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O94813

- SLIT2_HUMAN

UniProt

O94813 - SLIT2_HUMAN

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Protein

Slit homolog 2 protein

Gene

SLIT2

Organism
Homo sapiens (Human)
Status
Reviewed - 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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei1121 – 11222Cleavage

GO - Molecular functioni

  1. calcium ion binding Source: UniProtKB
  2. chemorepellent activity Source: Ensembl
  3. GTPase inhibitor activity Source: UniProtKB
  4. heparin binding Source: UniProtKB
  5. identical protein binding Source: IntAct
  6. laminin-1 binding Source: UniProtKB
  7. protein homodimerization activity Source: UniProtKB
  8. proteoglycan binding Source: UniProtKB
  9. Roundabout binding Source: UniProtKB

GO - Biological processi

  1. apoptotic process involved in luteolysis Source: UniProtKB
  2. axon extension involved in axon guidance Source: UniProtKB
  3. axon guidance Source: UniProtKB
  4. branching morphogenesis of an epithelial tube Source: UniProtKB
  5. cell migration involved in sprouting angiogenesis Source: BHF-UCL
  6. cellular response to heparin Source: UniProtKB
  7. cellular response to hormone stimulus Source: UniProtKB
  8. chemorepulsion involved in postnatal olfactory bulb interneuron migration Source: UniProtKB
  9. corticospinal neuron axon guidance through spinal cord Source: BHF-UCL
  10. dorsal/ventral axon guidance Source: Ensembl
  11. induction of negative chemotaxis Source: UniProtKB
  12. in utero embryonic development Source: Ensembl
  13. mammary duct terminal end bud growth Source: Ensembl
  14. metanephros development Source: Ensembl
  15. motor neuron axon guidance Source: UniProtKB
  16. negative chemotaxis Source: UniProtKB
  17. negative regulation of actin filament polymerization Source: UniProtKB
  18. negative regulation of axon extension Source: Ensembl
  19. negative regulation of catalytic activity Source: GOC
  20. negative regulation of cell growth Source: BHF-UCL
  21. negative regulation of cell migration Source: UniProtKB
  22. negative regulation of cell proliferation Source: Ensembl
  23. negative regulation of cellular response to growth factor stimulus Source: BHF-UCL
  24. negative regulation of chemokine-mediated signaling pathway Source: BHF-UCL
  25. negative regulation of endothelial cell migration Source: UniProtKB
  26. negative regulation of gene expression Source: Ensembl
  27. negative regulation of lamellipodium assembly Source: UniProtKB
  28. negative regulation of leukocyte chemotaxis Source: UniProtKB
  29. negative regulation of monocyte chemotaxis Source: BHF-UCL
  30. negative regulation of mononuclear cell migration Source: BHF-UCL
  31. negative regulation of neutrophil chemotaxis Source: UniProtKB
  32. negative regulation of protein phosphorylation Source: UniProtKB
  33. negative regulation of retinal ganglion cell axon guidance Source: UniProtKB
  34. negative regulation of small GTPase mediated signal transduction Source: UniProtKB
  35. negative regulation of smooth muscle cell chemotaxis Source: BHF-UCL
  36. negative regulation of smooth muscle cell migration Source: BHF-UCL
  37. negative regulation of vascular permeability Source: UniProtKB
  38. positive regulation of apoptotic process Source: UniProtKB
  39. positive regulation of axonogenesis Source: UniProtKB
  40. response to cortisol Source: UniProtKB
  41. retinal ganglion cell axon guidance Source: UniProtKB
  42. Roundabout signaling pathway Source: BHF-UCL
  43. single organismal cell-cell adhesion Source: Ensembl
  44. 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

ReactomeiREACT_19226. Activation of Rac.
REACT_19230. Role of Abl in Robo-Slit signaling.
REACT_19342. Inactivation of Cdc42 and Rac.
REACT_19351. Signaling by Robo receptor.
REACT_19376. Regulation of Commissural axon pathfinding by Slit and Robo.
REACT_22237. Netrin-1 signaling.

