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Sex comb on midleg-like protein 2

 SCML2_HUMAN             Reviewed;         700 AA.
Q9UQR0; Q5JXE6; Q86U98; Q8IWD0; Q8NDP2; Q9UGC5;
10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
27-SEP-2017, entry version 150.
RecName: Full=Sex comb on midleg-like protein 2;
Name=SCML2;
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), AND TISSUE SPECIFICITY.
PubMed=10331946; DOI=10.1006/geno.1999.5755;
Montini E., Buchner G., Spalluto C., Andolfi G., Caruso A.,
de Dunnen J.T., Trump D., Rocchi M., Ballabio A., Franco B.;
"Identification of SCML2, a second human gene homologous to the
Drosophila Sex comb on midleg (Scm): a new gene cluster on Xp22.";
Genomics 58:65-72(1999).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Testis;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15772651; DOI=10.1038/nature03440;
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A.,
Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G.,
Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S.,
Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R.,
Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L.,
Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A.,
Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S.,
Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R.,
Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M.,
Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N.,
Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D.,
Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W.,
Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C.,
Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C.,
Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
Corby N., Connor R.E., David R., Davies J., Davis C., Davis J.,
Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S.,
Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I.,
Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L.,
Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P.,
Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S.,
Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A.,
Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J.,
Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J.,
Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S.,
de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z.,
Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C.,
Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W.,
Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T.,
Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I.,
Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N.,
Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J.,
Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E.,
Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S.,
Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T.,
Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S.,
Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L.,
Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A.,
Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L.,
Williams G., Williams L., Williamson A., Williamson H., Wilming L.,
Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H.,
Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A.,
Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A.,
Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T.,
Gibbs R.A., Beck S., Rogers J., Bentley D.R.;
"The DNA sequence of the human X chromosome.";
Nature 434:325-337(2005).
[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=Testis, 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]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic kidney;
PubMed=17525332; DOI=10.1126/science.1140321;
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
"ATM and ATR substrate analysis reveals extensive protein networks
responsive to DNA damage.";
Science 316:1160-1166(2007).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-256; SER-267; SER-299;
SER-300; THR-305; SER-499; THR-503; SER-511; SER-583; SER-590 AND
SER-594, 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).
[8]
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).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-499; SER-511 AND
SER-590, 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).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-499; THR-503; SER-511
AND SER-590, 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).
[11]
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).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-499; SER-511 AND
SER-590, 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).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-256; SER-261; SER-267;
SER-499; SER-511; SER-522; SER-570; SER-583 AND SER-590, 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).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-590, 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).
[15]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-536, 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).
[16]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-518; LYS-536; LYS-599 AND
LYS-605, 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).
[17]
X-RAY CRYSTALLOGRAPHY (1.78 ANGSTROMS) OF 33-243.
PubMed=12952983; DOI=10.1074/jbc.M306469200;
Sathyamurthy A., Allen M.D., Murzin A.G., Bycroft M.;
"Crystal structure of the malignant brain tumor (MBT) repeats in sex
comb on midleg-like 2 (SCML2).";
J. Biol. Chem. 278:46968-46973(2003).
-!- FUNCTION: Putative Polycomb group (PcG) protein. PcG proteins act
by forming multiprotein complexes, which are required to maintain
the transcriptionally repressive state of homeotic genes
throughout development (By similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9UQR0-1; Sequence=Displayed;
Name=2;
IsoId=Q9UQR0-2; Sequence=VSP_010277;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Highly expressed in placenta, thymus and
testis. Detected at lower levels in brain, liver, skeletal muscle,
pancreas and ovary. {ECO:0000269|PubMed:10331946}.
-!- SIMILARITY: Belongs to the SCM family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAH51913.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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EMBL; Y18004; CAB38943.1; -; mRNA.
EMBL; AL833937; CAD38792.1; -; mRNA.
EMBL; AL096763; CAI42221.1; -; Genomic_DNA.
EMBL; AL031007; CAI42221.1; JOINED; Genomic_DNA.
EMBL; Z93023; CAI42221.1; JOINED; Genomic_DNA.
EMBL; AL031007; CAI43048.1; -; Genomic_DNA.
EMBL; AL096763; CAI43048.1; JOINED; Genomic_DNA.
EMBL; Z93023; CAI43048.1; JOINED; Genomic_DNA.
EMBL; Z93023; CAI43176.1; -; Genomic_DNA.
EMBL; AL031007; CAI43176.1; JOINED; Genomic_DNA.
EMBL; AL096763; CAI43176.1; JOINED; Genomic_DNA.
EMBL; BC040497; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; CH471074; EAW98937.1; -; Genomic_DNA.
