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Slit homolog 3 protein (Slit-3) (Multiple epidermal growth factor-like domains protein 5) (Multiple EGF-like domains protein 5)
SLIT3_HUMAN Reviewed; 1523 AA.
O75094; A6H8U9; J3KNP3; O95804; Q9UFH5;
15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
02-NOV-2010, sequence version 3.
28-MAR-2018, entry version 165.
RecName: Full=Slit homolog 3 protein;
Short=Slit-3;
AltName: Full=Multiple epidermal growth factor-like domains protein 5;
Short=Multiple EGF-like domains protein 5;
Flags: Precursor;
Name=SLIT3; Synonyms=KIAA0814, MEGF5, SLIL2; ORFNames=UNQ691/PRO1336;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), TISSUE SPECIFICITY,
AND VARIANT ALA-371.
PubMed=9813312; DOI=10.1016/S0169-328X(98)00224-1;
Itoh A., Miyabayashi T., Ohno M., Sakano S.;
"Cloning and expressions of three mammalian homologues of Drosophila
slit suggest possible roles for Slit in the formation and maintenance
of the nervous system.";
Brain Res. Mol. Brain Res. 62:175-186(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT ALA-371.
TISSUE=Brain;
PubMed=9693030; DOI=10.1006/geno.1998.5341;
Nakayama M., Nakajima D., Nagase T., Nomura N., Seki N., Ohara O.;
"Identification of high-molecular-weight proteins with multiple EGF-
like motifs by motif-trap screening.";
Genomics 51:27-34(1998).
[3]
SEQUENCE REVISION.
Nakayama M., Nakajima D., Nagase T., Nomura N., Seki N., Ohara O.;
Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS
ALA-371 AND SER-618.
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).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15372022; DOI=10.1038/nature02919;
Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T.,
Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M.,
Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K.,
Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C.,
Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M.,
Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A.,
Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M.,
Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M.,
Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S.,
Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
"The DNA sequence and comparative analysis of human chromosome 5.";
Nature 431:268-274(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
ALA-371.
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).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 337-657, AND VARIANT
ALA-371.
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).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 574-1523 (ISOFORM 2).
PubMed=10349621; DOI=10.1016/S0925-4773(98)00174-9;
Holmes G.P., Negus K., Burridge L., Raman S., Algar E., Yamada T.,
Little M.H.;
"Distinct but overlapping expression patterns of two vertebrate slit
homologs implies functional roles in CNS development and
organogenesis.";
Mech. Dev. 79:57-72(1998).
-!- FUNCTION: May act as molecular guidance cue in cellular migration,
and function may be mediated by interaction with roundabout
homolog receptors.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1;
IsoId=O75094-1; Sequence=Displayed;
Name=2;
IsoId=O75094-2; Sequence=VSP_009714;
Name=3;
IsoId=O75094-3; Sequence=VSP_009715;
Name=4;
IsoId=O75094-4; Sequence=VSP_054798;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Predominantly expressed in thyroid.
{ECO:0000269|PubMed:9813312}.
-!- SEQUENCE CAUTION:
Sequence=BAA32466.2; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=CAB59249.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/SLIT3ID50515ch5q34.html";
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EMBL; AB017169; BAA35186.1; -; mRNA.
EMBL; AB011538; BAA32466.2; ALT_INIT; mRNA.
EMBL; AY358884; AAQ89243.1; -; mRNA.
EMBL; AC008409; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC008479; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC011365; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC011389; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC027311; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC094081; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC112165; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC146759; AAI46760.1; -; mRNA.
EMBL; AL122074; CAB59249.1; ALT_SEQ; mRNA.
EMBL; AF075240; AAD19336.1; -; mRNA.
CCDS; CCDS4369.1; -. [O75094-1]
CCDS; CCDS64311.1; -. [O75094-4]
PIR; T34555; T34555.
RefSeq; NP_001258875.1; NM_001271946.1.
RefSeq; NP_003053.1; NM_003062.3.
UniGene; Hs.552087; -.
ProteinModelPortal; O75094; -.
BioGrid; 112473; 2.
IntAct; O75094; 4.
