Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Slit homolog 2 protein

Gene

SLIT2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Thought to act as molecular guidance cue in cellular migration, and function appears to be mediated by interaction with roundabout homolog receptors. During neural development involved in axonal navigation at the ventral midline of the neural tube and projection of axons to different regions. SLIT1 and SLIT2 seem to be essential for midline guidance in the forebrain by acting as repulsive signal preventing inappropriate midline crossing by axons projecting from the olfactory bulb. In spinal chord development may play a role in guiding commissural axons once they reached the floor plate by modulating the response to netrin. In vitro, silences the attractive effect of NTN1 but not its growth-stimulatory effect and silencing requires the formation of a ROBO1-DCC complex. May be implicated in spinal chord midline post-crossing axon repulsion. In vitro, only commissural axons that crossed the midline responded to SLIT2. In the developing visual system appears to function as repellent for retinal ganglion axons by providing a repulsion that directs these axons along their appropriate paths prior to, and after passage through, the optic chiasm. In vitro, collapses and repels retinal ganglion cell growth cones. Seems to play a role in branching and arborization of CNS sensory axons, and in neuronal cell migration. In vitro, Slit homolog 2 protein N-product, but not Slit homolog 2 protein C-product, repels olfactory bulb (OB) but not dorsal root ganglia (DRG) axons, induces OB growth cones collapse and induces branching of DRG axons. Seems to be involved in regulating leukocyte migration.6 Publications

GO - Molecular functioni

  • calcium ion binding Source: UniProtKB
  • GTPase inhibitor activity Source: UniProtKB
  • heparin binding Source: UniProtKB
  • laminin-1 binding Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB
  • proteoglycan binding Source: UniProtKB
  • Roundabout binding Source: UniProtKB

GO - Biological processi

  • apoptotic process involved in luteolysis Source: UniProtKB
  • axon extension involved in axon guidance Source: UniProtKB
  • axon guidance Source: UniProtKB
  • branching morphogenesis of an epithelial tube Source: UniProtKB
  • cell migration involved in sprouting angiogenesis Source: BHF-UCL
  • cellular response to heparin Source: UniProtKB
  • cellular response to hormone stimulus Source: UniProtKB
  • chemorepulsion involved in postnatal olfactory bulb interneuron migration Source: UniProtKB
  • corticospinal neuron axon guidance through spinal cord Source: BHF-UCL
  • induction of negative chemotaxis Source: UniProtKB
  • motor neuron axon guidance Source: UniProtKB
  • negative chemotaxis Source: UniProtKB
  • negative regulation of actin filament polymerization Source: UniProtKB
  • negative regulation of cell growth Source: BHF-UCL
  • negative regulation of cell migration Source: UniProtKB
  • negative regulation of cellular response to growth factor stimulus Source: BHF-UCL
  • negative regulation of chemokine-mediated signaling pathway Source: BHF-UCL
  • negative regulation of endothelial cell migration Source: UniProtKB
  • negative regulation of lamellipodium assembly Source: UniProtKB
  • negative regulation of leukocyte chemotaxis Source: UniProtKB
  • negative regulation of monocyte chemotaxis Source: BHF-UCL
  • negative regulation of mononuclear cell migration Source: BHF-UCL
  • negative regulation of neutrophil chemotaxis Source: UniProtKB
  • negative regulation of protein phosphorylation Source: UniProtKB
  • negative regulation of retinal ganglion cell axon guidance Source: UniProtKB
  • negative regulation of small GTPase mediated signal transduction Source: UniProtKB
  • negative regulation of smooth muscle cell chemotaxis Source: BHF-UCL
  • negative regulation of smooth muscle cell migration Source: BHF-UCL
  • negative regulation of vascular permeability Source: UniProtKB
  • positive regulation of apoptotic process Source: UniProtKB
  • positive regulation of axonogenesis Source: UniProtKB
  • response to cortisol Source: UniProtKB
  • retinal ganglion cell axon guidance Source: UniProtKB
  • Roundabout signaling pathway Source: BHF-UCL
  • ureteric bud development Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Chemotaxis, Differentiation, Neurogenesis

Keywords - Ligandi

Heparin-binding

Enzyme and pathway databases

ReactomeiR-HSA-373752. Netrin-1 signaling.
R-HSA-376176. Signaling by Robo receptor.
R-HSA-428540. Activation of Rac.
R-HSA-428542. Regulation of Commissural axon pathfinding by Slit and Robo.
R-HSA-428543. Inactivation of Cdc42 and Rac.
R-HSA-428890. Role of Abl in Robo-Slit signaling.
SIGNORiO94813.

