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Q9Y6N7

- ROBO1_HUMAN

UniProt

Q9Y6N7 - ROBO1_HUMAN

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Protein

Roundabout homolog 1

Gene

ROBO1

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

Functioni

Receptor for SLIT1 and SLIT2 which are thought to act as molecular guidance cue in cellular migration, including axonal navigation at the ventral midline of the neural tube and projection of axons to different regions during neuronal development. In axon growth cones, the silencing of the attractive effect of NTN1 by SLIT2 may require the formation of a ROBO1-DCC complex. May be required for lung development.1 Publication

GO - Molecular functioni

  1. axon guidance receptor activity Source: ProtInc
  2. identical protein binding Source: UniProtKB
  3. LRR domain binding Source: UniProtKB

GO - Biological processi

  1. activation of cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB
  2. axon guidance Source: Reactome
  3. axon midline choice point recognition Source: UniProtKB
  4. cell adhesion Source: ProtInc
  5. cell migration involved in sprouting angiogenesis Source: BHF-UCL
  6. chemorepulsion involved in postnatal olfactory bulb interneuron migration Source: UniProtKB
  7. homophilic cell adhesion Source: UniProtKB
  8. mammary duct terminal end bud growth Source: Ensembl
  9. negative regulation of chemokine-mediated signaling pathway Source: BHF-UCL
  10. negative regulation of mammary gland epithelial cell proliferation Source: BHF-UCL
  11. negative regulation of negative chemotaxis Source: UniProtKB
  12. nervous system development Source: ProtInc
  13. positive regulation of axonogenesis Source: UniProtKB
  14. Roundabout signaling pathway Source: BHF-UCL
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Receptor

Keywords - Biological processi

Chemotaxis, Differentiation, Neurogenesis

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:
Roundabout homolog 1
Alternative name(s):
Deleted in U twenty twenty
H-Robo-1
Gene namesi
Name:ROBO1
Synonyms:DUTT1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 3

Organism-specific databases

HGNCiHGNC:10249. ROBO1.

Subcellular locationi

GO - Cellular componenti

  1. axolemma Source: Ensembl
  2. cell surface Source: UniProtKB
  3. cytoplasm Source: UniProtKB
  4. integral component of plasma membrane Source: ProtInc
  5. plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA34620.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2525Sequence AnalysisAdd
BLAST
Chaini26 – 16511626Roundabout homolog 1PRO_0000031033Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi89 ↔ 1471 PublicationPROSITE-ProRule annotation
Glycosylationi160 – 1601N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi191 ↔ 240PROSITE-ProRule annotation
Disulfide bondi283 ↔ 330PROSITE-ProRule annotation
Disulfide bondi372 ↔ 428PROSITE-ProRule annotation
Glycosylationi463 – 4631N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi476 ↔ 525PROSITE-ProRule annotation
Glycosylationi790 – 7901N-linked (GlcNAc...)Sequence Analysis
Glycosylationi820 – 8201N-linked (GlcNAc...)Sequence Analysis
Glycosylationi827 – 8271N-linked (GlcNAc...)Sequence Analysis
Modified residuei940 – 9401Phosphoserine2 Publications
Modified residuei1038 – 10381Phosphotyrosine; by ABL; in vitro1 Publication
Modified residuei1055 – 10551Phosphoserine1 Publication
Modified residuei1073 – 10731Phosphotyrosine; by ABL; in vitro1 Publication
Modified residuei1114 – 11141Phosphotyrosine; by ABL; in vitro1 Publication
Modified residuei1240 – 12401Phosphothreonine1 Publication
Modified residuei1297 – 12971Phosphoserine1 Publication

Post-translational modificationi

Ubiquitinated. May be deubiquitinated by USP33 (By similarity).By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ9Y6N7.
PaxDbiQ9Y6N7.
PRIDEiQ9Y6N7.

PTM databases

PhosphoSiteiQ9Y6N7.

Expressioni

Tissue specificityi

Widely expressed, with exception of kidney.1 Publication

Gene expression databases

BgeeiQ9Y6N7.
CleanExiHS_ROBO1.
ExpressionAtlasiQ9Y6N7. baseline and differential.
GenevestigatoriQ9Y6N7.