STRING; 9606.ENSP00000430333; -.
iPTMnet; O75094; -.
PhosphoSitePlus; O75094; -.
MaxQB; O75094; -.
PaxDb; O75094; -.
PeptideAtlas; O75094; -.
PRIDE; O75094; -.
Ensembl; ENST00000332966; ENSP00000332164; ENSG00000184347. [O75094-4]
Ensembl; ENST00000519560; ENSP00000430333; ENSG00000184347. [O75094-1]
GeneID; 6586; -.
KEGG; hsa:6586; -.
UCSC; uc003mab.5; human. [O75094-1]
CTD; 6586; -.
DisGeNET; 6586; -.
EuPathDB; HostDB:ENSG00000184347.14; -.
GeneCards; SLIT3; -.
H-InvDB; HIX0005394; -.
HGNC; HGNC:11087; SLIT3.
HPA; HPA051630; -.
MIM; 603745; gene.
neXtProt; NX_O75094; -.
OpenTargets; ENSG00000184347; -.
PharmGKB; PA35940; -.
eggNOG; KOG4237; Eukaryota.
eggNOG; COG4886; LUCA.
GeneTree; ENSGT00910000144018; -.
HOGENOM; HOG000116120; -.
HOVERGEN; HBG057959; -.
InParanoid; O75094; -.
KO; K06850; -.
OMA; CPGPHSE; -.
OrthoDB; EOG091G0MHP; -.
PhylomeDB; O75094; -.
TreeFam; TF332887; -.
Reactome; R-HSA-373752; Netrin-1 signaling.
Reactome; R-HSA-376176; Signaling by ROBO receptors.
Reactome; R-HSA-428542; Regulation of commissural axon pathfinding by SLIT and ROBO.
ChiTaRS; SLIT3; human.
GeneWiki; SLIT3; -.
GenomeRNAi; 6586; -.
PRO; PR:O75094; -.
Proteomes; UP000005640; Chromosome 5.
Bgee; ENSG00000184347; -.
CleanEx; HS_SLIT3; -.
ExpressionAtlas; O75094; baseline and differential.
Genevisible; O75094; HS.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:0005739; C:mitochondrion; NAS:UniProtKB.
GO; GO:0005509; F:calcium ion binding; NAS:UniProtKB.
GO; GO:0048495; F:Roundabout binding; IPI:UniProtKB.
GO; GO:0009887; P:animal organ morphogenesis; IEA:Ensembl.
GO; GO:0061364; P:apoptotic process involved in luteolysis; IEP:UniProtKB.
GO; GO:0048846; P:axon extension involved in axon guidance; IDA:UniProtKB.
GO; GO:0007411; P:axon guidance; IDA:UniProtKB.
GO; GO:0032870; P:cellular response to hormone stimulus; IEP:UniProtKB.
GO; GO:0050919; P:negative chemotaxis; IDA:UniProtKB.
GO; GO:0030308; P:negative regulation of cell growth; IMP:BHF-UCL.
GO; GO:0008285; P:negative regulation of cell proliferation; IEA:Ensembl.
GO; GO:0070100; P:negative regulation of chemokine-mediated signaling pathway; IMP:BHF-UCL.
GO; GO:0010629; P:negative regulation of gene expression; IEA:Ensembl.
GO; GO:0051414; P:response to cortisol; IEP:UniProtKB.
GO; GO:0035385; P:Roundabout signaling pathway; IMP:BHF-UCL.
Gene3D; 3.80.10.10; -; 5.
InterPro; IPR013320; ConA-like_dom_sf.
InterPro; IPR000483; Cys-rich_flank_reg_C.
InterPro; IPR006207; Cys_knot_C.
InterPro; IPR001881; EGF-like_Ca-bd_dom.
InterPro; IPR013032; EGF-like_CS.
InterPro; IPR000742; EGF-like_dom.
InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
InterPro; IPR018097; EGF_Ca-bd_CS.
InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
InterPro; IPR001791; Laminin_G.
InterPro; IPR001611; Leu-rich_rpt.
InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
InterPro; IPR032675; LRR_dom_sf.
InterPro; IPR000372; LRRNT.