Names & Taxonomyi

Protein namesi
Recommended name:
Slit homolog 2 protein
Short name:
Slit-2
Cleaved into the following 2 chains:
Gene namesi
Name:SLIT2
Synonyms:SLIL3
OrganismiHomo sapiens (Human)Imported
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 4

Organism-specific databases

HGNCiHGNC:11086. SLIT2.

Subcellular locationi

  • Secreted 1 Publication

  • Note: The C-terminal cleavage protein is more diffusible than the larger N-terminal protein that is more tightly cell associated.

GO - Cellular componenti

  • cell surface Source: UniProtKB
  • cytoplasm Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • extracellular region Source: Reactome
  • extracellular space Source: UniProtKB
  • membrane Source: UniProtKB
  • plasma membrane Source: Reactome
  • proteinaceous extracellular matrix Source: GO_Central
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Organism-specific databases

DisGeNETi9353.
OpenTargetsiENSG00000145147.
PharmGKBiPA35939.

Polymorphism and mutation databases

BioMutaiSLIT2.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 30Sequence analysisAdd BLAST30
ChainiPRO_000000772531 – 1529Slit homolog 2 proteinAdd BLAST1499
ChainiPRO_000000772631 – 1121Slit homolog 2 protein N-productAdd BLAST1091
ChainiPRO_00000077271122 – 1529Slit homolog 2 protein C-productAdd BLAST408

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi66N-linked (GlcNAc...)Sequence analysis1
Glycosylationi186N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi277 ↔ 286
Disulfide bondi434 ↔ 457
Disulfide bondi436 ↔ 478
Disulfide bondi506 ↔ 512
Disulfide bondi510 ↔ 519
Glycosylationi564N-linked (GlcNAc...)Sequence analysis1
Glycosylationi623N-linked (GlcNAc...)1
Disulfide bondi668 ↔ 691
Disulfide bondi670 ↔ 712
Disulfide bondi727 ↔ 733
Disulfide bondi731 ↔ 740
Glycosylationi794N-linked (GlcNAc...)Sequence analysis1
Glycosylationi799N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi863 ↔ 886
Disulfide bondi865 ↔ 907
Disulfide bondi922 ↔ 933By similarity
Disulfide bondi927 ↔ 943By similarity
Disulfide bondi945 ↔ 954By similarity
Disulfide bondi961 ↔ 972By similarity
Disulfide bondi966 ↔ 984By similarity
Disulfide bondi986 ↔ 995By similarity
Disulfide bondi1002 ↔ 1013By similarity
Disulfide bondi1007 ↔ 1022By similarity
Glycosylationi1009N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1010N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1019N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1024 ↔ 1033By similarity
Disulfide bondi1040 ↔ 1053By similarity
Disulfide bondi1047 ↔ 1062By similarity
Disulfide bondi1064 ↔ 1073By similarity
Disulfide bondi1080 ↔ 1091By similarity
Disulfide bondi1085 ↔ 1100By similarity
Disulfide bondi1102 ↔ 1111By similarity
Disulfide bondi1125 ↔ 1136By similarity
Disulfide bondi1130 ↔ 1145By similarity
Disulfide bondi1147 ↔ 1156By similarity
Glycosylationi1183N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1266N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1300N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1307 ↔ 1333By similarity
Disulfide bondi1336 ↔ 1346By similarity
Disulfide bondi1341 ↔ 1356By similarity
Disulfide bondi1358 ↔ 1367By similarity
Disulfide bondi1375 ↔ 1385By similarity
Disulfide bondi1380 ↔ 1395By similarity
Disulfide bondi1397 ↔ 1406By similarity
Disulfide bondi1416 ↔ 1426By similarity
Disulfide bondi1421 ↔ 1436By similarity
Disulfide bondi1438 ↔ 1447By similarity
Disulfide bondi1453 ↔ 1492By similarity
Disulfide bondi1471 ↔ 1506By similarity
Disulfide bondi1482 ↔ 1522By similarity
Disulfide bondi1486 ↔ 1524By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei1121 – 1122Cleavage2

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiO94813.
PaxDbiO94813.
PeptideAtlasiO94813.
PRIDEiO94813.