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
ProteomesiUP000005640: 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

  1. cell surface Source: UniProtKB
  2. cytoplasm Source: UniProtKB
  3. extracellular region Source: Reactome
  4. extracellular space Source: UniProtKB
  5. extracellular vesicular exosome Source: UniProt
  6. membrane Source: UniProtKB
  7. plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA35939.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3030Sequence AnalysisAdd
BLAST
Chaini31 – 15291499Slit homolog 2 proteinPRO_0000007725Add
BLAST
Chaini31 – 11211091Slit homolog 2 protein N-productPRO_0000007726Add
BLAST
Chaini1122 – 1529408Slit homolog 2 protein C-productPRO_0000007727Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi66 – 661N-linked (GlcNAc...)Sequence Analysis
Glycosylationi186 – 1861N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi277 ↔ 286
Disulfide bondi434 ↔ 457
Disulfide bondi436 ↔ 478
Disulfide bondi506 ↔ 512
Disulfide bondi510 ↔ 519
Glycosylationi564 – 5641N-linked (GlcNAc...)Sequence Analysis
Glycosylationi623 – 6231N-linked (GlcNAc...)
Disulfide bondi668 ↔ 691
Disulfide bondi670 ↔ 712
Disulfide bondi727 ↔ 733
Disulfide bondi731 ↔ 740
Glycosylationi794 – 7941N-linked (GlcNAc...)Sequence Analysis
Glycosylationi799 – 7991N-linked (GlcNAc...)Sequence Analysis
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
Glycosylationi1009 – 10091N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1010 – 10101N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1019 – 10191N-linked (GlcNAc...)Sequence Analysis
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
Glycosylationi1183 – 11831N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1266 – 12661N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1300 – 13001N-linked (GlcNAc...)Sequence Analysis
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

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiO94813.
PaxDbiO94813.
PRIDEiO94813.

PTM databases

PhosphoSiteiO94813.

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

BgeeiO94813.
CleanExiHS_SLIT2.
ExpressionAtlasiO94813. baseline and differential.
GenevestigatoriO94813.

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

Protein-protein interaction databases

BioGridi114756. 7 interactions.
DIPiDIP-38198N.
IntActiO94813. 7 interactions.
MINTiMINT-6768470.
STRINGi9606.ENSP00000273739.

Structurei

Secondary structure

1
1529
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi277 – 2804
Beta strandi283 – 2853
Beta strandi304 – 3063
Turni317 – 3226
Beta strandi328 – 3303
Turni341 – 3466
Beta strandi352 – 3543
Turni365 – 3706
Beta strandi376 – 3783
Turni389 – 3946
Beta strandi400 – 4023
Turni413 – 4186
Beta strandi424 – 4263
Helixi436 – 4383
Helixi439 – 4479
Beta strandi456 – 4605
Helixi461 – 4633
Helixi468 – 4703
Helixi473 – 4753
Beta strandi511 – 5133
Beta strandi516 – 5183
Beta strandi536 – 5394
Helixi554 – 5563
Beta strandi562 – 5643
Turni575 – 5806
Beta strandi586 – 5883
Helixi599 – 6024
Beta strandi610 – 6123
Beta strandi633 – 6364
Turni647 – 6526
Beta strandi658 – 6603
Helixi670 – 6723
Helixi673 – 6819
Beta strandi690 – 6945
Helixi695 – 6973
Helixi702 – 7043
Helixi707 – 7093
Beta strandi732 – 7343
Beta strandi737 – 7393
Beta strandi758 – 7603
Helixi771 – 7755
Beta strandi781 – 7833
Turni794 – 7996
Beta strandi805 – 8073
Turni818 – 8236
Beta strandi829 – 8313
Turni842 – 8476
Beta strandi853 – 8553
Helixi865 – 8673
Helixi868 – 8769
Beta strandi885 – 8895
Helixi890 – 8923
Turni897 – 8993
Helixi902 – 9043