EMBL; BC051913; AAH51913.1; ALT_INIT; mRNA.
EMBL; BC064617; AAH64617.1; -; mRNA.
CCDS; CCDS14185.1; -. [Q9UQR0-1]
RefSeq; NP_006080.1; NM_006089.2. [Q9UQR0-1]
RefSeq; XP_016884708.1; XM_017029219.1. [Q9UQR0-1]
RefSeq; XP_016884709.1; XM_017029220.1. [Q9UQR0-1]
UniGene; Hs.495774; -.
PDB; 1OI1; X-ray; 1.78 A; A=24-243.
PDB; 2BIV; X-ray; 1.70 A; A/B/C=1-243.
PDB; 2MEM; NMR; -; A=354-468.
PDB; 2VYT; X-ray; 1.90 A; A/B=24-243.
PDB; 4EDU; X-ray; 2.58 A; A=29-243.
PDBsum; 1OI1; -.
PDBsum; 2BIV; -.
PDBsum; 2MEM; -.
PDBsum; 2VYT; -.
PDBsum; 4EDU; -.
ProteinModelPortal; Q9UQR0; -.
SMR; Q9UQR0; -.
BioGrid; 115661; 12.
DIP; DIP-53760N; -.
IntAct; Q9UQR0; 10.
STRING; 9606.ENSP00000251900; -.
iPTMnet; Q9UQR0; -.
PhosphoSitePlus; Q9UQR0; -.
BioMuta; SCML2; -.
DMDM; 47117338; -.
EPD; Q9UQR0; -.
PaxDb; Q9UQR0; -.
PeptideAtlas; Q9UQR0; -.
PRIDE; Q9UQR0; -.
Ensembl; ENST00000251900; ENSP00000251900; ENSG00000102098. [Q9UQR0-1]
Ensembl; ENST00000398048; ENSP00000381126; ENSG00000102098. [Q9UQR0-2]
GeneID; 10389; -.
KEGG; hsa:10389; -.
UCSC; uc004cyl.3; human. [Q9UQR0-1]
CTD; 10389; -.
DisGeNET; 10389; -.
EuPathDB; HostDB:ENSG00000102098.17; -.
GeneCards; SCML2; -.
HGNC; HGNC:10581; SCML2.
HPA; HPA001662; -.
HPA; HPA064713; -.
MIM; 300208; gene.
neXtProt; NX_Q9UQR0; -.
OpenTargets; ENSG00000102098; -.
PharmGKB; PA34999; -.
eggNOG; ENOG410IMEZ; Eukaryota.
eggNOG; ENOG410XPKI; LUCA.
GeneTree; ENSGT00760000119024; -.
HOGENOM; HOG000236280; -.
HOVERGEN; HBG056406; -.
InParanoid; Q9UQR0; -.
KO; K11465; -.
OMA; PPLGYQM; -.
OrthoDB; EOG091G05BW; -.
PhylomeDB; Q9UQR0; -.
TreeFam; TF106488; -.
ChiTaRS; SCML2; human.
EvolutionaryTrace; Q9UQR0; -.
GenomeRNAi; 10389; -.
PRO; PR:Q9UQR0; -.
Proteomes; UP000005640; Chromosome X.
Bgee; ENSG00000102098; -.
CleanEx; HS_SCML2; -.
ExpressionAtlas; Q9UQR0; baseline and differential.
Genevisible; Q9UQR0; HS.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0031519; C:PcG protein complex; IDA:UniProtKB.
GO; GO:0003677; F:DNA binding; TAS:ProtInc.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; TAS:ProtInc.
GO; GO:0009653; P:anatomical structure morphogenesis; TAS:ProtInc.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
InterPro; IPR004092; Mbt.
InterPro; IPR001660; SAM.
InterPro; IPR013761; SAM/pointed.
InterPro; IPR033763; SCML2_RBR.
InterPro; IPR021987; SLED.
Pfam; PF02820; MBT; 2.
Pfam; PF17208; RBR; 1.
Pfam; PF00536; SAM_1; 1.
Pfam; PF12140; SLED; 1.
SMART; SM00561; MBT; 2.
SMART; SM00454; SAM; 1.
SUPFAM; SSF47769; SSF47769; 1.
PROSITE; PS51079; MBT; 2.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome;
Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome; Repeat;
Repressor; Transcription; Transcription regulation; Ubl conjugation.
CHAIN 1 700 Sex comb on midleg-like protein 2.
/FTId=PRO_0000097628.
