC-interacting protein 1,PAK1-interacting protein 1,PAK1IP1,PIP1,WD repeat-containing protein 84,WDR84
EIAAB46349 Homo sapiens,Human,Protein PRPL-2,WAS_WASL-interacting protein family member 1,WASP-interacting protein,WASPIP,WIP,WIPF1,Wiskott-Aldrich syndrome protein-interacting protein
EIAAB39347 Mouse,Mus musculus,Spata24,Spermatogenesis-associated protein 24,TATA-binding protein-like factor-interacting protein,Testis protein T6441 homolog,Tipt,Tipt2,TLF-interacting protein,TRF2-interacting p
EIAAB07420 Cdc42-interacting protein 4,CIP4,Homo sapiens,hSTP,Human,Protein Felic,Salt tolerant protein,STOT,STP,Thyroid receptor-interacting protein 10,TR-interacting protein 10,TRIP10,TRIP-10
EIAAB31034 Androgen receptor-interacting protein 3,ARIP3,DAB2-interacting protein,DIP,E3 SUMO-protein ligase PIAS2,Homo sapiens,Human,Miz1,Msx-interacting zinc finger protein,PIAS2,PIAS-NY protein,PIASX,Protein
EIAAB27017 45 kDa NF-AT-interacting protein,45 kDa NFAT-interacting protein,Homo sapiens,Human,NFATC2-interacting protein,NFATC2IP,NIP45,Nuclear factor of activated T-cells, cytoplasmic 2-interacting protein
EIAAB27018 45 kDa NF-AT-interacting protein,45 kDa NFAT-interacting protein,Mouse,Mus musculus,NFATC2-interacting protein,Nfatc2ip,Nip45,Nuclear factor of activated T-cells, cytoplasmic 2-interacting protein
CSB-EL008337RA Rat Regulator of microtubule dynamics protein 3(FAM82A2) ELISA kit 96T
G7140 Regulator of microtubule dynamics protein 3 (FAM82A2), Rat, ELISA Kit 96T
CSB-EL008337BO Bovine Regulator of microtubule dynamics protein 3(FAM82A2) ELISA kit 96T
CSB-EL008337MO Mouse Regulator of microtubule dynamics protein 3(FAM82A2) ELISA kit 96T
G7138 Regulator of microtubule dynamics protein 3 (FAM82A2), Human, ELISA Kit 96T


 

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