Organism-specific databases

HPAiCAB013524.

Interactioni

Subunit structurei

Homodimer. Dimerization is mediated by the extracellular domain and is independent of SLIT liganding. Interacts with SLIT1 and SLIT2.4 Publications

Protein-protein interaction databases

BioGridi112018. 5 interactions.
DIPiDIP-33034N.
IntActiQ9Y6N7. 4 interactions.
MINTiMINT-1392694.
STRINGi9606.ENSP00000381450.

Structurei

Secondary structure

1
1651
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi66 – 727
Beta strandi77 – 793
Beta strandi85 – 873
Beta strandi90 – 956
Beta strandi98 – 1036
Turni111 – 1133
Beta strandi118 – 1214
Beta strandi127 – 1315
Beta strandi143 – 1519
Beta strandi154 – 1574
Beta strandi161 – 1655
Beta strandi179 – 1824
Beta strandi187 – 1904
Beta strandi196 – 1983
Beta strandi201 – 2066
Beta strandi209 – 2113
Beta strandi213 – 2153
Beta strandi218 – 2214
Beta strandi224 – 2296
Helixi232 – 2343
Beta strandi236 – 2449
Beta strandi247 – 2504
Beta strandi254 – 2596
Helixi261 – 2666
Beta strandi464 – 4674
Beta strandi471 – 4755
Beta strandi485 – 49410
Beta strandi502 – 5065
Beta strandi509 – 5146
Helixi517 – 5193
Beta strandi523 – 5286
Beta strandi533 – 5375
Beta strandi540 – 5434
Helixi666 – 67510
Beta strandi676 – 6805
Beta strandi687 – 6893
Beta strandi691 – 6999
Beta strandi706 – 71510
Helixi719 – 7213
Beta strandi724 – 7285
Beta strandi735 – 7384
Beta strandi746 – 75510
Beta strandi766 – 7694
Beta strandi780 – 7867
Beta strandi794 – 7996
Helixi803 – 8053
Beta strandi812 – 82110
Beta strandi825 – 8317
Beta strandi836 – 8394
Beta strandi848 – 8569
Beta strandi867 – 8693
Helixi880 – 8834

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2EO9NMR-A454-564[»]
2V9QX-ray2.50A61-266[»]
2V9RX-ray2.00A61-266[»]
2V9TX-ray1.70A61-166[»]
4HLJX-ray1.80A660-897[»]
ProteinModelPortaliQ9Y6N7.
SMRiQ9Y6N7. Positions 61-266, 454-564, 660-885.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9Y6N7.

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini26 – 897872ExtracellularSequence AnalysisAdd
BLAST
Topological domaini919 – 1651733CytoplasmicSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei898 – 91821HelicalSequence AnalysisAdd
BLAST

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini68 – 16497Ig-like C2-type 1Add
BLAST
Domaini170 – 25788Ig-like C2-type 2Add
BLAST
Domaini262 – 34685Ig-like C2-type 3Add
BLAST
Domaini351 – 44696Ig-like C2-type 4Add
BLAST
Domaini455 – 54187Ig-like C2-type 5Add
BLAST
Domaini563 – 65795Fibronectin type-III 1PROSITE-ProRule annotationAdd
BLAST
Domaini676 – 77398Fibronectin type-III 2PROSITE-ProRule annotationAdd
BLAST
Domaini778 – 87497Fibronectin type-III 3PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the immunoglobulin superfamily. ROBO family.Curated
Contains 3 fibronectin type-III domains.PROSITE-ProRule annotation

Keywords - Domaini

Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG238978.
GeneTreeiENSGT00760000118886.
HOGENOMiHOG000010267.
HOVERGENiHBG073476.
InParanoidiQ9Y6N7.
KOiK06753.
OMAiEDTQNGM.
OrthoDBiEOG7KWSGP.
PhylomeDBiQ9Y6N7.
TreeFamiTF351053.

