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O94813 (SLIT2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 144. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Slit homolog 2 protein

Short name=Slit-2
Gene names
Name:SLIT2
Synonyms:SLIL3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1529 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.3 Ref.6 Ref.7 Ref.8 Ref.10 Ref.11

Subunit structure

Interacts with GREM1 By similarity. Homodimer. Binds ROBO1 and ROBO2 with high affinity. Ref.3 Ref.10 Ref.15

Subcellular location

Secreted. Note: The C-terminal cleavage protein is more diffusible than the larger N-terminal protein that is more tightly cell associated. Ref.3

Tissue specificity

Fetal lung and kidney, and adult spinal cord. Weak expression in adult adrenal gland, thyroid, trachea and other tissues examined. Ref.1 Ref.2

Domain

The leucine-rich repeat domain is sufficient for guiding both axon projection and neuronal migration, in vitro. Ref.9

Sequence similarities

Contains 1 CTCK (C-terminal cystine knot-like) domain.

Contains 7 EGF-like domains.

Contains 1 laminin G-like domain.

Contains 20 LRR (leucine-rich) repeats.

Contains 4 LRRCT domains.

Contains 4 LRRNT domains.

Ontologies

Keywords
   Biological processChemotaxis
Differentiation
Neurogenesis
   Cellular componentSecreted
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainEGF-like domain
Leucine-rich repeat
Repeat
Signal
   LigandHeparin-binding
   Molecular functionDevelopmental protein
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processRoundabout signaling pathway