Pfam; PF00008; EGF; 6.
Pfam; PF02210; Laminin_G_2; 1.
Pfam; PF13855; LRR_8; 5.
Pfam; PF01463; LRRCT; 4.
Pfam; PF01462; LRRNT; 3.
SMART; SM00041; CT; 1.
SMART; SM00181; EGF; 9.
SMART; SM00179; EGF_CA; 9.
SMART; SM00282; LamG; 1.
SMART; SM00369; LRR_TYP; 18.
SMART; SM00082; LRRCT; 4.
SMART; SM00013; LRRNT; 4.
SUPFAM; SSF49899; SSF49899; 1.
SUPFAM; SSF57184; SSF57184; 1.
PROSITE; PS01185; CTCK_1; 1.
PROSITE; PS01225; CTCK_2; 1.
PROSITE; PS00022; EGF_1; 9.
PROSITE; PS01186; EGF_2; 7.
PROSITE; PS50026; EGF_3; 9.
PROSITE; PS01187; EGF_CA; 2.
PROSITE; PS50025; LAM_G_DOMAIN; 1.
PROSITE; PS51450; LRR; 20.
2: Evidence at transcript level;
Alternative splicing; Complete proteome; Developmental protein;
Differentiation; Disulfide bond; EGF-like domain; Glycoprotein;
Leucine-rich repeat; Neurogenesis; Polymorphism; Reference proteome;
Repeat; Secreted; Signal.
SIGNAL 1 33 {ECO:0000255}.
CHAIN 34 1523 Slit homolog 3 protein.
/FTId=PRO_0000007732.
DOMAIN 34 61 LRRNT.
REPEAT 62 83 LRR 1.
REPEAT 86 107 LRR 2.
REPEAT 110 131 LRR 3.
REPEAT 134 155 LRR 4.
REPEAT 158 179 LRR 5.
REPEAT 182 203 LRR 6.
DOMAIN 215 265 LRRCT 1.
DOMAIN 271 307 LRRNT 2.
REPEAT 308 329 LRR 7.
REPEAT 332 353 LRR 8.
REPEAT 356 377 LRR 9.
REPEAT 380 401 LRR 10.
REPEAT 404 425 LRR 11.
DOMAIN 437 487 LRRCT 2.
DOMAIN 496 532 LRRNT 3.
REPEAT 533 554 LRR 12.
REPEAT 558 579 LRR 13.
REPEAT 582 603 LRR 14.
REPEAT 606 627 LRR 15.
REPEAT 630 651 LRR 16.
DOMAIN 663 713 LRRCT 3.
DOMAIN 716 752 LRRNT 4.
REPEAT 753 775 LRR 17.
REPEAT 776 797 LRR 18.
REPEAT 800 821 LRR 19.
REPEAT 824 845 LRR 20.
DOMAIN 857 907 LRRCT 4.
DOMAIN 918 953 EGF-like 1. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 955 994 EGF-like 2. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 996 1032 EGF-like 3. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 1034 1072 EGF-like 4. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 1074 1110 EGF-like 5. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 1119 1155 EGF-like 6. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 1158 1332 Laminin G-like. {ECO:0000255|PROSITE-
ProRule:PRU00122}.
DOMAIN 1340 1365 EGF-like 7. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 1368 1403 EGF-like 8. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 1408 1444 EGF-like 9. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 1449 1523 CTCK. {ECO:0000255|PROSITE-
ProRule:PRU00039}.
CARBOHYD 72 72 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 192 192 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 563 563 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 622 622 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 784 784 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 792 792 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 797 797 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 928 928 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1008 1008 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1025 1025 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1181 1181 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1247 1247 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1406 1406 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 284 293 {ECO:0000250}.
DISULFID 441 464 {ECO:0000250}.
DISULFID 443 485 {ECO:0000250}.
DISULFID 505 511 {ECO:0000250}.
DISULFID 509 518 {ECO:0000250}.
DISULFID 667 690 {ECO:0000250}.
DISULFID 669 711 {ECO:0000250}.
DISULFID 920 931 {ECO:0000250}.
DISULFID 925 941 {ECO:0000250}.