Family and domain databases

Gene3Di2.60.40.10. 9 hits.
InterProiIPR003961. Fibronectin_type3.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003598. Ig_sub2.
IPR003596. Ig_V-set_subgr.
[Graphical view]
PfamiPF00041. fn3. 3 hits.
PF07679. I-set. 5 hits.
[Graphical view]
SMARTiSM00060. FN3. 3 hits.
SM00408. IGc2. 4 hits.
SM00406. IGv. 1 hit.
[Graphical view]
SUPFAMiSSF49265. SSF49265. 2 hits.
PROSITEiPS50853. FN3. 3 hits.
PS50835. IG_LIKE. 5 hits.
[Graphical view]

Sequences (6)i

Sequence statusi: Complete.

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

This entry describes 6 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9Y6N7-1) [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
MKWKHVPFLV MISLLSLSPN HLFLAQLIPD PEDVERGNDH GTPIPTSDND
60 70 80 90 100
DNSLGYTGSR LRQEDFPPRI VEHPSDLIVS KGEPATLNCK AEGRPTPTIE
110 120 130 140 150
WYKGGERVET DKDDPRSHRM LLPSGSLFFL RIVHGRKSRP DEGVYVCVAR
160 170 180 190 200
NYLGEAVSHN ASLEVAILRD DFRQNPSDVM VAVGEPAVME CQPPRGHPEP
210 220 230 240 250
TISWKKDGSP LDDKDERITI RGGKLMITYT RKSDAGKYVC VGTNMVGERE
260 270 280 290 300
SEVAELTVLE RPSFVKRPSN LAVTVDDSAE FKCEARGDPV PTVRWRKDDG
310 320 330 340 350
ELPKSRYEIR DDHTLKIRKV TAGDMGSYTC VAENMVGKAE ASATLTVQEP
360 370 380 390 400
PHFVVKPRDQ VVALGRTVTF QCEATGNPQP AIFWRREGSQ NLLFSYQPPQ
410 420 430 440 450
SSSRFSVSQT GDLTITNVQR SDVGYYICQT LNVAGSIITK AYLEVTDVIA
460 470 480 490 500
DRPPPVIRQG PVNQTVAVDG TFVLSCVATG SPVPTILWRK DGVLVSTQDS
510 520 530 540 550
RIKQLENGVL QIRYAKLGDT GRYTCIASTP SGEATWSAYI EVQEFGVPVQ
560 570 580 590 600
PPRPTDPNLI PSAPSKPEVT DVSRNTVTLS WQPNLNSGAT PTSYIIEAFS
610 620 630 640 650
HASGSSWQTV AENVKTETSA IKGLKPNAIY LFLVRAANAY GISDPSQISD
660 670 680 690 700
PVKTQDVLPT SQGVDHKQVQ RELGNAVLHL HNPTVLSSSS IEVHWTVDQQ
710 720 730 740 750
SQYIQGYKIL YRPSGANHGE SDWLVFEVRT PAKNSVVIPD LRKGVNYEIK
760 770 780 790 800
ARPFFNEFQG ADSEIKFAKT LEEAPSAPPQ GVTVSKNDGN GTAILVSWQP
810 820 830 840 850
PPEDTQNGMV QEYKVWCLGN ETRYHINKTV DGSTFSVVIP FLVPGIRYSV
860 870 880 890 900
EVAASTGAGS GVKSEPQFIQ LDAHGNPVSP EDQVSLAQQI SDVVKQPAFI
910 920 930 940 950
AGIGAACWII LMVFSIWLYR HRKKRNGLTS TYAGIRKVPS FTFTPTVTYQ
960 970 980 990 1000
RGGEAVSSGG RPGLLNISEP AAQPWLADTW PNTGNNHNDC SISCCTAGNG
1010 1020 1030 1040 1050
NSDSNLTTYS RPADCIANYN NQLDNKQTNL MLPESTVYGD VDLSNKINEM
1060 1070 1080 1090 1100
KTFNSPNLKD GRFVNPSGQP TPYATTQLIQ SNLSNNMNNG SGDSGEKHWK
1110 1120 1130 1140 1150
PLGQQKQEVA PVQYNIVEQN KLNKDYRAND TVPPTIPYNQ SYDQNTGGSY
1160 1170 1180 1190 1200
NSSDRGSSTS GSQGHKKGAR TPKVPKQGGM NWADLLPPPP AHPPPHSNSE
1210 1220 1230 1240 1250
EYNISVDESY DQEMPCPVPP ARMYLQQDEL EEEEDERGPT PPVRGAASSP
1260 1270 1280 1290 1300
AAVSYSHQST ATLTPSPQEE LQPMLQDCPE ETGHMQHQPD RRRQPVSPPP
1310 1320 1330 1340 1350
PPRPISPPHT YGYISGPLVS DMDTDAPEEE EDEADMEVAK MQTRRLLLRG
1360 1370 1380 1390 1400
LEQTPASSVG DLESSVTGSM INGWGSASEE DNISSGRSSV SSSDGSFFTD
1410 1420 1430 1440 1450
ADFAQAVAAA AEYAGLKVAR RQMQDAAGRR HFHASQCPRP TSPVSTDSNM
1460 1470 1480 1490 1500
SAAVMQKTRP AKKLKHQPGH LRRETYTDDL PPPPVPPPAI KSPTAQSKTQ
1510 1520 1530 1540 1550
LEVRPVVVPK LPSMDARTDR SSDRKGSSYK GREVLDGRQV VDMRTNPGDP
1560 1570 1580 1590 1600
REAQEQQNDG KGRGNKAAKR DLPPAKTHLI QEDILPYCRP TFPTSNNPRD
1610 1620 1630 1640 1650
PSSSSSMSSR GSGSRQREQA NVGRRNIAEM QVLGGYERGE DNNEELEETE