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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. Positions 25-1480.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO94813.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini31 – 5525LRRNTAdd
BLAST
Repeati56 – 7722LRR 1Add
BLAST
Repeati80 – 10122LRR 2Add
BLAST
Repeati104 – 12522LRR 3Add
BLAST
Repeati128 – 14922LRR 4Add
BLAST
Repeati152 – 17322LRR 5Add
BLAST
Repeati176 – 19722LRR 6Add
BLAST
Domaini209 – 25951LRRCT 1Add
BLAST
Domaini264 – 30037LRRNT 2Add
BLAST
Repeati301 – 32222LRR 7Add
BLAST
Repeati325 – 34622LRR 8Add
BLAST
Repeati349 – 37022LRR 9Add
BLAST
Repeati373 – 39422LRR 10Add
BLAST
Repeati397 – 41822LRR 11Add
BLAST
Domaini430 – 48051LRRCT 2Add
BLAST
Domaini497 – 53337LRRNT 3Add
BLAST
Repeati534 – 55522LRR 12Add
BLAST
Repeati559 – 58022LRR 13Add
BLAST
Repeati583 – 60422LRR 14Add
BLAST
Repeati607 – 62822LRR 15Add
BLAST
Repeati631 – 65222LRR 16Add
BLAST
Domaini664 – 71451LRRCT 3Add
BLAST
Domaini718 – 75437LRRNT 4Add
BLAST
Repeati755 – 77723LRR 17Add
BLAST
Repeati778 – 79922LRR 18Add
BLAST
Repeati802 – 82322LRR 19Add
BLAST
Repeati826 – 84722LRR 20Add
BLAST
Domaini859 – 90951LRRCT 4Add
BLAST
Domaini918 – 95538EGF-like 1PROSITE-ProRule annotationAdd
BLAST
Domaini957 – 99640EGF-like 2PROSITE-ProRule annotationAdd
BLAST
Domaini998 – 103437EGF-like 3; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1036 – 107439EGF-like 4PROSITE-ProRule annotationAdd
BLAST
Domaini1076 – 111237EGF-like 5; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1121 – 115737EGF-like 6PROSITE-ProRule annotationAdd
BLAST
Domaini1160 – 1333174Laminin G-likePROSITE-ProRule annotationAdd
BLAST
Domaini1332 – 136837EGF-like 7PROSITE-ProRule annotationAdd
BLAST
Domaini1453 – 152876CTCKCuratedPROSITE-ProRule annotationAdd
BLAST

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.CuratedPROSITE-ProRule annotation
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

eggNOGiCOG4886.
GeneTreeiENSGT00760000118811.
HOGENOMiHOG000116120.
HOVERGENiHBG057959.
InParanoidiO94813.
KOiK06839.
OrthoDBiEOG78WKQW.
PhylomeDBiO94813.
TreeFamiTF332887.

Family and domain databases

Gene3Di2.60.120.200. 1 hit.
InterProiIPR013320. ConA-like_dom.
IPR000483. Cys-rich_flank_reg_C.
IPR006207. Cys_knot_C.
IPR000742. EG-like_dom.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR003645. Fol_N.
IPR001791. Laminin_G.
IPR001611. Leu-rich_rpt.
IPR003591. Leu-rich_rpt_typical-subtyp.
IPR000372. LRR-contain_N.
[Graphical view]
PfamiPF00008. EGF. 6 hits.
PF02210. Laminin_G_2. 1 hit.
PF00560. LRR_1. 1 hit.
PF13855. LRR_8. 7 hits.
PF01463. LRRCT. 4 hits.
PF01462. LRRNT. 4 hits.
[Graphical view]
SMARTiSM00041. CT. 1 hit.
SM00181. EGF. 7 hits.
SM00179. EGF_CA. 2 hits.
SM00274. FOLN. 3 hits.
SM00282. LamG. 1 hit.
SM00369. LRR_TYP. 8 hits.
SM00082. LRRCT. 4 hits.
SM00013. LRRNT. 4 hits.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 1 hit.
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. Align

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti226 – 2261Q → K in AAD25539. (PubMed:10349621)Curated
Sequence conflicti607 – 6104SLKT → KPQN in AAD04309. (PubMed:10102268)Curated
Sequence conflicti634 – 6341L → M in AAD04309. (PubMed:10102268)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti636 – 6361S → P.1 Publication
VAR_018098
Natural varianti1277 – 12771S → F.1 Publication
VAR_018099

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei258 – 2581S → SDEEE in isoform 2. 2 PublicationsVSP_050035
Alternative sequencei480 – 4878Missing in isoform 2 and isoform 3. 4 PublicationsVSP_050036

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB017168 mRNA. Translation: BAA35185.1.
AF055585 mRNA. Translation: AAD04309.1.
AF133270 mRNA. Translation: AAD25539.1.
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_001289135.1. [O94813-2]
NP_001276065.1. NM_001289136.1. [O94813-3]
NP_004778.1. NM_004787.2. [O94813-1]
UniGeneiHs.29802.