PTM databases

iPTMnetiO94813.
PhosphoSitePlusiO94813.

Expressioni

Tissue specificityi

Fetal lung and kidney, and adult spinal cord. Weak expression in adult adrenal gland, thyroid, trachea and other tissues examined.2 Publications

Gene expression databases

BgeeiENSG00000145147.
CleanExiHS_SLIT2.
ExpressionAtlasiO94813. baseline and differential.
GenevisibleiO94813. HS.

Organism-specific databases

HPAiCAB007590.
HPA019511.
HPA023088.

Interactioni

Subunit structurei

Interacts with GREM1 (By similarity). Homodimer. Binds ROBO1 and ROBO2 with high affinity.By similarity4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself2EBI-1236865,EBI-1236865

GO - Molecular functioni

  • laminin-1 binding Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB
  • Roundabout binding Source: UniProtKB

Protein-protein interaction databases

BioGridi114756. 11 interactors.
DIPiDIP-38198N.
IntActiO94813. 8 interactors.
MINTiMINT-6768470.
STRINGi9606.ENSP00000422591.

Structurei

Secondary structure

11529
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi277 – 280Combined sources4
Beta strandi283 – 285Combined sources3
Beta strandi304 – 306Combined sources3
Turni317 – 322Combined sources6
Beta strandi328 – 330Combined sources3
Turni341 – 346Combined sources6
Beta strandi352 – 354Combined sources3
Turni365 – 370Combined sources6
Beta strandi376 – 378Combined sources3
Turni389 – 394Combined sources6
Beta strandi400 – 402Combined sources3
Turni413 – 418Combined sources6
Beta strandi424 – 426Combined sources3
Helixi436 – 438Combined sources3
Helixi439 – 447Combined sources9
Beta strandi456 – 460Combined sources5
Helixi461 – 463Combined sources3
Helixi468 – 470Combined sources3
Helixi473 – 475Combined sources3
Beta strandi511 – 513Combined sources3
Beta strandi516 – 518Combined sources3
Beta strandi536 – 539Combined sources4
Helixi554 – 556Combined sources3
Beta strandi562 – 564Combined sources3
Turni575 – 580Combined sources6
Beta strandi586 – 588Combined sources3
Helixi599 – 602Combined sources4
Beta strandi610 – 612Combined sources3
Beta strandi633 – 636Combined sources4
Turni647 – 652Combined sources6
Beta strandi658 – 660Combined sources3
Helixi670 – 672Combined sources3
Helixi673 – 681Combined sources9
Beta strandi690 – 694Combined sources5
Helixi695 – 697Combined sources3
Helixi702 – 704Combined sources3
Helixi707 – 709Combined sources3
Beta strandi732 – 734Combined sources3
Beta strandi737 – 739Combined sources3
Beta strandi758 – 760Combined sources3
Helixi771 – 775Combined sources5
Beta strandi781 – 783Combined sources3
Turni794 – 799Combined sources6
Beta strandi805 – 807Combined sources3
Turni818 – 823Combined sources6
Beta strandi829 – 831Combined sources3
Turni842 – 847Combined sources6
Beta strandi853 – 855Combined sources3
Helixi865 – 867Combined sources3
Helixi868 – 876Combined sources9
Beta strandi885 – 889Combined sources5
Helixi890 – 892Combined sources3
Turni897 – 899Combined sources3
Helixi902 – 904Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2V70X-ray3.01A/B/C/D504-714[»]
2V9SX-ray2.00A/B/C/D271-480[»]
2V9TX-ray1.70B271-479[»]
2WFHX-ray1.80A/B726-907[»]
ProteinModelPortaliO94813.
SMRiO94813.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO94813.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini31 – 55LRRNTAdd BLAST25
Repeati56 – 77LRR 1Add BLAST22
Repeati80 – 101LRR 2Add BLAST22
Repeati104 – 125LRR 3Add BLAST22
Repeati128 – 149LRR 4Add BLAST22
Repeati152 – 173LRR 5Add BLAST22
Repeati176 – 197LRR 6Add BLAST22
Domaini209 – 259LRRCT 1Add BLAST51
Domaini264 – 300LRRNT 2Add BLAST37
Repeati301 – 322LRR 7Add BLAST22
Repeati325 – 346LRR 8Add BLAST22
Repeati349 – 370LRR 9Add BLAST22
Repeati373 – 394LRR 10Add BLAST22
Repeati397 – 418LRR 11Add BLAST22
Domaini430 – 480LRRCT 2Add BLAST51
Domaini497 – 533LRRNT 3Add BLAST37
Repeati534 – 555LRR 12Add BLAST22
Repeati559 – 580LRR 13Add BLAST22
Repeati583 – 604LRR 14Add BLAST22
Repeati607 – 628LRR 15Add BLAST22
Repeati631 – 652LRR 16Add BLAST22
Domaini664 – 714LRRCT 3Add BLAST51
Domaini718 – 754LRRNT 4Add BLAST37
Repeati755 – 777LRR 17Add BLAST23
Repeati778 – 799LRR 18Add BLAST22
Repeati802 – 823LRR 19Add BLAST22
Repeati826 – 847LRR 20Add BLAST22
Domaini859 – 909LRRCT 4Add BLAST51
Domaini918 – 955EGF-like 1PROSITE-ProRule annotationAdd BLAST38
Domaini957 – 996EGF-like 2PROSITE-ProRule annotationAdd BLAST40
Domaini998 – 1034EGF-like 3; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini1036 – 1074EGF-like 4PROSITE-ProRule annotationAdd BLAST39
Domaini1076 – 1112EGF-like 5; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini1121 – 1157EGF-like 6PROSITE-ProRule annotationAdd BLAST37
Domaini1160 – 1333Laminin G-likePROSITE-ProRule annotationAdd BLAST174
Domaini1332 – 1368EGF-like 7PROSITE-ProRule annotationAdd BLAST37
Domaini1453 – 1528CTCKPROSITE-ProRule annotationCuratedAdd BLAST76