S
Length:1,651
Mass (Da):180,930
Last modified:November 1, 1999 - v1
Checksum:i9D98CD7CAB73074D
GO
Isoform 2 (identifier: Q9Y6N7-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     543-543: Q → QGKVN

Note: Incomplete.

Show »
Length:1,655
Mass (Da):181,328
Checksum:iEB2C3DFF6013A30F
GO
Isoform 3 (identifier: Q9Y6N7-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-39: Missing.
     40-57: HGTPIPTSDNDDNSLGYT → MIAEPAHFYLFGLICLCS
     348-348: Q → QVGS

Show »
Length:1,615
Mass (Da):176,814
Checksum:i66D6413527161E25
GO
Isoform 4 (identifier: Q9Y6N7-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-39: Missing.
     40-57: HGTPIPTSDNDDNSLGYT → MIAEPAHFYLFGLICLCS

Show »
Length:1,612
Mass (Da):176,571
Checksum:i4625E96485E88C34
GO
Isoform 5 (identifier: Q9Y6N7-5) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-57: MKWKHVPFLVMISLLSLSPNHLFLAQLIPDPEDVERGNDHGTPIPTSDNDDNSLGYT → MIAEPAHFYLFGLICLCS
     348-348: Q → QVGS
     938-946: Missing.

Note: No experimental confirmation available.

Show »
Length:1,606
Mass (Da):175,836
Checksum:i79FA0AA96275B1A2
GO
Isoform 6 (identifier: Q9Y6N7-6) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-57: MKWKHVPFLVMISLLSLSPNHLFLAQLIPDPEDVERGNDHGTPIPTSDNDDNSLGYT → MIAEPAHFYLFGLICLCS
     348-348: Q → QVGS
     938-946: Missing.
     1013-1067: Missing.

Note: No experimental confirmation available.

