Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Syndetin (Coiled-coil domain-containing protein 132) (EARP/GARPII complex subunit VPS50)

 VPS50_HUMAN             Reviewed;         964 AA.
Q96JG6; B3KX22; D1MQ00; F5H5U7; Q75N07; Q8WVK3; Q9H5C6;
23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
23-OCT-2007, sequence version 3.
12-SEP-2018, entry version 117.
RecName: Full=Syndetin {ECO:0000303|PubMed:25799061};
AltName: Full=Coiled-coil domain-containing protein 132 {ECO:0000305};
AltName: Full=EARP/GARPII complex subunit VPS50 {ECO:0000312|HGNC:HGNC:25956};
Name=VPS50 {ECO:0000312|HGNC:HGNC:25956};
Synonyms=CCDC132, KIAA1861 {ECO:0000303|PubMed:11347906};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=11347906; DOI=10.1093/dnares/8.2.85;
Nagase T., Nakayama M., Nakajima D., Kikuno R., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. XX.
The complete sequences of 100 new cDNA clones from brain which code
for large proteins in vitro.";
DNA Res. 8:85-95(2001).
[2]
SEQUENCE REVISION.
Nagase T., Nakayama M., Nakajima D., Kikuno R., Ohara O.;
Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
PubMed=21472204; DOI=10.3892/mmr_00000222;
Matsumoto Y., Imai Y., Sugita Y., Tanaka T., Tsujimoto G., Saito H.,
Oshida T.;
"CCDC132 is highly expressed in atopic dermatitis T cells.";
Mol. Med. Report. 3:83-87(2010).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND NUCLEOTIDE
SEQUENCE [LARGE SCALE MRNA] OF 446-964 (ISOFORM 1).
TISSUE=Lung, and Uterus;
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).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12853948; DOI=10.1038/nature01782;
Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R.,
Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E.,
Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H.,
Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A.,
Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J.,
Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A.,
Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S.,
Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M.,
Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C.,
Latreille P., Miller N., Johnson D., Murray J., Woessner J.P.,
Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J.,
Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L.,
Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R.,
Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K.,
Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S.,
Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M.,
Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R.,
Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D.,
Waterston R.H., Wilson R.K.;
"The DNA sequence of human chromosome 7.";
Nature 424:157-164(2003).
[6]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Skin, and Testis;
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).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=16964243; DOI=10.1038/nbt1240;
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein
phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15, AND 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).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-494; SER-498; SER-559
AND SER-561, 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).
[11]
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).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-559 AND SER-561, 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).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15 AND SER-559, AND
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).
[14]
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).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-559 AND SER-561, AND
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).
[16]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15; SER-494; SER-498;
SER-559 AND SER-561, 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).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-494; SER-559 AND
SER-561, 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).
[19]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-963, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25218447; DOI=10.1038/nsmb.2890;
Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
Vertegaal A.C.;
"Uncovering global SUMOylation signaling networks in a site-specific
manner.";
Nat. Struct. Mol. Biol. 21:927-936(2014).
[20]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-963, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25114211; DOI=10.1073/pnas.1413825111;
Impens F., Radoshevich L., Cossart P., Ribet D.;
"Mapping of SUMO sites and analysis of SUMOylation changes induced by
external stimuli.";
Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
[21]
FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY,
AND IDENTIFICATION IN THE EARP COMPLEX.
PubMed=25799061; DOI=10.1038/ncb3129;
Schindler C., Chen Y., Pu J., Guo X., Bonifacino J.S.;
"EARP is a multisubunit tethering complex involved in endocytic
recycling.";
Nat. Cell Biol. 17:639-650(2015).
[22]
IDENTIFICATION IN THE EARP COMPLEX, AND INTERACTION WITH EIPR1.
PubMed=27440922; DOI=10.1091/mbc.E16-04-0209;
Gershlick D.C., Schindler C., Chen Y., Bonifacino J.S.;
"TSSC1 is novel component of the endosomal retrieval machinery.";
Mol. Biol. Cell 27:2867-2878(2016).