Domaini

The leucine-rich repeat domain is sufficient for guiding both axon projection and neuronal migration, in vitro.1 Publication

Sequence similaritiesi

Contains 1 CTCK (C-terminal cystine knot-like) domain.PROSITE-ProRule annotation
Contains 7 EGF-like domains.PROSITE-ProRule annotationCurated
Contains 1 laminin G-like domain.PROSITE-ProRule annotation
Contains 20 LRR (leucine-rich) repeats.Curated
Contains 4 LRRCT domains.Curated
Contains 4 LRRNT domains.Curated

Keywords - Domaini

EGF-like domain, Leucine-rich repeat, Repeat, Signal

Phylogenomic databases

eggNOGiKOG4237. Eukaryota.
COG4886. LUCA.
GeneTreeiENSGT00840000129708.
HOGENOMiHOG000116120.
HOVERGENiHBG057959.
InParanoidiO94813.
KOiK06839.
PhylomeDBiO94813.
TreeFamiTF332887.

Family and domain databases

Gene3Di2.60.120.200. 1 hit.
3.80.10.10. 6 hits.
InterProiIPR013320. ConA-like_dom.
IPR000483. Cys-rich_flank_reg_C.
IPR006207. Cys_knot_C.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR003645. Fol_N.
IPR032675. L_dom-like.
IPR001791. Laminin_G.
IPR001611. Leu-rich_rpt.
IPR003591. Leu-rich_rpt_typical-subtyp.
IPR000372. LRRNT.
[Graphical view]
PfamiPF00008. EGF. 5 hits.
PF12661. hEGF. 2 hits.
PF00054. Laminin_G_1. 1 hit.
PF13855. LRR_8. 7 hits.
PF01463. LRRCT. 4 hits.
PF01462. LRRNT. 4 hits.
[Graphical view]
SMARTiSM00041. CT. 1 hit.
SM00181. EGF. 9 hits.
SM00179. EGF_CA. 7 hits.
SM00274. FOLN. 3 hits.
SM00282. LamG. 1 hit.
SM00369. LRR_TYP. 17 hits.
SM00082. LRRCT. 4 hits.
SM00013. LRRNT. 4 hits.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 1 hit.
SSF52058. SSF52058. 4 hits.
PROSITEiPS00010. ASX_HYDROXYL. 2 hits.
PS01185. CTCK_1. 1 hit.
PS01225. CTCK_2. 1 hit.
PS00022. EGF_1. 9 hits.
PS01186. EGF_2. 7 hits.
PS50026. EGF_3. 9 hits.
PS01187. EGF_CA. 2 hits.
PS50025. LAM_G_DOMAIN. 1 hit.
PS51450. LRR. 20 hits.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1Curated (identifier: O94813-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MRGVGWQMLS LSLGLVLAIL NKVAPQACPA QCSCSGSTVD CHGLALRSVP
60 70 80 90 100
RNIPRNTERL DLNGNNITRI TKTDFAGLRH LRVLQLMENK ISTIERGAFQ
110 120 130 140 150
DLKELERLRL NRNHLQLFPE LLFLGTAKLY RLDLSENQIQ AIPRKAFRGA
160 170 180 190 200
VDIKNLQLDY NQISCIEDGA FRALRDLEVL TLNNNNITRL SVASFNHMPK
210 220 230 240 250