Show »
Length:1,551
Mass (Da):169,661
Checksum:i89F1C62C15B8C9A2
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti182 – 1821A → V in AAI15023. (PubMed:15489334)Curated
Sequence conflicti835 – 8351F → L in AAI15023. (PubMed:15489334)Curated
Sequence conflicti1095 – 10951G → S in CAD98093. (PubMed:17974005)Curated
Sequence conflicti1223 – 12231M → T in Z95705. (PubMed:16641997)Curated
Sequence conflicti1443 – 14431P → L in CAD98093. (PubMed:17974005)Curated
Sequence conflicti1536 – 15361D → G in Z95705. (PubMed:16641997)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti336 – 3361V → A.
Corresponds to variant rs9647397 [ dbSNP | Ensembl ].
VAR_053640
Natural varianti1055 – 10551S → N in a breast cancer sample. 1 Publication
VAR_019071
Natural varianti1091 – 10911S → N.
Corresponds to variant rs35456279 [ dbSNP | Ensembl ].
VAR_053641
Natural varianti1533 – 15331E → D in a breast cancer sample. 1 Publication
Corresponds to variant rs36055689 [ dbSNP | Ensembl ].
VAR_019072

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 5757MKWKH…SLGYT → MIAEPAHFYLFGLICLCS in isoform 5 and isoform 6. 1 PublicationVSP_043881Add
BLAST
Alternative sequencei1 – 3939Missing in isoform 3 and isoform 4. CuratedVSP_010643Add
BLAST
Alternative sequencei40 – 5718HGTPI…SLGYT → MIAEPAHFYLFGLICLCS in isoform 3 and isoform 4. CuratedVSP_010644Add
BLAST
Alternative sequencei348 – 3481Q → QVGS in isoform 3, isoform 5 and isoform 6. 1 PublicationVSP_010645
Alternative sequencei543 – 5431Q → QGKVN in isoform 2. 1 PublicationVSP_010646
Alternative sequencei938 – 9469Missing in isoform 5 and isoform 6. 1 PublicationVSP_043882
Alternative sequencei1013 – 106755Missing in isoform 6. 1 PublicationVSP_046084Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF040990 mRNA. Translation: AAC39575.1.
Z95705 Genomic DNA. No translation available.
AC016946 Genomic DNA. No translation available.
AC055731 Genomic DNA. No translation available.
AC106718 Genomic DNA. No translation available.
AC106720 Genomic DNA. No translation available.
AC108719 Genomic DNA. No translation available.
AC117461 Genomic DNA. No translation available.
AC117479 Genomic DNA. No translation available.
AC119035 Genomic DNA. No translation available.
AC123565 Genomic DNA. No translation available.
AC125624 Genomic DNA. No translation available.
AC125766 Genomic DNA. No translation available.
AC125815 Genomic DNA. No translation available.
AC131008 Genomic DNA. No translation available.
CH471110 Genomic DNA. Translation: EAW68884.1.
CH471110 Genomic DNA. Translation: EAW68885.1.
BC001969 mRNA. Translation: AAH01969.1.
BC115022 mRNA. Translation: AAI15023.1.
BC157861 mRNA. Translation: AAI57862.1.
BC171855 mRNA. Translation: AAI71855.1.
BX538319 mRNA. Translation: CAD98093.1.
CCDSiCCDS46872.2. [Q9Y6N7-5]
CCDS54610.1. [Q9Y6N7-6]
CCDS54611.1. [Q9Y6N7-1]
RefSeqiNP_001139317.1. NM_001145845.1. [Q9Y6N7-6]
NP_002932.1. NM_002941.3. [Q9Y6N7-1]
NP_598334.2. NM_133631.3. [Q9Y6N7-5]
XP_006713340.1. XM_006713277.1. [Q9Y6N7-3]
UniGeneiHs.744218.

Genome annotation databases

EnsembliENST00000464233; ENSP00000420321; ENSG00000169855. [Q9Y6N7-1]
ENST00000467549; ENSP00000417992; ENSG00000169855. [Q9Y6N7-6]
ENST00000495273; ENSP00000420637; ENSG00000169855. [Q9Y6N7-5]
GeneIDi6091.
KEGGihsa:6091.
UCSCiuc003dqb.2. human. [Q9Y6N7-4]
uc003dqd.2. human. [Q9Y6N7-5]
uc003dqe.2. human. [Q9Y6N7-1]

Polymorphism databases

DMDMi49036500.