Inferred from mutant phenotype PubMed 18829537. Source: BHF-UCL

apoptotic process involved in luteolysis

Inferred from expression pattern PubMed 18566128. Source: UniProtKB

axon extension involved in axon guidance

Inferred from direct assay PubMed 16840550. Source: UniProtKB

axon guidance

Inferred from direct assay PubMed 11748139. Source: UniProtKB

branching morphogenesis of an epithelial tube

Inferred from direct assay PubMed 18345009. Source: UniProtKB

cell migration involved in sprouting angiogenesis

Inferred from mutant phenotype PubMed 19351956. Source: BHF-UCL

cell-cell adhesion

Inferred from electronic annotation. Source: Ensembl

cellular response to heparin

Inferred from direct assay PubMed 17062560. Source: UniProtKB

cellular response to hormone stimulus

Inferred from expression pattern PubMed 18566128. Source: UniProtKB

chemorepulsion involved in postnatal olfactory bulb interneuron migration

Inferred from direct assay PubMed 15207848. Source: UniProtKB

corticospinal neuron axon guidance through spinal cord

Inferred from mutant phenotype Ref.6. Source: BHF-UCL

dorsal/ventral axon guidance

Inferred from electronic annotation. Source: Ensembl

in utero embryonic development

Inferred from electronic annotation. Source: Ensembl

induction of negative chemotaxis

Inferred from direct assay PubMed 10197527. Source: UniProtKB

mammary duct terminal end bud growth

Inferred from electronic annotation. Source: Ensembl

metanephros development

Inferred from electronic annotation. Source: Ensembl

motor neuron axon guidance

Inferred from direct assay Ref.3. Source: UniProtKB

negative chemotaxis

Inferred from direct assay PubMed 11748139. Source: UniProtKB

negative regulation of actin filament polymerization

Inferred from direct assay PubMed 19759280. Source: UniProtKB

negative regulation of catalytic activity

Inferred from direct assay PubMed 16439689PubMed 19759280. Source: GOC

negative regulation of cell growth

Inferred from mutant phenotype PubMed 18829537. Source: BHF-UCL

negative regulation of cell migration

Inferred from direct assay PubMed 19005219. Source: UniProtKB

negative regulation of cell proliferation

Inferred from electronic annotation. Source: Ensembl

negative regulation of cellular response to growth factor stimulus

Inferred from direct assay PubMed 16439689. Source: BHF-UCL

negative regulation of chemokine-mediated signaling pathway

Inferred from mutant phenotype PubMed 18829537. Source: BHF-UCL

negative regulation of endothelial cell migration

Inferred from direct assay PubMed 18345009. Source: UniProtKB

negative regulation of gene expression

Inferred from electronic annotation. Source: Ensembl

negative regulation of lamellipodium assembly

Inferred from direct assay PubMed 16439689. Source: UniProtKB

negative regulation of leukocyte chemotaxis

Inferred from direct assay Ref.8. Source: UniProtKB

negative regulation of monocyte chemotaxis

Inferred from sequence or structural similarity. Source: BHF-UCL

negative regulation of mononuclear cell migration

Inferred from direct assay PubMed 16439689. Source: BHF-UCL

negative regulation of neutrophil chemotaxis

Inferred from direct assay PubMed 19759280. Source: UniProtKB

negative regulation of protein phosphorylation

Inferred from direct assay PubMed 18345009. Source: UniProtKB

negative regulation of retinal ganglion cell axon guidance

Inferred from direct assay PubMed 17062560. Source: UniProtKB

negative regulation of small GTPase mediated signal transduction

Inferred from direct assay PubMed 16439689. Source: UniProtKB

negative regulation of smooth muscle cell chemotaxis

Inferred from direct assay PubMed 16439689. Source: BHF-UCL

negative regulation of smooth muscle cell migration

Inferred from direct assay PubMed 16439689. Source: BHF-UCL

negative regulation of vascular permeability

Inferred from direct assay PubMed 18345009. Source: UniProtKB

positive regulation of apoptotic process

Inferred from mutant phenotype PubMed 18566128. Source: UniProtKB

positive regulation of axonogenesis

Traceable author statement PubMed 10197527. Source: UniProtKB

response to cortisol

Inferred from expression pattern PubMed 18566128. Source: UniProtKB

retinal ganglion cell axon guidance

Inferred from direct assay Ref.7Ref.15. Source: UniProtKB

ureteric bud development

Inferred from mutant phenotype PubMed 15130495. Source: UniProtKB

   Cellular_componentcell surface

Inferred from direct assay Ref.3. Source: UniProtKB

cytoplasm

Inferred from direct assay PubMed 18566128. Source: UniProtKB

extracellular region

Traceable author statement. Source: Reactome

extracellular space

Inferred from direct assay PubMed 16439689PubMed 19005219Ref.3. Source: UniProtKB

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867. Source: UniProt

membrane

Non-traceable author statement PubMed 16439689. Source: UniProtKB

plasma membrane

Traceable author statement. Source: Reactome

   Molecular_functionGTPase inhibitor activity

Inferred from direct assay PubMed 16439689PubMed 19759280. Source: UniProtKB

Roundabout binding

Inferred from physical interaction Ref.3PubMed 15207848Ref.14. Source: UniProtKB

calcium ion binding

Non-traceable author statement Ref.1. Source: UniProtKB

chemorepellent activity

Inferred from electronic annotation. Source: Ensembl

heparin binding

Inferred from direct assay PubMed 17062560. Source: UniProtKB

identical protein binding

Inferred from physical interaction Ref.15. Source: IntAct

laminin-1 binding

Inferred from direct assay Ref.3. Source: UniProtKB

protein homodimerization activity

Inferred from direct assay Ref.15. Source: UniProtKB

proteoglycan binding

Inferred from physical interaction PubMed 11375980. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

itself2EBI-1236865,EBI-1236865

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O94813-1)

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.
Isoform 2 (identifier: O94813-2)

The sequence of this isoform differs from the canonical sequence as follows:
     258-258: S → SDEEE
     480-487: Missing.
Isoform 3 (identifier: O94813-3)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3030 Potential
Chain31 – 15291499Slit homolog 2 protein
PRO_0000007725
Chain31 – 11211091Slit homolog 2 protein N-product Ref.3
PRO_0000007726
Chain1122 – 1529408Slit homolog 2 protein C-product Ref.3
PRO_0000007727

Regions

Domain31 – 5525LRRNT
Repeat56 – 7722LRR 1
Repeat80 – 10122LRR 2
Repeat104 – 12522LRR 3
Repeat128 – 14922LRR 4
Repeat152 – 17322LRR 5
Repeat176 – 19722LRR 6
Domain209 – 25951LRRCT 1
Domain264 – 30037LRRNT 2
Repeat301 – 32222LRR 7
Repeat325 – 34622LRR 8
Repeat349 – 37022LRR 9
Repeat373 – 39422LRR 10
Repeat397 – 41822LRR 11
Domain430 – 48051LRRCT 2
Domain497 – 53337LRRNT 3
Repeat534 – 55522LRR 12
Repeat559 – 58022LRR 13
Repeat583 – 60422LRR 14
Repeat607 – 62822LRR 15
Repeat631 – 65222LRR 16
Domain664 – 71451LRRCT 3
Domain718 – 75437LRRNT 4
Repeat755 – 77723LRR 17
Repeat778 – 79922LRR 18
Repeat802 – 82322LRR 19
Repeat826 – 84722LRR 20
Domain859 – 90951LRRCT 4
Domain918 – 95538EGF-like 1
Domain957 – 99640EGF-like 2
Domain998 – 103437EGF-like 3; calcium-binding Potential
Domain1036 – 107439EGF-like 4
Domain1076 – 111237EGF-like 5; calcium-binding Potential
Domain1121 – 115737EGF-like 6
Domain1160 – 1333174Laminin G-like
Domain1332 – 136837EGF-like 7
Domain1453 – 152876CTCK