DISULFID 943 952 {ECO:0000250}.
DISULFID 959 970 {ECO:0000250}.
DISULFID 964 982 {ECO:0000250}.
DISULFID 984 993 {ECO:0000250}.
DISULFID 1000 1011 {ECO:0000250}.
DISULFID 1005 1020 {ECO:0000250}.
DISULFID 1022 1031 {ECO:0000250}.
DISULFID 1038 1051 {ECO:0000250}.
DISULFID 1045 1060 {ECO:0000250}.
DISULFID 1062 1071 {ECO:0000250}.
DISULFID 1078 1089 {ECO:0000250}.
DISULFID 1083 1098 {ECO:0000250}.
DISULFID 1100 1109 {ECO:0000250}.
DISULFID 1123 1134 {ECO:0000250}.
DISULFID 1128 1143 {ECO:0000250}.
DISULFID 1145 1154 {ECO:0000250}.
DISULFID 1305 1332 {ECO:0000250}.
DISULFID 1355 1364 {ECO:0000250}.
DISULFID 1372 1382 {ECO:0000250}.
DISULFID 1377 1391 {ECO:0000250}.
DISULFID 1393 1402 {ECO:0000250}.
DISULFID 1412 1422 {ECO:0000250}.
DISULFID 1417 1432 {ECO:0000250}.
DISULFID 1434 1443 {ECO:0000250}.
DISULFID 1449 1487 {ECO:0000250}.
DISULFID 1467 1501 {ECO:0000250}.
DISULFID 1478 1517 {ECO:0000250}.
DISULFID 1482 1519 {ECO:0000250}.
VAR_SEQ 906 906 K -> KVLWFCCP (in isoform 4).
{ECO:0000305}.
/FTId=VSP_054798.
VAR_SEQ 1117 1216 Missing (in isoform 2).
{ECO:0000303|PubMed:10349621,
ECO:0000303|PubMed:9813312}.
/FTId=VSP_009714.
VAR_SEQ 1446 1523 ENPCLGQVVREVIRRQKGYASCATASKVPIMECRGGCGPQC
CQPTRSKRRKYVFQCTDGSSFVEEVERHLECGCLACS ->
VFRAQVFQSSLPGNCSWSCWPPRPPMP (in isoform
3). {ECO:0000303|PubMed:9813312}.
/FTId=VSP_009715.
VARIANT 371 371 V -> A (in dbSNP:rs891921).
{ECO:0000269|PubMed:12975309,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:17974005,
ECO:0000269|PubMed:9693030,
ECO:0000269|PubMed:9813312}.
/FTId=VAR_049004.
VARIANT 395 395 R -> Q (in dbSNP:rs2288792).
/FTId=VAR_021905.
VARIANT 618 618 G -> S (in dbSNP:rs10036727).
{ECO:0000269|PubMed:12975309}.
/FTId=VAR_024265.
VARIANT 810 810 R -> Q (in dbSNP:rs36052924).
/FTId=VAR_049005.
VARIANT 994 994 E -> G (in dbSNP:rs2305993).
/FTId=VAR_020168.
VARIANT 1064 1064 P -> A (in dbSNP:rs10072243).
/FTId=VAR_049006.