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
AF040990 mRNA. Translation: AAC39575.1 .
Z95705 Genomic DNA. No translation available.
AC016946 Genomic DNA. No translation available.
AC055731 Genomic DNA. No translation available.
AC106718 Genomic DNA. No translation available.
AC106720 Genomic DNA. No translation available.
AC108719 Genomic DNA. No translation available.
AC117461 Genomic DNA. No translation available.
AC117479 Genomic DNA. No translation available.
AC119035 Genomic DNA. No translation available.
AC123565 Genomic DNA. No translation available.
AC125624 Genomic DNA. No translation available.
AC125766 Genomic DNA. No translation available.
AC125815 Genomic DNA. No translation available.
AC131008 Genomic DNA. No translation available.
CH471110 Genomic DNA. Translation: EAW68884.1 .
CH471110 Genomic DNA. Translation: EAW68885.1 .
BC001969 mRNA. Translation: AAH01969.1 .
BC115022 mRNA. Translation: AAI15023.1 .
BC157861 mRNA. Translation: AAI57862.1 .
BC171855 mRNA. Translation: AAI71855.1 .
BX538319 mRNA. Translation: CAD98093.1 .
CCDSi CCDS46872.2. [Q9Y6N7-5 ]
CCDS54610.1. [Q9Y6N7-6 ]
CCDS54611.1. [Q9Y6N7-1 ]
RefSeqi NP_001139317.1. NM_001145845.1. [Q9Y6N7-6 ]
NP_002932.1. NM_002941.3. [Q9Y6N7-1 ]
NP_598334.2. NM_133631.3. [Q9Y6N7-5 ]
XP_006713340.1. XM_006713277.1. [Q9Y6N7-3 ]
UniGenei Hs.744218.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2EO9 NMR - A 454-564 [» ]
2V9Q X-ray 2.50 A 61-266 [» ]
2V9R X-ray 2.00 A 61-266 [» ]
2V9T X-ray 1.70 A 61-166 [» ]
4HLJ X-ray 1.80 A 660-897 [» ]
ProteinModelPortali Q9Y6N7.
SMRi Q9Y6N7. Positions 61-266, 454-564, 660-885.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 112018. 5 interactions.
DIPi DIP-33034N.
IntActi Q9Y6N7. 4 interactions.
MINTi MINT-1392694.
STRINGi 9606.ENSP00000381450.

PTM databases

PhosphoSitei Q9Y6N7.

Polymorphism databases

DMDMi 49036500.

Proteomic databases

MaxQBi Q9Y6N7.
PaxDbi Q9Y6N7.
PRIDEi Q9Y6N7.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000464233 ; ENSP00000420321 ; ENSG00000169855 . [Q9Y6N7-1 ]
ENST00000467549 ; ENSP00000417992 ; ENSG00000169855 . [Q9Y6N7-6 ]
ENST00000495273 ; ENSP00000420637 ; ENSG00000169855 . [Q9Y6N7-5 ]
GeneIDi 6091.
KEGGi hsa:6091.
UCSCi uc003dqb.2. human. [Q9Y6N7-4 ]
uc003dqd.2. human. [Q9Y6N7-5 ]
uc003dqe.2. human. [Q9Y6N7-1 ]

Organism-specific databases

CTDi 6091.
GeneCardsi GC03M078729.
HGNCi HGNC:10249. ROBO1.
HPAi CAB013524.
MIMi 602430. gene.
neXtProti NX_Q9Y6N7.
PharmGKBi PA34620.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG238978.
GeneTreei ENSGT00760000118886.
HOGENOMi HOG000010267.
HOVERGENi HBG073476.
InParanoidi Q9Y6N7.
KOi K06753.
OMAi EDTQNGM.
OrthoDBi EOG7KWSGP.
PhylomeDBi Q9Y6N7.
TreeFami TF351053.

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

ChiTaRSi ROBO1. human.
EvolutionaryTracei Q9Y6N7.
GeneWikii ROBO1.
GenomeRNAii 6091.
NextBioi 23685.
PROi Q9Y6N7.
SOURCEi Search...

Gene expression databases

Bgeei Q9Y6N7.
CleanExi HS_ROBO1.
ExpressionAtlasi Q9Y6N7. baseline and differential.
Genevestigatori Q9Y6N7.