Sites

Site1121 – 11222Cleavage Ref.3

Amino acid modifications

Glycosylation661N-linked (GlcNAc...) Potential
Glycosylation1861N-linked (GlcNAc...) Potential
Glycosylation5641N-linked (GlcNAc...) Potential
Glycosylation6231N-linked (GlcNAc...)
Glycosylation7941N-linked (GlcNAc...) Potential
Glycosylation7991N-linked (GlcNAc...) Potential
Glycosylation10091N-linked (GlcNAc...) Potential
Glycosylation10101N-linked (GlcNAc...) Potential
Glycosylation10191N-linked (GlcNAc...) Potential
Glycosylation11831N-linked (GlcNAc...) Potential
Glycosylation12661N-linked (GlcNAc...) Potential
Glycosylation13001N-linked (GlcNAc...) Potential
Disulfide bond277 ↔ 286 Ref.13 Ref.14 Ref.15
Disulfide bond434 ↔ 457 Ref.13 Ref.14 Ref.15
Disulfide bond436 ↔ 478 Ref.13 Ref.14 Ref.15
Disulfide bond506 ↔ 512 Ref.13 Ref.14 Ref.15
Disulfide bond510 ↔ 519 Ref.13 Ref.14 Ref.15
Disulfide bond668 ↔ 691 Ref.13 Ref.14 Ref.15
Disulfide bond670 ↔ 712 Ref.13 Ref.14 Ref.15
Disulfide bond727 ↔ 733 Ref.13 Ref.14 Ref.15
Disulfide bond731 ↔ 740 Ref.13 Ref.14 Ref.15
Disulfide bond863 ↔ 886 Ref.13 Ref.14 Ref.15
Disulfide bond865 ↔ 907 Ref.13 Ref.14 Ref.15
Disulfide bond922 ↔ 933 By similarity
Disulfide bond927 ↔ 943 By similarity
Disulfide bond945 ↔ 954 By similarity
Disulfide bond961 ↔ 972 By similarity
Disulfide bond966 ↔ 984 By similarity
Disulfide bond986 ↔ 995 By similarity
Disulfide bond1002 ↔ 1013 By similarity
Disulfide bond1007 ↔ 1022 By similarity
Disulfide bond1024 ↔ 1033 By similarity
Disulfide bond1040 ↔ 1053 By similarity
Disulfide bond1047 ↔ 1062 By similarity
Disulfide bond1064 ↔ 1073 By similarity
Disulfide bond1080 ↔ 1091 By similarity
Disulfide bond1085 ↔ 1100 By similarity
Disulfide bond1102 ↔ 1111 By similarity
Disulfide bond1125 ↔ 1136 By similarity
Disulfide bond1130 ↔ 1145 By similarity
Disulfide bond1147 ↔ 1156 By similarity
Disulfide bond1307 ↔ 1333 By similarity
Disulfide bond1336 ↔ 1346 By similarity
Disulfide bond1341 ↔ 1356 By similarity
Disulfide bond1358 ↔ 1367 By similarity
Disulfide bond1375 ↔ 1385 By similarity
Disulfide bond1380 ↔ 1395 By similarity
Disulfide bond1397 ↔ 1406 By similarity
Disulfide bond1416 ↔ 1426 By similarity
Disulfide bond1421 ↔ 1436 By similarity
Disulfide bond1438 ↔ 1447 By similarity
Disulfide bond1453 ↔ 1492 By similarity
Disulfide bond1471 ↔ 1506 By similarity
Disulfide bond1482 ↔ 1522 By similarity
Disulfide bond1486 ↔ 1524 By similarity

Natural variations

Alternative sequence2581S → SDEEE in isoform 2.
VSP_050035
Alternative sequence480 – 4878Missing in isoform 2 and isoform 3.
VSP_050036
Natural variant6361S → P. Ref.1
VAR_018098
Natural variant12771S → F. Ref.1
VAR_018099

Experimental info

Sequence conflict2261Q → K in AAD25539. Ref.2
Sequence conflict607 – 6104SLKT → KPQN in AAD04309. Ref.3
Sequence conflict6341L → M in AAD04309. Ref.3