SEQUENCE 1523 AA; 167713 MW; CEB00887F6908554 CRC64;
MAPGWAGVGA AVRARLALAL ALASVLSGPP AVACPTKCTC SAASVDCHGL GLRAVPRGIP
RNAERLDLDR NNITRITKMD FAGLKNLRVL HLEDNQVSVI ERGAFQDLKQ LERLRLNKNK
LQVLPELLFQ STPKLTRLDL SENQIQGIPR KAFRGITDVK NLQLDNNHIS CIEDGAFRAL
RDLEILTLNN NNISRILVTS FNHMPKIRTL RLHSNHLYCD CHLAWLSDWL RQRRTVGQFT
LCMAPVHLRG FNVADVQKKE YVCPAPHSEP PSCNANSISC PSPCTCSNNI VDCRGKGLME
IPANLPEGIV EIRLEQNSIK AIPAGAFTQY KKLKRIDISK NQISDIAPDA FQGLKSLTSL
VLYGNKITEI VKGLFDGLVS LQLLLLNANK INCLRVNTFQ DLQNLNLLSL YDNKLQTISK
GLFAPLQSIQ TLHLAQNPFV CDCHLKWLAD YLQDNPIETS GARCSSPRRL ANKRISQIKS
KKFRCSGSED YRSRFSSECF MDLVCPEKCR CEGTIVDCSN QKLVRIPSHL PEYVTDLRLN
DNEVSVLEAT GIFKKLPNLR KINLSNNKIK EVREGAFDGA ASVQELMLTG NQLETVHGRV
FRGLSGLKTL MLRSNLIGCV SNDTFAGLSS VRLLSLYDNR ITTITPGAFT TLVSLSTINL
LSNPFNCNCH LAWLGKWLRK RRIVSGNPRC QKPFFLKEIP IQDVAIQDFT CDGNEESSCQ
LSPRCPEQCT CMETVVRCSN KGLRALPRGM PKDVTELYLE GNHLTAVPRE LSALRHLTLI
DLSNNSISML TNYTFSNMSH LSTLILSYNR LRCIPVHAFN GLRSLRVLTL HGNDISSVPE
GSFNDLTSLS HLALGTNPLH CDCSLRWLSE WVKAGYKEPG IARCSSPEPM ADRLLLTTPT
HRFQCKGPVD INIVAKCNAC LSSPCKNNGT CTQDPVELYR CACPYSYKGK DCTVPINTCI
QNPCQHGGTC HLSDSHKDGF SCSCPLGFEG QRCEINPDDC EDNDCENNAT CVDGINNYVC
ICPPNYTGEL CDEVIDHCVP ELNLCQHEAK CIPLDKGFSC ECVPGYSGKL CETDNDDCVA
HKCRHGAQCV DTINGYTCTC PQGFSGPFCE HPPPMVLLQT SPCDQYECQN GAQCIVVQQE
PTCRCPPGFA GPRCEKLITV NFVGKDSYVE LASAKVRPQA NISLQVATDK DNGILLYKGD
NDPLALELYQ GHVRLVYDSL SSPPTTVYSV ETVNDGQFHS VELVTLNQTL NLVVDKGTPK
SLGKLQKQPA VGINSPLYLG GIPTSTGLSA LRQGTDRPLG GFHGCIHEVR INNELQDFKA
LPPQSLGVSP GCKSCTVCKH GLCRSVEKDS VVCECRPGWT GPLCDQEARD PCLGHRCHHG
KCVATGTSYM CKCAEGYGGD LCDNKNDSAN ACSAFKCHHG QCHISDQGEP YCLCQPGFSG
EHCQQENPCL GQVVREVIRR QKGYASCATA SKVPIMECRG GCGPQCCQPT RSKRRKYVFQ
CTDGSSFVEE VERHLECGCL ACS
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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
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BIC: FINVBGSF
GENTAUR Poland Sp. z o.o.