Family and domain databases

Gene3Di 2.60.40.10. 9 hits.
InterProi IPR003961. Fibronectin_type3.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003598. Ig_sub2.
IPR003596. Ig_V-set_subgr.
[Graphical view ]
Pfami PF00041. fn3. 3 hits.
PF07679. I-set. 5 hits.
[Graphical view ]
SMARTi SM00060. FN3. 3 hits.
SM00408. IGc2. 4 hits.
SM00406. IGv. 1 hit.
[Graphical view ]
SUPFAMi SSF49265. SSF49265. 2 hits.
PROSITEi PS50853. FN3. 3 hits.
PS50835. IG_LIKE. 5 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Roundabout controls axon crossing of the CNS midline and defines a novel subfamily of evolutionarily conserved guidance receptors."
    Kidd T., Brose K., Mitchell K.J., Fetter R.D., Tessier-Lavigne M., Goodman C.S., Tear G.
    Cell 92:205-215(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "The DNA sequence, annotation and analysis of human chromosome 3."
    Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
    , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
    Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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 5 AND 6), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1158-1651 (ISOFORMS 1/2/3/4).
    Tissue: Placenta.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 366-1651 (ISOFORM 2).
    Tissue: Uterine endothelium.
  6. "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: FUNCTION, INTERACTION WITH SLIT2.
    Tissue: Fetal brain.
  7. "The DUTT1 gene, a novel NCAM family member is expressed in developing murine neural tissues and has an unusually broad pattern of expression."
    Sundaresan V., Roberts I., Bateman A., Bankier A., Sheppard M., Hobbs C., Xiong J., Minna J., Latif F., Lerman M., Rabbitts P.
    Mol. Cell. Neurosci. 11:29-35(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  8. Cited for: MAPPING, IDENTIFICATION (ISOFORM 3).
  9. "Repulsive axon guidance: Abelson and Enabled play opposing roles downstream of the roundabout receptor."
    Bashaw G.J., Kidd T., Murray D., Pawson T., Goodman C.S.
    Cell 101:703-715(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT TYR-1038; TYR-1073 AND TYR-1114.
  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: INTERACTION WITH SLIT2.
  11. "Tumour specific promoter region methylation of the human homologue of the Drosophila Roundabout gene DUTT1 (ROBO1) in human cancers."
    Dallol A., Forgacs E., Martinez A., Sekido Y., Walker R., Kishida T., Rabbitts P., Maher E.R., Minna J.D., Latif F.
    Oncogene 21:3020-3028(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROMOTER HYPERMETHYLATION, VARIANTS ASN-1055 AND ASP-1533.
  12. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-940; SER-1055; THR-1240 AND SER-1297, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-940, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "Roundabout 1 exists predominantly as a basal dimeric complex and this is unaffected by binding of the ligand Slit2."
    Zakrys L., Ward R.J., Pediani J.D., Godin A.G., Graham G.J., Milligan G.
    Biochem. J. 461:61-73(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT.
  17. Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 61-166 IN COMPLEX WITH SLIT2, DISULFIDE BOND.
  18. "Solution structure of the fifth Ig-like domain from human roundabout homolog 1."
    RIKEN structural genomics initiative (RSGI)
    Submitted (OCT-2007) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 454-564.

Entry informationi

Entry nameiROBO1_HUMAN
AccessioniPrimary (citable) accession number: Q9Y6N7
Secondary accession number(s): B2RXI1
, D3DU36, E9PD49, Q1RMC7, Q7Z300, Q9BUS7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 21, 2004
Last sequence update: November 1, 1999
Last modified: October 29, 2014
This is version 130 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

Miscellaneous

Maps within a region of overlapping homozygous deletions characterized in both small cell lung cancer cell lines (SCLC) and in a breast cancer cell line. The promoter region of ROBO1 shows complete hypermethylation of CpG sites in the BT-20 breast tumor cell lines, some primary invasive breast carcinomasa and some primary clear cell renal cell carcinomas (CC-RCC).

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 3
    Human chromosome 3: 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