LRTFRLHSNN LYCDCHLAWL SDWLRQRPRV GLYTQCMGPS HLRGHNVAEV
260 270 280 290 300
QKREFVCSGH QSFMAPSCSV LHCPAACTCS NNIVDCRGKG LTEIPTNLPE
310 320 330 340 350
TITEIRLEQN TIKVIPPGAF SPYKKLRRID LSNNQISELA PDAFQGLRSL
360 370 380 390 400
NSLVLYGNKI TELPKSLFEG LFSLQLLLLN ANKINCLRVD AFQDLHNLNL
410 420 430 440 450
LSLYDNKLQT IAKGTFSPLR AIQTMHLAQN PFICDCHLKW LADYLHTNPI
460 470 480 490 500
ETSGARCTSP RRLANKRIGQ IKSKKFRCSA KEQYFIPGTE DYRSKLSGDC
510 520 530 540 550
FADLACPEKC RCEGTTVDCS NQKLNKIPEH IPQYTAELRL NNNEFTVLEA
560 570 580 590 600
TGIFKKLPQL RKINFSNNKI TDIEEGAFEG ASGVNEILLT SNRLENVQHK
610 620 630 640 650
MFKGLESLKT LMLRSNRITC VGNDSFIGLS SVRLLSLYDN QITTVAPGAF
660 670 680 690 700
DTLHSLSTLN LLANPFNCNC YLAWLGEWLR KKRIVTGNPR CQKPYFLKEI
710 720 730 740 750
PIQDVAIQDF TCDDGNDDNS CSPLSRCPTE CTCLDTVVRC SNKGLKVLPK
760 770 780 790 800
GIPRDVTELY LDGNQFTLVP KELSNYKHLT LIDLSNNRIS TLSNQSFSNM
810 820 830 840 850
TQLLTLILSY NRLRCIPPRT FDGLKSLRLL SLHGNDISVV PEGAFNDLSA
860 870 880 890 900
LSHLAIGANP LYCDCNMQWL SDWVKSEYKE PGIARCAGPG EMADKLLLTT
910 920 930 940 950
PSKKFTCQGP VDVNILAKCN PCLSNPCKND GTCNSDPVDF YRCTCPYGFK
960 970 980 990 1000
GQDCDVPIHA CISNPCKHGG TCHLKEGEED GFWCICADGF EGENCEVNVD
1010 1020 1030 1040 1050
DCEDNDCENN STCVDGINNY TCLCPPEYTG ELCEEKLDFC AQDLNPCQHD
1060 1070 1080 1090 1100
SKCILTPKGF KCDCTPGYVG EHCDIDFDDC QDNKCKNGAH CTDAVNGYTC
1110 1120 1130 1140 1150
ICPEGYSGLF CEFSPPMVLP RTSPCDNFDC QNGAQCIVRI NEPICQCLPG
1160 1170 1180 1190 1200
YQGEKCEKLV SVNFINKESY LQIPSAKVRP QTNITLQIAT DEDSGILLYK
1210 1220 1230 1240 1250
GDKDHIAVEL YRGRVRASYD TGSHPASAIY SVETINDGNF HIVELLALDQ
1260 1270 1280 1290 1300
SLSLSVDGGN PKIITNLSKQ STLNFDSPLY VGGMPGKSNV ASLRQAPGQN
1310 1320 1330 1340 1350
GTSFHGCIRN LYINSELQDF QKVPMQTGIL PGCEPCHKKV CAHGTCQPSS
1360 1370 1380 1390 1400
QAGFTCECQE GWMGPLCDQR TNDPCLGNKC VHGTCLPINA FSYSCKCLEG
1410 1420 1430 1440 1450
HGGVLCDEEE DLFNPCQAIK CKHGKCRLSG LGQPYCECSS GYTGDSCDRE
1460 1470 1480 1490 1500
ISCRGERIRD YYQKQQGYAA CQTTKKVSRL ECRGGCAGGQ CCGPLRSKRR
1510 1520
KYSFECTDGS SFVDEVEKVV KCGCTRCVS
Length:1,529
Mass (Da):169,870
Last modified:May 1, 1999 - v1
Checksum:i5D19CC5E7FD461BA
GO
Isoform 2Curated (identifier: O94813-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     258-258: S → SDEEE
     480-487: Missing.