[23]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-963, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
-!- FUNCTION: Acts as component of the EARP complex that is involved
in endocytic recycling. The EARP complex associates with Rab4-
positive endosomes and promotes recycling of internalized
transferrin receptor (TFRC) to the plasma membrane. Within the
EARP complex, required to tether the complex to recycling
endosomes. Not involved in retrograde transport from early and
late endosomes to the trans-Golgi network (TGN).
{ECO:0000269|PubMed:25799061}.
-!- SUBUNIT: Component of the endosome-associated retrograde protein
(EARP) complex, composed of VPS51, VPS52, VPS53 and VPS50/Syndetin
(PubMed:25799061, PubMed:27440922). The EARP complex interacts
with EIPR1 (PubMed:27440922). {ECO:0000269|PubMed:25799061,
ECO:0000269|PubMed:27440922}.
-!- INTERACTION:
Q9UID3-1:VPS51; NbExp=6; IntAct=EBI-11044388, EBI-16067837;
Q8N1B4:VPS52; NbExp=7; IntAct=EBI-11044388, EBI-2799833;
Q5VIR6:VPS53; NbExp=7; IntAct=EBI-11044388, EBI-2850511;
-!- SUBCELLULAR LOCATION: Recycling endosome
{ECO:0000269|PubMed:25799061}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q96JG6-1; Sequence=Displayed;
Name=2;
IsoId=Q96JG6-2; Sequence=VSP_028658, VSP_028659;
Name=3;
IsoId=Q96JG6-3; Sequence=VSP_045572;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Ubiquitous, with higher expression in brain
and skeletal muscle. {ECO:0000269|PubMed:21472204}.
-!- MISCELLANEOUS: Was named 'syndetin' after the Greek 'syndeo',
which means 'connect' or 'tether'. {ECO:0000303|PubMed:25799061}.
-!- SIMILARITY: Belongs to the syndetin family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAB15701.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=BAB47490.2; Type=Frameshift; Positions=2; Evidence={ECO:0000305};
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; AB058764; BAB47490.2; ALT_FRAME; mRNA.
EMBL; AB100163; BAI52922.1; -; mRNA.
EMBL; AK027234; BAB15701.1; ALT_INIT; mRNA.
EMBL; AK126478; BAG54334.1; -; mRNA.
EMBL; AC002379; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC002453; AAS02023.1; -; Genomic_DNA.
EMBL; CH236949; EAL24143.1; -; Genomic_DNA.
EMBL; CH471091; EAW76816.1; -; Genomic_DNA.
EMBL; CH471091; EAW76818.1; -; Genomic_DNA.
EMBL; BC108708; AAI08709.1; -; mRNA.
EMBL; BC017888; AAH17888.1; -; mRNA.
EMBL; BC132740; AAI32741.1; -; mRNA.
EMBL; BC132742; AAI32743.1; -; mRNA.
CCDS; CCDS43617.1; -. [Q96JG6-1]
CCDS; CCDS5630.1; -. [Q96JG6-2]
CCDS; CCDS59065.1; -. [Q96JG6-3]
RefSeq; NP_001244927.1; NM_001257998.1. [Q96JG6-3]
RefSeq; NP_060137.2; NM_017667.3. [Q96JG6-1]
RefSeq; NP_078829.1; NM_024553.2. [Q96JG6-2]
UniGene; Hs.202424; -.
ProteinModelPortal; Q96JG6; -.
BioGrid; 120750; 66.
CORUM; Q96JG6; -.
DIP; DIP-61628N; -.
IntAct; Q96JG6; 27.
STRING; 9606.ENSP00000307666; -.
iPTMnet; Q96JG6; -.
PhosphoSitePlus; Q96JG6; -.
BioMuta; CCDC132; -.
DMDM; 160019079; -.
EPD; Q96JG6; -.
MaxQB; Q96JG6; -.
PaxDb; Q96JG6; -.