Genome annotation databases

GeneIDi9353.
KEGGihsa:9353.
UCSCiuc003gpr.1. human. [O94813-1]
uc003gps.1. human. [O94813-3]

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:
EMBL
GenBank
DDBJ
Links Updated
AB017168 mRNA. Translation: BAA35185.1 .
AF055585 mRNA. Translation: AAD04309.1 .
AF133270 mRNA. Translation: AAD25539.1 .
CH471069 Genomic DNA. Translation: EAW92793.1 .
BC117190 mRNA. Translation: AAI17191.1 .
BC143978 mRNA. Translation: AAI43979.1 .
CCDSi CCDS3426.1. [O94813-1 ]
CCDS75110.1. [O94813-2 ]
CCDS75111.1. [O94813-3 ]
RefSeqi NP_001276064.1. NM_001289135.1. [O94813-2 ]
NP_001276065.1. NM_001289136.1. [O94813-3 ]
NP_004778.1. NM_004787.2. [O94813-1 ]
UniGenei Hs.29802.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2V70 X-ray 3.01 A/B/C/D 504-714 [» ]
2V9S X-ray 2.00 A/B/C/D 271-480 [» ]
2V9T X-ray 1.70 B 271-479 [» ]
2WFH X-ray 1.80 A/B 726-907 [» ]
ProteinModelPortali O94813.
SMRi O94813. Positions 25-1480.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 114756. 7 interactions.
DIPi DIP-38198N.
IntActi O94813. 7 interactions.
MINTi MINT-6768470.
STRINGi 9606.ENSP00000273739.

PTM databases

PhosphoSitei O94813.

Proteomic databases

MaxQBi O94813.
PaxDbi O94813.
PRIDEi O94813.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 9353.
KEGGi hsa:9353.
UCSCi uc003gpr.1. human. [O94813-1 ]
uc003gps.1. human. [O94813-3 ]

Organism-specific databases

CTDi 9353.
GeneCardsi GC04P020254.
HGNCi HGNC:11086. SLIT2.
HPAi CAB007590.
HPA019511.
HPA023088.
MIMi 603746. gene.
neXtProti NX_O94813.
PharmGKBi PA35939.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG4886.
GeneTreei ENSGT00760000118811.
HOGENOMi HOG000116120.
HOVERGENi HBG057959.
InParanoidi O94813.
KOi K06839.
OrthoDBi EOG78WKQW.
PhylomeDBi O94813.
TreeFami TF332887.

Enzyme and pathway databases

Reactomei REACT_19226. Activation of Rac.
REACT_19230. Role of Abl in Robo-Slit signaling.
REACT_19342. Inactivation of Cdc42 and Rac.
REACT_19351. Signaling by Robo receptor.
REACT_19376. Regulation of Commissural axon pathfinding by Slit and Robo.
REACT_22237. Netrin-1 signaling.

Miscellaneous databases

EvolutionaryTracei O94813.
GeneWikii SLIT2.
GenomeRNAii 9353.
NextBioi 35025.
PROi O94813.
SOURCEi Search...

Gene expression databases

Bgeei O94813.
CleanExi HS_SLIT2.
ExpressionAtlasi O94813. baseline and differential.
Genevestigatori O94813.