Show »
Length:1,525
Mass (Da):169,395
Checksum:i56DE2356BB2E5CAD
GO
Isoform 3Curated (identifier: O94813-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     480-487: Missing.

Show »
Length:1,521
Mass (Da):168,893
Checksum:i7620F3C96DD4E534
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti226Q → K in AAD25539 (PubMed:10349621).Curated1
Sequence conflicti607 – 610SLKT → KPQN in AAD04309 (PubMed:10102268).Curated4
Sequence conflicti634L → M in AAD04309 (PubMed:10102268).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_018098636S → P.1 Publication1
Natural variantiVAR_0180991277S → F.1 PublicationCorresponds to variant rs771375896dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_050035258S → SDEEE in isoform 2. 2 Publications1
Alternative sequenceiVSP_050036480 – 487Missing in isoform 2 and isoform 3. 4 Publications8

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB017168 mRNA. Translation: BAA35185.1.
AF055585 mRNA. Translation: AAD04309.1.
AF133270 mRNA. Translation: AAD25539.1.
AC021118 Genomic DNA. No translation available.
AC092577 Genomic DNA. No translation available.
AC096718 Genomic DNA. No translation available.
AC108011 Genomic DNA. No translation available.
CH471069 Genomic DNA. Translation: EAW92793.1.
BC117190 mRNA. Translation: AAI17191.1.
BC143978 mRNA. Translation: AAI43979.1.
CCDSiCCDS3426.1. [O94813-1]
CCDS75110.1. [O94813-2]
CCDS75111.1. [O94813-3]
RefSeqiNP_001276064.1. NM_001289135.2. [O94813-2]
NP_001276065.1. NM_001289136.2. [O94813-3]
NP_004778.1. NM_004787.3. [O94813-1]
UniGeneiHs.29802.

Genome annotation databases

EnsembliENST00000503823; ENSP00000427548; ENSG00000145147. [O94813-3]
ENST00000503837; ENSP00000422261; ENSG00000145147. [O94813-2]
ENST00000504154; ENSP00000422591; ENSG00000145147. [O94813-1]
GeneIDi9353.
KEGGihsa:9353.
UCSCiuc003gpr.3. human. [O94813-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB017168 mRNA. Translation: BAA35185.1.
AF055585 mRNA. Translation: AAD04309.1.
AF133270 mRNA. Translation: AAD25539.1.
AC021118 Genomic DNA. No translation available.
AC092577 Genomic DNA. No translation available.
AC096718 Genomic DNA. No translation available.
AC108011 Genomic DNA. No translation available.
CH471069 Genomic DNA. Translation: EAW92793.1.
BC117190 mRNA. Translation: AAI17191.1.
BC143978 mRNA. Translation: AAI43979.1.
CCDSiCCDS3426.1. [O94813-1]
CCDS75110.1. [O94813-2]
CCDS75111.1. [O94813-3]
RefSeqiNP_001276064.1. NM_001289135.2. [O94813-2]
NP_001276065.1. NM_001289136.2. [O94813-3]
NP_004778.1. NM_004787.3. [O94813-1]
UniGeneiHs.29802.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2V70X-ray3.01A/B/C/D504-714[»]
2V9SX-ray2.00A/B/C/D271-480[»]
2V9TX-ray1.70B271-479[»]
2WFHX-ray1.80A/B726-907[»]
ProteinModelPortaliO94813.
SMRiO94813.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114756. 11 interactors.
DIPiDIP-38198N.
IntActiO94813. 8 interactors.
MINTiMINT-6768470.
STRINGi9606.ENSP00000422591.