Secondary structure

....................................................................................................... 1529
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: 5D19CC5E7FD461BA

FASTA1,529169,870
        10         20         30         40         50         60 
MRGVGWQMLS LSLGLVLAIL NKVAPQACPA QCSCSGSTVD CHGLALRSVP RNIPRNTERL 

        70         80         90        100        110        120 
DLNGNNITRI TKTDFAGLRH LRVLQLMENK ISTIERGAFQ DLKELERLRL NRNHLQLFPE 

       130        140        150        160        170        180 
LLFLGTAKLY RLDLSENQIQ AIPRKAFRGA VDIKNLQLDY NQISCIEDGA FRALRDLEVL 

       190        200        210        220        230        240 
TLNNNNITRL SVASFNHMPK LRTFRLHSNN LYCDCHLAWL SDWLRQRPRV GLYTQCMGPS 

       250        260        270        280        290        300 
HLRGHNVAEV QKREFVCSGH QSFMAPSCSV LHCPAACTCS NNIVDCRGKG LTEIPTNLPE 

       310        320        330        340        350        360 
TITEIRLEQN TIKVIPPGAF SPYKKLRRID LSNNQISELA PDAFQGLRSL NSLVLYGNKI 

       370        380        390        400        410        420 
TELPKSLFEG LFSLQLLLLN ANKINCLRVD AFQDLHNLNL LSLYDNKLQT IAKGTFSPLR 

       430        440        450        460        470        480 
AIQTMHLAQN PFICDCHLKW LADYLHTNPI ETSGARCTSP RRLANKRIGQ IKSKKFRCSA 

       490        500        510        520        530        540 
KEQYFIPGTE DYRSKLSGDC FADLACPEKC RCEGTTVDCS NQKLNKIPEH IPQYTAELRL 

       550        560        570        580        590        600 
NNNEFTVLEA TGIFKKLPQL RKINFSNNKI TDIEEGAFEG ASGVNEILLT SNRLENVQHK 

       610        620        630        640        650        660 
MFKGLESLKT LMLRSNRITC VGNDSFIGLS SVRLLSLYDN QITTVAPGAF DTLHSLSTLN 

       670        680        690        700        710        720 
LLANPFNCNC YLAWLGEWLR KKRIVTGNPR CQKPYFLKEI PIQDVAIQDF TCDDGNDDNS 

       730        740        750        760        770        780 
CSPLSRCPTE CTCLDTVVRC SNKGLKVLPK GIPRDVTELY LDGNQFTLVP KELSNYKHLT 

       790        800        810        820        830        840 
LIDLSNNRIS TLSNQSFSNM TQLLTLILSY NRLRCIPPRT FDGLKSLRLL SLHGNDISVV 

       850        860        870        880        890        900 
PEGAFNDLSA LSHLAIGANP LYCDCNMQWL SDWVKSEYKE PGIARCAGPG EMADKLLLTT 

       910        920        930        940        950        960 
PSKKFTCQGP VDVNILAKCN PCLSNPCKND GTCNSDPVDF YRCTCPYGFK GQDCDVPIHA 

       970        980        990       1000       1010       1020 
CISNPCKHGG TCHLKEGEED GFWCICADGF EGENCEVNVD DCEDNDCENN STCVDGINNY 

      1030       1040       1050       1060       1070       1080 
TCLCPPEYTG ELCEEKLDFC AQDLNPCQHD SKCILTPKGF KCDCTPGYVG EHCDIDFDDC 

      1090       1100       1110       1120       1130       1140 
QDNKCKNGAH CTDAVNGYTC ICPEGYSGLF CEFSPPMVLP RTSPCDNFDC QNGAQCIVRI 

      1150       1160       1170       1180       1190       1200 
NEPICQCLPG YQGEKCEKLV SVNFINKESY LQIPSAKVRP QTNITLQIAT DEDSGILLYK 

      1210       1220       1230       1240       1250       1260 
GDKDHIAVEL YRGRVRASYD TGSHPASAIY SVETINDGNF HIVELLALDQ SLSLSVDGGN 

      1270       1280       1290       1300       1310       1320 
PKIITNLSKQ STLNFDSPLY VGGMPGKSNV ASLRQAPGQN GTSFHGCIRN LYINSELQDF 

      1330       1340       1350       1360       1370       1380 
QKVPMQTGIL PGCEPCHKKV CAHGTCQPSS QAGFTCECQE GWMGPLCDQR TNDPCLGNKC 

      1390       1400       1410       1420       1430       1440 
VHGTCLPINA FSYSCKCLEG HGGVLCDEEE DLFNPCQAIK CKHGKCRLSG LGQPYCECSS 

      1450       1460       1470       1480       1490       1500 
GYTGDSCDRE ISCRGERIRD YYQKQQGYAA CQTTKKVSRL ECRGGCAGGQ CCGPLRSKRR 

      1510       1520 
KYSFECTDGS SFVDEVEKVV KCGCTRCVS 

« Hide

Isoform 2 [UniParc].