PeptideAtlas; Q96JG6; -.
PRIDE; Q96JG6; -.
ProteomicsDB; 76956; -.
ProteomicsDB; 76957; -. [Q96JG6-2]
DNASU; 55610; -.
Ensembl; ENST00000251739; ENSP00000251739; ENSG00000004766. [Q96JG6-2]
Ensembl; ENST00000305866; ENSP00000307666; ENSG00000004766. [Q96JG6-1]
Ensembl; ENST00000544910; ENSP00000443104; ENSG00000004766. [Q96JG6-3]
GeneID; 55610; -.
KEGG; hsa:55610; -.
UCSC; uc003umn.4; human. [Q96JG6-1]
CTD; 55610; -.
EuPathDB; HostDB:ENSG00000004766.15; -.
GeneCards; VPS50; -.
H-InvDB; HIX0006848; -.
HGNC; HGNC:25956; VPS50.
HPA; HPA026679; -.
MIM; 616465; gene.
neXtProt; NX_Q96JG6; -.
OpenTargets; ENSG00000004766; -.
PharmGKB; PA162381332; -.
eggNOG; KOG2939; Eukaryota.
eggNOG; ENOG410XS88; LUCA.
GeneTree; ENSGT00390000003442; -.
HOGENOM; HOG000230787; -.
HOVERGEN; HBG075377; -.
InParanoid; Q96JG6; -.
OMA; KWDVKEI; -.
OrthoDB; EOG091G01I8; -.
PhylomeDB; Q96JG6; -.
TreeFam; TF106152; -.
ChiTaRS; VPS50; human.
GeneWiki; FLJ20097_/_CCDC132; -.
GenomeRNAi; 55610; -.
PRO; PR:Q96JG6; -.
Proteomes; UP000005640; Chromosome 7.
Bgee; ENSG00000004766; Expressed in 203 organ(s), highest expression level in stomach.
CleanEx; HS_CCDC132; -.
ExpressionAtlas; Q96JG6; baseline and differential.
Genevisible; Q96JG6; HS.
GO; GO:0005829; C:cytosol; IEA:GOC.
GO; GO:1990745; C:EARP complex; IDA:UniProtKB.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0016020; C:membrane; HDA:UniProtKB.
GO; GO:0055037; C:recycling endosome; IDA:UniProtKB.
GO; GO:0000149; F:SNARE binding; IDA:MGI.
GO; GO:0032456; P:endocytic recycling; IDA:MGI.
GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
InterPro; IPR019514; DUF2451_C.
InterPro; IPR019515; VPS54_N.
Pfam; PF10474; DUF2451; 1.
Pfam; PF10475; Vps54_N; 1.
1: Evidence at protein level;
Acetylation; Alternative splicing; Coiled coil; Complete proteome;
Endosome; Isopeptide bond; Phosphoprotein; Protein transport;
Reference proteome; Transport; Ubl conjugation.
CHAIN 1 964 Syndetin.
/FTId=PRO_0000307265.
COILED 82 105 {ECO:0000255}.
COILED 216 244 {ECO:0000255}.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000244|PubMed:22814378}.
MOD_RES 15 15 Phosphoserine.
{ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 494 494 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 498 498 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 559 559 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 561 561 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
CROSSLNK 963 963 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1);
alternate. {ECO:0000244|PubMed:25114211}.
CROSSLNK 963 963 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:25114211,
ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:28112733}.
VAR_SEQ 1 34 MQKIKSLMTRQGLKSPQESLSDLGAIESLRVPGK -> MLT
L (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_045572.
VAR_SEQ 315 327 HVTPDSYIPCLAD -> VCSDLITIHISLL (in
isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_028658.
VAR_SEQ 328 964 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_028659.
CONFLICT 96 96 Q -> H (in Ref. 4; BAG54334).
{ECO:0000305}.
CONFLICT 670 670 Missing (in Ref. 4; BAB15701).
{ECO:0000305}.
CONFLICT 812 812 H -> Y (in Ref. 4; BAB15701).
