SynDB Home Page
SynDB Home Page
Browse
Search
Download
Help
People
links

blue bulletSynDB protein details  


Parse error: syntax error, unexpected T_VARIABLE in /home/kongl/syndb/www/sdb_nats.php on line 52
0ROBO2_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameROBO2
DescriptionRoundabout homolog 2 precursor.
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0009986 cell surface (IDA)
0008046 axon guidance receptor activity (NAS)
0042802 protein self binding (IDA)
0007420 brain development (IEP)
0007156 homophilic cell adhesion (IDA)
0050772 positive regulation of axonogenesis (IDA)
0001657 ureteric bud development (IMP)

Warning: fopen(/home/kongl/syndb/www/temp/1181616285.dot) [function.fopen]: failed to open stream: Permission denied in /home/kongl/syndb/www/sdb_pro.php on line 269

Warning: fwrite(): supplied argument is not a valid stream resource in /home/kongl/syndb/www/sdb_pro.php on line 270

Warning: fwrite(): supplied argument is not a valid stream resource in /home/kongl/syndb/www/sdb_pro.php on line 271

Warning: fwrite(): supplied argument is not a valid stream resource in /home/kongl/syndb/www/sdb_pro.php on line 272

Warning: fwrite(): supplied argument is not a valid stream resource in /home/kongl/syndb/www/sdb_pro.php on line 273

Warning: fwrite(): supplied argument is not a valid stream resource in /home/kongl/syndb/www/sdb_pro.php on line 274

Warning: fwrite(): supplied argument is not a valid stream resource in /home/kongl/syndb/www/sdb_pro.php on line 299