ul. Grunwaldzka 88/A m.2
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TEL Gdansk 058 710 33 44 FAX 058 710 33 48
poland@gentaur.com | Gentaur
Other countries
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Canada Montreal +15149077481
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Ireland Dublin+35316526556
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Norge Oslo+4721031366
Sverige Stockholm+46852503438
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US New York+17185132983
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italia@gentaur.com | Gentaur
Pathways :
WP1049: G Protein Signaling Pathways
WP1165: G Protein Signaling Pathways
WP1371: G Protein Signaling Pathways
WP1438: Influenza A virus infection
WP1493: Carbon assimilation C4 pathway
WP1502: Mitochondrial biogenesis
WP1531: Vitamin D synthesis
WP1566: Citrate cycle (TCA cycle)
WP1613: 1,4-Dichlorobenzene degradation
WP1616: ABC transporters
WP1624: Bacterial secretion system
WP1625: Base excision repair
WP1644: DNA replication
WP1650: Fluorobenzoate degradation
WP1654: gamma-Hexachlorocyclohexane degradation
WP1657: Glycerolipid metabolism
WP1659: Glycine, serine and threonine metabolism
WP1661: Glyoxylate and dicarboxylate metabolism
WP1663: Homologous recombination
WP1665: Limonene and pinene degradation
WP1672: Mismatch repair
WP1673: Naphthalene and anthracene degradation
WP1675: Nitrogen metabolism
WP1676: Non-homologous end-joining
WP1678: Nucleotide excision repair
Related Genes :
[SLIT2 SLIL3] Slit homolog 2 protein (Slit-2) [Cleaved into: Slit homolog 2 protein N-product; Slit homolog 2 protein C-product]
[Slit2] Slit homolog 2 protein (Slit-2) [Cleaved into: Slit homolog 2 protein N-product; Slit homolog 2 protein C-product]
[SLIT1 KIAA0813 MEGF4 SLIL1] Slit homolog 1 protein (Slit-1) (Multiple epidermal growth factor-like domains protein 4) (Multiple EGF-like domains protein 4)
[sli CG43758] Protein slit (dSlit) [Cleaved into: Protein slit N-product; Protein slit C-product]
[Slit1 Kiaa0813] Slit homolog 1 protein (Slit-1)
[SLIT3 KIAA0814 MEGF5 SLIL2 UNQ691/PRO1336] Slit homolog 3 protein (Slit-3) (Multiple epidermal growth factor-like domains protein 5) (Multiple EGF-like domains protein 5)
[Slit1 Megf4] Slit homolog 1 protein (Slit-1) (Multiple epidermal growth factor-like domains protein 4) (Multiple EGF-like domains protein 4)
[Slit2] Slit homolog 2 protein (Slit-2) (Fragment)
[Slit3] Slit homolog 3 protein (Slit-3) (Slit3)
[Slit3 Megf5] Slit homolog 3 protein (Slit-3) (Multiple epidermal growth factor-like domains protein 5) (Multiple EGF-like domains protein 5)
[SRGAP1 ARHGAP13 KIAA1304] SLIT-ROBO Rho GTPase-activating protein 1 (srGAP1) (Rho GTPase-activating protein 13)
[SRGAP2 ARHGAP34 FNBP2 KIAA0456 SRGAP2A] SLIT-ROBO Rho GTPase-activating protein 2 (srGAP2) (Formin-binding protein 2) (Rho GTPase-activating protein 34)
[SLIT2] Slit guidance ligand 2
[SLIT2] Slit guidance ligand 2
[Slit2] Slit homolog 2 protein
[Srgap2 Fbp27 Fnbp2] SLIT-ROBO Rho GTPase-activating protein 2 (srGAP2) (Formin-binding protein 2) (Formin-binding protein 27) (FBP-27)
[SRGAP3 ARHGAP14 KIAA0411 KIAA1156 MEGAP SRGAP2] SLIT-ROBO Rho GTPase-activating protein 3 (srGAP3) (Mental disorder-associated GAP) (Rho GTPase-activating protein 14) (WAVE-associated Rac GTPase-activating protein) (WRP)
[Slit2] Slit homolog 2 protein
[Srgap2] SLIT-ROBO Rho GTPase-activating protein 2 (srGAP2)
[SLIT2] Slit guidance ligand 2
[SRGAP2C SRGAP2P1] SLIT-ROBO Rho GTPase-activating protein 2C (SLIT-ROBO Rho GTPase activating protein 2 pseudogene 1)
[slt-1 F40E10.4] Slit homolog 1 protein (Slt-1)
[Slitrk5] SLIT and NTRK-like protein 5
[SLITRK6] SLIT and NTRK-like protein 6
[SLITRK1 KIAA1910 LRRC12 UNQ233/PRO266] SLIT and NTRK-like protein 1 (Leucine-rich repeat-containing protein 12)
[Slitrk2] SLIT and NTRK-like protein 2
[Slitrk1 Sltk1] SLIT and NTRK-like protein 1
[Slitrk6 Sltk6] SLIT and NTRK-like protein 6
[SLIT2] Slit guidance ligand 2
[SLITRK2 CXorf2 KIAA1854 SLITL1 UNQ9197/PRO34756] SLIT and NTRK-like protein 2
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