{ECO:0000305}.
CONFLICT 926 926 E -> K (in Ref. 4; BAB15701).
{ECO:0000305}.
SEQUENCE 964 AA; 111174 MW; 2C748490DDBCBAD5 CRC64;
MQKIKSLMTR QGLKSPQESL SDLGAIESLR VPGKEEFREL REQPSDPQAE QELINSIEQV
YFSVDSFDIV KYELEKLPPV LNLQELEAYR DKLKQQQAAV SKKVADLILE KQPAYVKELE
RVTSLQTGLQ LAAVICTNGR RHLNIAKEGF TQASLGLLAN QRKRQLLIGL LKSLRTIKTL
QRTDVRLSEM LEEEDYPGAI QLCLECQKAA STFKHYSCIS ELNSKLQDTL EQIEEQLDVA
LSKICKNFDI NHYTKVQQAY RLLGKTQTAM DQLHMHFTQA IHNTVFQVVL GYVELCAGNT
DTKFQKLQYK DLCTHVTPDS YIPCLADLCK ALWEVMLSYY RTMEWHEKHD NEDTASASEG
SNMIGTEETN FDRGYIKKKL EHGLTRIWQD VQLKVKTYLL GTDLSIFKYD DFIFVLDIIS
RLMQVGEEFC GSKSEVLQES IRKQSVNYFK NYHRTRLDEL RMFLENETWE LCPVKSNFSI
LQLHEFKFME QSRSPSVSPS KQPVSTSSKT VTLFEQYCSG GNPFEIQANH KDEETEDVLA
SNGYESDEQE KSAYQEYDSD SDVPEELKRD YVDEQTGDGP VKSVSRETLK SRKKSDYSLN
KVNAPILTNT TLNVIRLVGK YMQMMNILKP IAFDVIHFMS QLFDYYLYAI YTFFGRNDSL
ESTGLGLSSS RLRTTLNRIQ ESLIDLEVSA DPTATLTAAE ERKEKVPSPH LSHLVVLTSG
DTLYGLAERV VATESLVFLA EQFEFLQPHL DAVMPAVKKP FLQQFYSQTV STASELRKPI
YWIVAGKALD YEQMLLLMAN VKWDVKEIMS QHNIYVDALL KEFEQFNRRL NEVSKRVRIP
LPVSNILWEH CIRLANRTIV EGYANVKKCS NEGRALMQLD FQQFLMKLEK LTDIRPIPDK
EFVETYIKAY YLTENDMERW IKEHREYSTK QLTNLVNVCL GSHINKKARQ KLLAAIDDID
RPKR


Related products :

Catalog number Product name Quantity
EIAAB07128 C9orf49,CHCHD2P9,CHCHD9,Coiled-coil-helix-coiled-coil-helix domain-containing 2 pseudogene 9,Homo sapiens,Human,Putative coiled-coil-helix-coiled-coil-helix domain-containing protein CHCHD2P9, mitocho
EIAAB05955 Ccdc53,Coiled-coil domain-containing protein 53,Mouse,Mus musculus,WASH complex subunit CCDC53
EIAAB05954 Bos taurus,Bovine,CCDC53,Coiled-coil domain-containing protein 53,WASH complex subunit CCDC53
EIAAB05953 AD-016,CCDC53,CGI-116,Coiled-coil domain-containing protein 53,Homo sapiens,Human,WASH complex subunit CCDC53,x0009
EIAAB13843 Abra1,BRCA1-A complex subunit Abraxas,Ccdc98,Coiled-coil domain-containing protein 98,Fam175a,Protein FAM175A,Rat,Rattus norvegicus
EIAAB13845 Abra1,BRCA1-A complex subunit Abraxas,Ccdc98,Coiled-coil domain-containing protein 98,Fam175a,Mouse,Mus musculus,Protein FAM175A
EIAAB13841 ABRA1,Bos taurus,Bovine,BRCA1-A complex subunit Abraxas,CCDC98,Coiled-coil domain-containing protein 98,FAM175A,Protein FAM175A
EIAAB13844 ABRA1,BRCA1-A complex subunit Abraxas,CCDC98,Coiled-coil domain-containing protein 98,FAM175A,Homo sapiens,Human,Protein FAM175A,UNQ496_PRO1013
EIAAB46890 CCDC131,Coiled-coil domain-containing protein 131,Homo sapiens,Human,KIAA0546,Proline_serine-rich coiled-coil protein 2,PSRC2,ZFC3H1,Zinc finger C3H1 domain-containing protein