REPEAT 33 131 MBT 1.
REPEAT 139 240 MBT 2.
DOMAIN 631 700 SAM.
MOD_RES 256 256 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 261 261 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 267 267 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 299 299 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 300 300 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 305 305 Phosphothreonine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 499 499 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 503 503 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231}.
MOD_RES 511 511 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 522 522 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 570 570 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 583 583 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 590 590 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 594 594 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
CROSSLNK 518 518 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 536 536 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:28112733}.
CROSSLNK 599 599 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 605 605 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VAR_SEQ 1 562 Missing (in isoform 2).
{ECO:0000303|PubMed:17974005}.
/FTId=VSP_010277.
HELIX 35 42 {ECO:0000244|PDB:2BIV}.
HELIX 49 51 {ECO:0000244|PDB:2BIV}.
STRAND 52 54 {ECO:0000244|PDB:2BIV}.
STRAND 68 73 {ECO:0000244|PDB:2BIV}.
STRAND 76 89 {ECO:0000244|PDB:2BIV}.
STRAND 92 97 {ECO:0000244|PDB:2BIV}.
STRAND 102 104 {ECO:0000244|PDB:2BIV}.
STRAND 106 109 {ECO:0000244|PDB:2BIV}.
STRAND 115 117 {ECO:0000244|PDB:4EDU}.
HELIX 120 123 {ECO:0000244|PDB:2BIV}.
HELIX 138 140 {ECO:0000244|PDB:2BIV}.
HELIX 141 149 {ECO:0000244|PDB:2BIV}.
HELIX 157 159 {ECO:0000244|PDB:2BIV}.
STRAND 177 181 {ECO:0000244|PDB:2BIV}.
STRAND 189 198 {ECO:0000244|PDB:2BIV}.
STRAND 201 206 {ECO:0000244|PDB:2BIV}.
HELIX 211 213 {ECO:0000244|PDB:2BIV}.
STRAND 215 218 {ECO:0000244|PDB:2BIV}.
HELIX 229 233 {ECO:0000244|PDB:2BIV}.
STRAND 356 359 {ECO:0000244|PDB:2MEM}.
STRAND 369 371 {ECO:0000244|PDB:2MEM}.
HELIX 373 378 {ECO:0000244|PDB:2MEM}.
STRAND 383 387 {ECO:0000244|PDB:2MEM}.
HELIX 388 402 {ECO:0000244|PDB:2MEM}.
HELIX 406 409 {ECO:0000244|PDB:2MEM}.
STRAND 422 427 {ECO:0000244|PDB:2MEM}.
STRAND 430 435 {ECO:0000244|PDB:2MEM}.
HELIX 442 455 {ECO:0000244|PDB:2MEM}.
SEQUENCE 700 AA; 77257 MW; 05E086D4928DEE73 CRC64;
MGQTVNEDSM DVKKENQEKT PQSSTSSVQR DDFHWEEYLK ETGSISAPSE CFRQSQIPPV
NDFKVGMKLE ARDPRNATSV CIATVIGITG ARLRLRLDGS DNRNDFWRLV DSPDIQPVGT
CEKEGDLLQP PLGYQMNTSS WPMFLLKTLN GSEMASATLF KKEPPKPPLN NFKVGMKLEA
IDKKNPYLIC PATIGDVKGD EVHITFDGWS GAFDYWCKYD SRDIFPAGWC RLTGDVLQPP
GTSVPIVKNI AKTESSPSEA SQHSMQSPQK TTLILPTQQV RRSSRIKPPG PTAVPKRSSS
VKNITPRKKG PNSGKKEKPL PVICSTSAAS LKSLTRDRGM LYKDVASGPC KIVMSTVCVY
VNKHGNFGPH LDPKRIQQLP DHFGPGPVNV VLRRIVQACV DCALETKTVF GYLKPDNRGG
EVITASFDGE THSIQLPPVN SASFALRFLE NFCHSLQCDN LLSSQPFSSS RGHTHSSAEH
DKNQSAKEDV TERQSTKRSP QQTVPYVVPL SPKLPKTKEY ASEGEPLFAG GSAIPKEENL
SEDSKSSSLN SGNYLNPACR NPMYIHTSVS QDFSRSVPGT TSSPLVGDIS PKSSPHEVKF
QMQRKSEAPS YIAVPDPSVL KQGFSKDPST WSVDEVIQFM KHTDPQISGP LADLFRQHEI
DGKALFLLKS DVMMKYMGLK LGPALKLCYY IEKLKEGKYS


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