Checksum: 56DE2356BB2E5CAD
Show »

FASTA1,525169,395
Isoform 3 [UniParc].

Checksum: 7620F3C96DD4E534
Show »

FASTA1,521168,893

References

« Hide 'large scale' references
[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]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. expand/collapse author list , 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
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]"Structural insights into the Slit-Robo complex."
Morlot C., Thielens N.M., Ravelli R.B., Hemrika W., Romijn R.A., Gros P., Cusack S., McCarthy A.A.
Proc. Natl. Acad. Sci. U.S.A. 104:14923-14928(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 271-480 IN COMPLEX WITH ROBO1, DISULFIDE BONDS.
[15]"Structure and functional relevance of the Slit2 homodimerization domain."
Seiradake E., von Philipsborn A.C., Henry M., Fritz M., Lortat-Jacob H., Jamin M., Hemrika W., Bastmeyer M., Cusack S., McCarthy A.A.
EMBO Rep. 10:736-741(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 726-907, SUBUNIT, DISULFIDE BONDS, HEPARIN-BINDING.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_004778.1. NM_004787.2.
UniGeneHs.29802.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2V70X-ray3.01A/B/C/D504-714[»]
2V9SX-ray2.00A/B/C/D271-480[»]
2V9TX-ray1.70B271-480[»]
2WFHX-ray1.80A/B726-907[»]
ProteinModelPortalO94813.
SMRO94813. Positions 25-1451.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114756. 5 interactions.
DIPDIP-38198N.
IntActO94813. 7 interactions.
MINTMINT-6768470.
STRING9606.ENSP00000273739.

PTM databases

PhosphoSiteO94813.

Proteomic databases

PaxDbO94813.
PRIDEO94813.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000503823; ENSP00000427548; ENSG00000145147. [O94813-3]
ENST00000503837; ENSP00000422261; ENSG00000145147. [O94813-2]
ENST00000504154; ENSP00000422591; ENSG00000145147. [O94813-1]
GeneID9353.
KEGGhsa:9353.
UCSCuc003gpr.1. human. [O94813-1]
uc003gps.1. human. [O94813-3]

Organism-specific databases

CTD9353.
GeneCardsGC04P020254.
HGNCHGNC:11086. SLIT2.
HPACAB007590.
HPA019511.
HPA023088.
MIM603746. gene.
neXtProtNX_O94813.
PharmGKBPA35939.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG4886.
HOGENOMHOG000116120.
HOVERGENHBG057959.
InParanoidO94813.
KOK06839.
OrthoDBEOG78WKQW.
PhylomeDBO94813.
TreeFamTF332887.

Enzyme and pathway databases

ReactomeREACT_111045. Developmental Biology.
REACT_195021. Developmental Biology.

Gene expression databases

ArrayExpressO94813.
BgeeO94813.
CleanExHS_SLIT2.
GenevestigatorO94813.

Family and domain databases

Gene3D2.60.120.200. 1 hit.
InterProIPR008985. ConA-like_lec_gl_sf.
IPR013320. ConA-like_subgrp.
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]
PfamPF00008. EGF. 6 hits.
PF02210. Laminin_G_2. 1 hit.
PF00560. LRR_1. 1 hit.
PF01463. LRRCT. 4 hits.
PF01462. LRRNT. 4 hits.
[Graphical view]
SMARTSM00041. 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]
SUPFAMSSF49899. SSF49899. 1 hit.
PROSITEPS00010. 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]
ProtoNetSearch...

Other

EvolutionaryTraceO94813.
GeneWikiSLIT2.
GenomeRNAi9353.
NextBio35025.
PROO94813.
SOURCESearch...

Entry information

Entry nameSLIT2_HUMAN
AccessionPrimary (citable) accession number: O94813
Secondary accession number(s): B7ZLR5 expand/collapse secondary AC list , O95710, Q17RU3, Q9Y5Q7
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2003
Last sequence update: May 1, 1999
Last modified: April 16, 2014
This is version 144 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 4

Human chromosome 4: entries, gene names and cross-references to MIM