PTM databases

iPTMnetiO94813.
PhosphoSitePlusiO94813.

Polymorphism and mutation databases

BioMutaiSLIT2.

Proteomic databases

MaxQBiO94813.
PaxDbiO94813.
PeptideAtlasiO94813.
PRIDEiO94813.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000503823; ENSP00000427548; ENSG00000145147. [O94813-3]
ENST00000503837; ENSP00000422261; ENSG00000145147. [O94813-2]
ENST00000504154; ENSP00000422591; ENSG00000145147. [O94813-1]
GeneIDi9353.
KEGGihsa:9353.
UCSCiuc003gpr.3. human. [O94813-1]

Organism-specific databases

CTDi9353.
DisGeNETi9353.
GeneCardsiSLIT2.
HGNCiHGNC:11086. SLIT2.
HPAiCAB007590.
HPA019511.
HPA023088.
MIMi603746. gene.
neXtProtiNX_O94813.
OpenTargetsiENSG00000145147.
PharmGKBiPA35939.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4237. Eukaryota.
COG4886. LUCA.
GeneTreeiENSGT00840000129708.
HOGENOMiHOG000116120.
HOVERGENiHBG057959.
InParanoidiO94813.
KOiK06839.
PhylomeDBiO94813.
TreeFamiTF332887.

Enzyme and pathway databases

ReactomeiR-HSA-373752. Netrin-1 signaling.
R-HSA-376176. Signaling by Robo receptor.
R-HSA-428540. Activation of Rac.
R-HSA-428542. Regulation of Commissural axon pathfinding by Slit and Robo.
R-HSA-428543. Inactivation of Cdc42 and Rac.
R-HSA-428890. Role of Abl in Robo-Slit signaling.
SIGNORiO94813.

Miscellaneous databases

ChiTaRSiSLIT2. human.
EvolutionaryTraceiO94813.
GeneWikiiSLIT2.
GenomeRNAii9353.
PROiO94813.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000145147.
CleanExiHS_SLIT2.
ExpressionAtlasiO94813. baseline and differential.
GenevisibleiO94813. HS.

Family and domain databases

Gene3Di2.60.120.200. 1 hit.
3.80.10.10. 6 hits.
InterProiIPR013320. ConA-like_dom.
IPR000483. Cys-rich_flank_reg_C.
IPR006207. Cys_knot_C.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR003645. Fol_N.
IPR032675. L_dom-like.
IPR001791. Laminin_G.
IPR001611. Leu-rich_rpt.
IPR003591. Leu-rich_rpt_typical-subtyp.
IPR000372. LRRNT.
[Graphical view]
PfamiPF00008. EGF. 5 hits.
PF12661. hEGF. 2 hits.
PF00054. Laminin_G_1. 1 hit.
PF13855. LRR_8. 7 hits.
PF01463. LRRCT. 4 hits.
PF01462. LRRNT. 4 hits.
[Graphical view]
SMARTiSM00041. CT. 1 hit.
SM00181. EGF. 9 hits.
SM00179. EGF_CA. 7 hits.
SM00274. FOLN. 3 hits.
SM00282. LamG. 1 hit.
SM00369. LRR_TYP. 17 hits.
SM00082. LRRCT. 4 hits.
SM00013. LRRNT. 4 hits.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 1 hit.
SSF52058. SSF52058. 4 hits.
PROSITEiPS00010. ASX_HYDROXYL. 2 hits.
PS01185. CTCK_1. 1 hit.
PS01225. CTCK_2. 1 hit.
PS00022. EGF_1. 9 hits.
PS01186. EGF_2. 7 hits.
PS50026. EGF_3. 9 hits.
PS01187. EGF_CA. 2 hits.
PS50025. LAM_G_DOMAIN. 1 hit.
PS51450. LRR. 20 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiSLIT2_HUMAN
AccessioniPrimary (citable) accession number: O94813
Secondary accession number(s): A0A0A6YYB8
, B7ZLR5, O95710, Q17RU3, Q9Y5Q7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2003
Last sequence update: May 1, 1999
Last modified: November 2, 2016
This is version 170 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 4
    Human chromosome 4: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.