EIAAB06031 Ccdc86,Coiled-coil domain-containing protein 86,Cyclon,Cytokine-induced protein with coiled-coil domain,D19Ertd678e,mCyclon,MNCb-4327,Mouse,Mus musculus
EIAAB05828 C6orf184,C6orf185,CCDC162,CCDC162P,Coiled-coil domain-containing protein 162,Coiled-coil domain-containing protein 162 pseudogene,Homo sapiens,Human
EIAAB06030 CCDC86,Coiled-coil domain-containing protein 86,CYCLON,Cytokine-induced protein with coiled-coil domain,Homo sapiens,Human
EIAAB06029 Ccdc86,Coiled-coil domain-containing protein 86,Cyclon,Cytokine-induced protein with coiled-coil domain,Rat,Rattus norvegicus
EIAAB13842 ABRA1,BRCA1-A complex subunit Abraxas,CCDC98,Chicken,Coiled-coil domain-containing protein 98,FAM175A,Gallus gallus,Protein FAM175A,RCJMB04_33o10
EIAAB05061 Calcium-binding and coiled-coil domain-containing protein 1,Calcoco1,CocoA,Coiled-coil coactivator protein,Kiaa1536,Mouse,Mus musculus
EIAAB05058 Calcium-binding and coiled-coil domain-containing protein 1,CALCOCO1,Calphoglin,Coiled-coil coactivator protein,Homo sapiens,Human,KIAA1536,PP13275,Sarcoma antigen NY-SAR-3,UNQ2436_PRO4996
EIAAB05742 Ccdc115,Ccp1,Coiled-coil domain-containing protein 115,Coiled-coil protein 1,Mouse,Mus musculus
EIAAB07114 AAG10,Aging-associated gene 10 protein,C7orf17,CHCHD2,Coiled-coil-helix-coiled-coil-helix domain-containing protein 2, mitochondrial,HCV NS2 trans-regulated protein,Homo sapiens,Human,NS2TP
EIAAB07113 C10orf34,CHCHD1,Coiled-coil-helix-coiled-coil-helix domain-containing protein 1,Homo sapiens,Human,Nuclear protein C2360
EIAAB11296 CCD1,Coiled-coil protein DIX1,Coiled-coil-DIX1,DIX domain-containing protein 1,DIXDC1,Dixin,Homo sapiens,Human,KIAA1735
EIAAB07111 C22orf16,CHCHD10,Coiled-coil-helix-coiled-coil-helix domain-containing protein 10, mitochondrial,Homo sapiens,Human,Protein N27C7-4
EIAAB07126 CHCHD8,Coiled-coil-helix-coiled-coil-helix domain-containing protein 8,E2IG2,E2-induced gene 2 protein,Homo sapiens,Human
EIAAB11295 Ccd1,Coiled-coil protein DIX1,Coiled-coil-DIX1,DIX domain-containing protein 1,Dixdc1,Dixin,Kiaa1735,Mouse,Mus musculus
CSB-EL005324HU Human Putative coiled-coil-helix-coiled-coil-helix domain-containing protein CHCHD2P9, mitochondrial(CHCHD9) ELISA kit SpeciesHuman 96T
EIAAB05910 Ccdc30,Coiled-coil domain-containing protein 30,Mouse,Mus musculus,Pfdn6l,Prefoldin subunit 6-like protein


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur