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Q9Y6N7 (ROBO1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 123. 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·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Roundabout homolog 1
Alternative name(s):
Deleted in U twenty twenty
H-Robo-1
Gene names
Name:ROBO1
Synonyms:DUTT1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1651 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.6

Subunit structure

Interacts with SLIT1 and SLIT2. Ref.6 Ref.10

Subcellular location

Membrane; Single-pass type I membrane protein Potential.

Tissue specificity

Widely expressed, with exception of kidney. Ref.7

Post-translational modification

Ubiquitinated. May be deubiquitinated by USP33 By similarity.

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).

Sequence similarities

Belongs to the immunoglobulin superfamily. ROBO family.

Contains 3 fibronectin type-III domains.

Contains 5 Ig-like C2-type (immunoglobulin-like) domains.

Ontologies

Keywords
   Biological processChemotaxis
Differentiation
Neurogenesis
   Cellular componentMembrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainImmunoglobulin domain
Repeat
Signal
Transmembrane
Transmembrane helix
   Molecular functionDevelopmental protein
Receptor
   PTMDisulfide bond
Glycoprotein
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processRoundabout signaling pathway

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

activation of cysteine-type endopeptidase activity involved in apoptotic process

Inferred from mutant phenotype PubMed 18566128. Source: UniProtKB

axon midline choice point recognition

Inferred from sequence or structural similarity. Source: UniProtKB

cell migration involved in sprouting angiogenesis

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

chemorepulsion involved in postnatal olfactory bulb interneuron migration

Inferred from direct assay PubMed 15207848. Source: UniProtKB

homophilic cell adhesion

Inferred from direct assay PubMed 12504588. Source: UniProtKB

mammary duct terminal end bud growth

Inferred from electronic annotation. Source: Ensembl

negative regulation of chemokine-mediated signaling pathway

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

negative regulation of mammary gland epithelial cell proliferation

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

negative regulation of negative chemotaxis

Inferred from direct assay PubMed 11748139. Source: UniProtKB

positive regulation of axonogenesis

Inferred from direct assay PubMed 12504588. Source: UniProtKB

   Cellular_componentaxolemma

Inferred from electronic annotation. Source: Ensembl

cell surface

Inferred from direct assay PubMed 12504588. Source: UniProtKB

cytoplasm

Inferred from direct assay PubMed 18566128. Source: UniProtKB

integral component of plasma membrane

Traceable author statement Ref.7. Source: ProtInc

   Molecular_functionaxon guidance receptor activity

Traceable author statement Ref.1. Source: ProtInc

identical protein binding

Inferred from direct assay PubMed 12504588. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 6 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9Y6N7-1)

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: Q9Y6N7-2)

The sequence of this isoform differs from the canonical sequence as follows:
     543-543: Q → QGKVN
Note: Incomplete.
Isoform 3 (identifier: Q9Y6N7-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-39: Missing.
     40-57: HGTPIPTSDNDDNSLGYT → MIAEPAHFYLFGLICLCS
     348-348: Q → QVGS
Isoform 4 (identifier: Q9Y6N7-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-39: Missing.
     40-57: HGTPIPTSDNDDNSLGYT → MIAEPAHFYLFGLICLCS
Isoform 5 (identifier: Q9Y6N7-5)

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.
Isoform 6 (identifier: Q9Y6N7-6)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2525 Potential
Chain26 – 16511626Roundabout homolog 1
PRO_0000031033

Regions

Topological domain26 – 897872Extracellular Potential
Transmembrane898 – 91821Helical; Potential
Topological domain919 – 1651733Cytoplasmic Potential
Domain68 – 16497Ig-like C2-type 1
Domain170 – 25788Ig-like C2-type 2
Domain262 – 34685Ig-like C2-type 3
Domain351 – 44696Ig-like C2-type 4
Domain455 – 54187Ig-like C2-type 5
Domain563 – 65795Fibronectin type-III 1
Domain676 – 77398Fibronectin type-III 2
Domain778 – 87497Fibronectin type-III 3

Amino acid modifications

Modified residue9401Phosphoserine Ref.13 Ref.14
Modified residue10381Phosphotyrosine; by ABL; in vitro Ref.9
Modified residue10551Phosphoserine Ref.13
Modified residue10731Phosphotyrosine; by ABL; in vitro Ref.9
Modified residue11141Phosphotyrosine; by ABL; in vitro Ref.9
Modified residue12401Phosphothreonine Ref.13
Modified residue12971Phosphoserine Ref.13
Glycosylation1601N-linked (GlcNAc...) Potential
Glycosylation4631N-linked (GlcNAc...) Potential
Glycosylation7901N-linked (GlcNAc...) Potential
Glycosylation8201N-linked (GlcNAc...) Potential
Glycosylation8271N-linked (GlcNAc...) Potential
Disulfide bond89 ↔ 147 Ref.16
Disulfide bond191 ↔ 240 Potential
Disulfide bond283 ↔ 330 Potential
Disulfide bond372 ↔ 428 Potential
Disulfide bond476 ↔ 525 Potential

Natural variations

Alternative sequence1 – 5757MKWKH…SLGYT → MIAEPAHFYLFGLICLCS in isoform 5 and isoform 6.
VSP_043881
Alternative sequence1 – 3939Missing in isoform 3 and isoform 4.
VSP_010643
Alternative sequence40 – 5718HGTPI…SLGYT → MIAEPAHFYLFGLICLCS in isoform 3 and isoform 4.
VSP_010644
Alternative sequence3481Q → QVGS in isoform 3, isoform 5 and isoform 6.
VSP_010645
Alternative sequence5431Q → QGKVN in isoform 2.
VSP_010646
Alternative sequence938 – 9469Missing in isoform 5 and isoform 6.
VSP_043882
Alternative sequence1013 – 106755Missing in isoform 6.
VSP_046084
Natural variant3361V → A.
Corresponds to variant rs9647397 [ dbSNP | Ensembl ].
VAR_053640
Natural variant10551S → N in a breast cancer sample. Ref.11
VAR_019071
Natural variant10911S → N.
Corresponds to variant rs35456279 [ dbSNP | Ensembl ].
VAR_053641
Natural variant15331E → D in a breast cancer sample. Ref.11
Corresponds to variant rs36055689 [ dbSNP | Ensembl ].
VAR_019072

Experimental info

Sequence conflict1821A → V in AAI15023. Ref.4
Sequence conflict8351F → L in AAI15023. Ref.4
Sequence conflict10951G → S in CAD98093. Ref.5
Sequence conflict12231M → T in Z95705. Ref.2
Sequence conflict14431P → L in CAD98093. Ref.5
Sequence conflict15361D → G in Z95705. Ref.2

Secondary structure

........................................................................................................ 1651
Helix Strand Turn

Details...

Sequences

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

Last modified November 1, 1999. Version 1.
Checksum: 9D98CD7CAB73074D

FASTA1,651180,930
        10         20         30         40         50         60 
MKWKHVPFLV MISLLSLSPN HLFLAQLIPD PEDVERGNDH GTPIPTSDND DNSLGYTGSR 

        70         80         90        100        110        120 
LRQEDFPPRI VEHPSDLIVS KGEPATLNCK AEGRPTPTIE WYKGGERVET DKDDPRSHRM 

       130        140        150        160        170        180 
LLPSGSLFFL RIVHGRKSRP DEGVYVCVAR NYLGEAVSHN ASLEVAILRD DFRQNPSDVM 

       190        200        210        220        230        240 
VAVGEPAVME CQPPRGHPEP TISWKKDGSP LDDKDERITI RGGKLMITYT RKSDAGKYVC 

       250        260        270        280        290        300 
VGTNMVGERE SEVAELTVLE RPSFVKRPSN LAVTVDDSAE FKCEARGDPV PTVRWRKDDG 

       310        320        330        340        350        360 
ELPKSRYEIR DDHTLKIRKV TAGDMGSYTC VAENMVGKAE ASATLTVQEP PHFVVKPRDQ 

       370        380        390        400        410        420 
VVALGRTVTF QCEATGNPQP AIFWRREGSQ NLLFSYQPPQ SSSRFSVSQT GDLTITNVQR 

       430        440        450        460        470        480 
SDVGYYICQT LNVAGSIITK AYLEVTDVIA DRPPPVIRQG PVNQTVAVDG TFVLSCVATG 

       490        500        510        520        530        540 
SPVPTILWRK DGVLVSTQDS RIKQLENGVL QIRYAKLGDT GRYTCIASTP SGEATWSAYI 

       550        560        570        580        590        600 
EVQEFGVPVQ PPRPTDPNLI PSAPSKPEVT DVSRNTVTLS WQPNLNSGAT PTSYIIEAFS 

       610        620        630        640        650        660 
HASGSSWQTV AENVKTETSA IKGLKPNAIY LFLVRAANAY GISDPSQISD PVKTQDVLPT 

       670        680        690        700        710        720 
SQGVDHKQVQ RELGNAVLHL HNPTVLSSSS IEVHWTVDQQ SQYIQGYKIL YRPSGANHGE 

       730        740        750        760        770        780 
SDWLVFEVRT PAKNSVVIPD LRKGVNYEIK ARPFFNEFQG ADSEIKFAKT LEEAPSAPPQ 

       790        800        810        820        830        840 
GVTVSKNDGN GTAILVSWQP PPEDTQNGMV QEYKVWCLGN ETRYHINKTV DGSTFSVVIP 

       850        860        870        880        890        900 
FLVPGIRYSV EVAASTGAGS GVKSEPQFIQ LDAHGNPVSP EDQVSLAQQI SDVVKQPAFI 

       910        920        930        940        950        960 
AGIGAACWII LMVFSIWLYR HRKKRNGLTS TYAGIRKVPS FTFTPTVTYQ RGGEAVSSGG 

       970        980        990       1000       1010       1020 
RPGLLNISEP AAQPWLADTW PNTGNNHNDC SISCCTAGNG NSDSNLTTYS RPADCIANYN 

      1030       1040       1050       1060       1070       1080 
NQLDNKQTNL MLPESTVYGD VDLSNKINEM KTFNSPNLKD GRFVNPSGQP TPYATTQLIQ 

      1090       1100       1110       1120       1130       1140 
SNLSNNMNNG SGDSGEKHWK PLGQQKQEVA PVQYNIVEQN KLNKDYRAND TVPPTIPYNQ 

      1150       1160       1170       1180       1190       1200 
SYDQNTGGSY NSSDRGSSTS GSQGHKKGAR TPKVPKQGGM NWADLLPPPP AHPPPHSNSE 

      1210       1220       1230       1240       1250       1260 
EYNISVDESY DQEMPCPVPP ARMYLQQDEL EEEEDERGPT PPVRGAASSP AAVSYSHQST 

      1270       1280       1290       1300       1310       1320 
ATLTPSPQEE LQPMLQDCPE ETGHMQHQPD RRRQPVSPPP PPRPISPPHT YGYISGPLVS 

      1330       1340       1350       1360       1370       1380 
DMDTDAPEEE EDEADMEVAK MQTRRLLLRG LEQTPASSVG DLESSVTGSM INGWGSASEE 

      1390       1400       1410       1420       1430       1440 
DNISSGRSSV SSSDGSFFTD ADFAQAVAAA AEYAGLKVAR RQMQDAAGRR HFHASQCPRP 

      1450       1460       1470       1480       1490       1500 
TSPVSTDSNM SAAVMQKTRP AKKLKHQPGH LRRETYTDDL PPPPVPPPAI KSPTAQSKTQ 

      1510       1520       1530       1540       1550       1560 
LEVRPVVVPK LPSMDARTDR SSDRKGSSYK GREVLDGRQV VDMRTNPGDP REAQEQQNDG 

      1570       1580       1590       1600       1610       1620 
KGRGNKAAKR DLPPAKTHLI QEDILPYCRP TFPTSNNPRD PSSSSSMSSR GSGSRQREQA 

      1630       1640       1650 
NVGRRNIAEM QVLGGYERGE DNNEELEETE S 

« Hide

Isoform 2 [UniParc].

Checksum: EB2C3DFF6013A30F
Show »

FASTA1,655181,328
Isoform 3 [UniParc].

Checksum: 66D6413527161E25
Show »

FASTA1,615176,814
Isoform 4 [UniParc].

Checksum: 4625E96485E88C34
Show »

FASTA1,612176,571
Isoform 5 [UniParc].

Checksum: 79FA0AA96275B1A2
Show »

FASTA1,606175,836
Isoform 6 [UniParc].