Family and domain databases

Gene3Di 2.60.120.200. 1 hit.
InterProi IPR013320. ConA-like_dom.
IPR000483. Cys-rich_flank_reg_C.
IPR006207. Cys_knot_C.
IPR000742. EG-like_dom.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR003645. Fol_N.
IPR001791. Laminin_G.
IPR001611. Leu-rich_rpt.
IPR003591. Leu-rich_rpt_typical-subtyp.
IPR000372. LRR-contain_N.
[Graphical view ]
Pfami PF00008. EGF. 6 hits.
PF02210. Laminin_G_2. 1 hit.
PF00560. LRR_1. 1 hit.
PF13855. LRR_8. 7 hits.
PF01463. LRRCT. 4 hits.
PF01462. LRRNT. 4 hits.
[Graphical view ]
SMARTi SM00041. CT. 1 hit.
SM00181. EGF. 7 hits.
SM00179. EGF_CA. 2 hits.
SM00274. FOLN. 3 hits.
SM00282. LamG. 1 hit.
SM00369. LRR_TYP. 8 hits.
SM00082. LRRCT. 4 hits.
SM00013. LRRNT. 4 hits.
[Graphical view ]
SUPFAMi SSF49899. SSF49899. 1 hit.
PROSITEi PS00010. 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 ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and expressions of three mammalian homologues of Drosophila slit suggest possible roles for Slit in the formation and maintenance of the nervous system."
    Itoh A., Miyabayashi T., Ohno M., Sakano S.
    Brain Res. Mol. Brain Res. 62:175-186(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY, VARIANTS PRO-636 AND PHE-1277.
    Tissue: Fetal lung.
  2. "Distinct but overlapping expression patterns of two vertebrate slit homologs implies functional roles in CNS development and organogenesis."
    Holmes G.P., Negus K., Burridge L., Raman S., Algar E., Yamada T., Little M.H.
    Mech. Dev. 79:57-72(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), TISSUE SPECIFICITY.
    Tissue: Fetal brain and Fetal kidney.
  3. "Slit proteins bind Robo receptors and have an evolutionarily conserved role in repulsive axon guidance."
    Brose K., Bland K.S., Wang K.H., Arnott D., Henzel W., Goodman C.S., Tessier-Lavigne M., Kidd T.
    Cell 96:795-806(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), PROTEIN SEQUENCE OF 1122-1129, FUNCTION, INTERACTION WITH ROBO1 AND ROBO2, SUBCELLULAR LOCATION.
    Tissue: Fetal brain.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
  6. "Squeezing axons out of the gray matter: a role for slit and semaphorin proteins from midline and ventral spinal cord."
    Zou Y., Stoeckli E., Chen H., Tessier-Lavigne M.
    Cell 102:363-375(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  7. "Slit2 is a repellent for retinal ganglion cell axons."
    Niclou S.P., Jia L., Raper J.A.
    J. Neurosci. 20:4962-4974(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. "The neuronal repellent Slit inhibits leukocyte chemotaxis induced by chemotactic factors."
    Wu J.Y., Feng L., Park H.T., Havlioglu N., Wen L., Tang H., Bacon K.B., Jiang Z.H., Zhang X.C., Rao Y.
    Nature 410:948-952(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  9. "The N-terminal leucine-rich regions in Slit are sufficient to repel olfactory bulb axons and subventricular zone neurons."
    Chen J.H., Wen L., Dupuis S., Wu J.Y., Rao Y.
    J. Neurosci. 21:1548-1556(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: DOMAIN.
  10. "Diversity and specificity of actions of Slit2 proteolytic fragments in axon guidance."
    Nguyen-Ba-Charvet K.T., Brose K., Ma L., Wang K.H., Marillat V., Sotelo C., Tessier-Lavigne M., Chedotal A.
    J. Neurosci. 21:4281-4289(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH ROBO1 AND ROBO2.
  11. "Hierarchical organization of guidance receptors: silencing of netrin attraction by slit through a Robo/DCC receptor complex."
    Stein E., Tessier-Lavigne M.
    Science 291:1928-1938(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  12. "Slit proteins: molecular guidance cues for cells ranging from neurons to leukocytes."
    Wong K., Park H.T., Wu J.Y., Rao Y.
    Curr. Opin. Genet. Dev. 12:583-591(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  13. "Production of Slit2 LRR domains in mammalian cells for structural studies and the structure of human Slit2 domain 3."
    Morlot C., Hemrika W., Romijn R.A., Gros P., Cusack S., McCarthy A.A.
    Acta Crystallogr. D 63:961-968(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.01 ANGSTROMS) OF 504-716, DISULFIDE BONDS.
  14. Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 271-480 IN COMPLEX WITH ROBO1, DISULFIDE BONDS.
  15. Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 726-907, SUBUNIT, DISULFIDE BONDS, HEPARIN-BINDING.

Entry informationi

Entry nameiSLIT2_HUMAN
AccessioniPrimary (citable) accession number: O94813
Secondary accession number(s): B7ZLR5
, O95710, Q17RU3, Q9Y5Q7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2003
Last sequence update: May 1, 1999
Last modified: October 29, 2014
This is version 150 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

External Data

Dasty 3