Checksum: 89F1C62C15B8C9A2
Show »

FASTA1,551169,661

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]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 (SEP-2005) to the EMBL/GenBank/DDBJ databases
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]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
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]"Homozygous deletions at 3p12 in breast and lung cancer."
Sundaresan V., Chung G., Heppell-Parton A., Xiong J., Grundy C., Roberts I., James L., Cahn A., Bench A., Douglas J., Minna J., Sekido Y., Lerman M., Latif F., Bergh J., Li H., Lowe N., Ogilvie D., Rabbitts P.
Oncogene 17:1723-1729(1998) [PubMed] [Europe PMC] [Abstract]
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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"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 61-166 IN COMPLEX WITH SLIT2, DISULFIDE BOND.
[17]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_001139317.1. NM_001145845.1.
NP_002932.1. NM_002941.3.
NP_598334.2. NM_133631.3.
UniGeneHs.744218.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2EO9NMR-A454-564[»]
2V9QX-ray2.50A61-266[»]
2V9RX-ray2.00A61-266[»]
2V9TX-ray1.70A61-166[»]
4HLJX-ray1.80A660-897[»]
ProteinModelPortalQ9Y6N7.
SMRQ9Y6N7. Positions 61-266, 454-564.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112018. 5 interactions.
DIPDIP-33034N.
IntActQ9Y6N7. 3 interactions.
MINTMINT-1392694.
STRING9606.ENSP00000381450.

PTM databases

PhosphoSiteQ9Y6N7.

Polymorphism databases

DMDM49036500.

Proteomic databases

PaxDbQ9Y6N7.
PRIDEQ9Y6N7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000436010; ENSP00000406043; ENSG00000169855. [Q9Y6N7-4]
ENST00000464233; ENSP00000420321; ENSG00000169855. [Q9Y6N7-1]
ENST00000467549; ENSP00000417992; ENSG00000169855. [Q9Y6N7-6]
ENST00000495273; ENSP00000420637; ENSG00000169855. [Q9Y6N7-5]
GeneID6091.
KEGGhsa:6091.
UCSCuc003dqb.2. human. [Q9Y6N7-4]
uc003dqd.2. human. [Q9Y6N7-5]
uc003dqe.2. human. [Q9Y6N7-1]

Organism-specific databases

CTD6091.
GeneCardsGC03M078729.
HGNCHGNC:10249. ROBO1.
HPACAB013524.
MIM602430. gene.
neXtProtNX_Q9Y6N7.
PharmGKBPA34620.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG238978.
HOGENOMHOG000010267.
HOVERGENHBG073476.
InParanoidQ9Y6N7.
KOK06753.
OMAEDTQNGM.
OrthoDBEOG7KWSGP.
TreeFamTF351053.

Enzyme and pathway databases

ReactomeREACT_111045. Developmental Biology.

Gene expression databases

ArrayExpressQ9Y6N7.
BgeeQ9Y6N7.
CleanExHS_ROBO1.
GenevestigatorQ9Y6N7.

Family and domain databases

Gene3D2.60.40.10. 9 hits.
InterProIPR003961. Fibronectin_type3.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003598. Ig_sub2.
IPR003596. Ig_V-set_subgr.
[Graphical view]
PfamPF00041. fn3. 3 hits.
PF07679. I-set. 5 hits.
[Graphical view]
SMARTSM00060. FN3. 3 hits.
SM00408. IGc2. 4 hits.
SM00406. IGv. 1 hit.
[Graphical view]
SUPFAMSSF49265. SSF49265. 2 hits.
PROSITEPS50853. FN3. 3 hits.
PS50835. IG_LIKE. 5 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSROBO1. human.
EvolutionaryTraceQ9Y6N7.
GeneWikiROBO1.
GenomeRNAi6091.
NextBio23685.
PROQ9Y6N7.
SOURCESearch...

Entry information

Entry nameROBO1_HUMAN
AccessionPrimary (citable) accession number: Q9Y6N7
Secondary accession number(s): B2RXI1 expand/collapse secondary AC list , D3DU36, E9PD49, Q1RMC7, Q7Z300, Q9BUS7
Entry history
Integrated into UniProtKB/Swiss-Prot: June 21, 2004
Last sequence update: November 1, 1999
Last modified: March 19, 2014
This is version 123 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 3

Human chromosome 3: entries, gene names and cross-references to MIM