Warning: fclose(): supplied argument is not a valid stream resource in /home/kongl/syndb/www/sdb_pro.php on line 300
schematic display of those terms with internal associations, click the node and browse the corresponding GO term
Domain Architecture (Details)
InterPro domains unassigned to SynO:
Fibronectins are multi-domain glycoproteins found in a soluble form in plasma.nd in an insoluble form in loose connective tissue and basement membranes . They contain multiple copies of 3 repeat regions (types I.I and III).hich bind to a variety of substances including heparin.ollagen.NA.ctin.ibrin and fibronectin receptors on cell surfaces. The wide variety of these substances means that fibronectins are involved in a number of important functions: e.g..ound healing; cell adhesion; blood coagulation; cell differentiation and migration; maintenance of the cellular cytoskeleton; and tumour metastasis . The role of fibronectin in cell differentiation is demonstrated by the marked reduction in the expression of its gene when neoplastic transformation occurs. Cell attachment has been found to be mediated by the binding of the tetrapeptide RGDS to integrins on the cell surface .lthough related sequences can also display cell adhesion activity.Plasma fibronectin occurs as a dimer of 2 different subunits.inked together by 2 disulphide bonds near the C-terminus. The difference in the 2 chains occurs in the type III repeat region and is caused by alternative splicing of the mRNA from one gene . The observation that.n a given protein.n individual repeat of one of the 3 types (e.g..he first FnIII repeat) shows much less similarity to its subsequent tandem repeats within that protein than to its equivalent repeat between fibronectins from other species.as suggested that the repeating structure of fibronectin arose at an early stage of evolution. It also seems to suggest that the structure is subject to high selective pressure .The fibronectin type III repeat region is an approximately 100 amino acid domain.ifferent tandem repeats of which contain binding sites for DNA.eparin and the cell surface . The superfamily of sequences believed to contain FnIII repeats represents 45 different families.he majority of which are involved in cell surface binding in some manner.r are receptor protein tyrosine kinases.r cytokine receptors.
  IPR003961:Fibronectin, type III
The basic structure of immunoglobulin (Ig) molecules is a tetramer of two light chains and two heavy chains linked by disulfide bonds. There are two types of light chains: kappa and lambda.ach composed of a constant domain (CL) and a variable domain (VL). There are five types of heavy chains: alpha.elta.psilon.amma and mu.ll consisting of a variable domain (VH) and three (in alpha.elta and gamma) or four (in epsilon and mu) constant domains (CH1 to CH4). Ig molecules are highly modular proteins.n which the variable and constant domains have clear.onserved sequence patterns. The domains in Ig and Ig-like molecules are grouped into four types: V-set (variable; ).1-set (constant-1; ).2-set (constant-2; ) and I-set (intermediate; ) . Structural studies have shown that these domains share a common core Greek-key beta-sandwich structure.ith the types differing in the number of strands in the beta-sheets as well as in their sequence patterns .Immunoglobulin-like domains that are related in both sequence and structure can be found in several diverse protein families. Ig-like domains are involved in a variety of functions.ncluding cell-cell recognition.ell-surface receptors.uscle structure and the immune system . This entry represents I-set domains.hich are found in several cell adhesion molecules.ncluding vascular (VCAM).ntercellular (ICAM).eural (NCAM) and mucosal addressin (MADCAM) cell adhesion molecules.s well as junction adhesion molecules (JAM). I-set domains are also present in several other diverse protein families.ncluding several tyrosine-protein kinase receptors.he hemolymph protein hemolin.he muscle proteins titin.elokin.nd twitchin.he neuronal adhesion molecule axonin-1 .nd the signalling molecule semaphorin 4D that is involved in axonal guidance.mmune function and angiogenesis .
  IPR013098:Immunoglobulin I-set
The basic structure of immunoglobulin (Ig) molecules is a tetramer of two light chains and two heavy chains linked by disulfide bonds. There are two types of light chains: kappa and lambda.ach composed of a constant domain (CL) and a variable domain (VL). There are five types of heavy chains: alpha.elta.psilon.amma and mu.ll consisting of a variable domain (VH) and three (in alpha.elta and gamma) or four (in epsilon and mu) constant domains (CH1 to CH4). Ig molecules are highly modular proteins.n which the variable and constant domains have clear.onserved sequence patterns. The domains in Ig and Ig-like molecules are grouped into four types: V-set (variable; ).1-set (constant-1; ).2-set (constant-2; ) and I-set (intermediate; ) . Structural studies have shown that these domains share a common core Greek-key beta-sandwich structure.ith the types differing in the number of strands in the beta-sheets as well as in their sequence patterns .Immunoglobulin-like domains that are related in both sequence and structure can be found in several diverse protein families. Ig-like domains are involved in a variety of functions.ncluding cell-cell recognition.ell-surface receptors.uscle structure and the immune system . This entry represents a subtype of the immunoglobulin domain.nd is found in a diverse range of protein families that includes glycoproteins.ibroblast growth factor receptors.ascular endothelial growth factor receptors.nterleukin-6 receptor.nd neural cell adhesion molecules. It also includes proteins that are classified as unassigned proteinase inhibitors belonging to MEROPS inhibitor families I2.17 and I43 .
  IPR003598:Immunoglobulin subtype 2
Fibronectin is composed of three repeating structural motifs.f which one is the FnIII module. The three modules form a linear sequence of multiple tandem copies connected by short linker peptides. The secondary structure of the FnIII10 module.hich is the only fibronectin module to possess an integrin binding RGD motif.onsists of two beta-sheets containing the antiparallel beta-strands ABE and DCFG.espectively.hich fold up to form a beta-sandwich. The RGD sequence is located in the loop connecting the beta-strands .The SSF signature in this entry is currently under review. Please be aware that some of the protein hits may be false positives.
  IPR008957:Fibronectin, type III-like fold
Neural cell adhesion molecules (NCAM) are cell surface glycoproteins thatshare structural motifs related to immunoglobulin (Ig) and fibronectin typeIII (FNIII) domains. Expressed in neurons.lial cells and skeletal muscle.CAM binds both homophilically and heterophilically.ediating processessuch as neural cell growth and migration . Polysialic acid binds toN-glycosylation sites in the Ig domains.ffecting the binding of NCAM.Decreasing levels of sialynation on NCAM promotes aggregation.nd isthought to be important in regulation of tissue stability .The full length transcript contains (from N-terminus to C-terminus) five Igdomains.wo FNIII domains. transmembrane (TM) region and a cytosolicdomain. Alternative splicing is known to generate at least four productswith (apparent desialylated) molecular weights of 180.40.20 and 105kDa.The longer TM products are expressed in neurons (180 and 140kDa) and glialcells (140 kDa).hereas the 120kDa product is GPI-anchored on the surfaceof myotubes and the 105kDa product is secreted (for review see ).Further splice variation arises from a variable alternatively spliced exon (VASE) in the fourth Ig domain and a muscle-specific domain (MSD) betweenthe two FNIII domains containing an O-glycosylation site.
  IPR009138:Neural cell adhesion
This entry represents domains with an immunoglobulin-like (Ig-like) fold.hich consists of a beta-sandwich of seven or more strands in two sheets with a Greek-key topology. Ig-like domains are one of the most common protein modules found in animals.ccurring in a variety of different proteins. These domains are often involved in interactions.ommonly with other Ig-like domains via their beta-sheets . Domains within this fold-family share the same structure.ut can diverge with respect to their sequence. Based on sequence.g-like domains can be classified as V-set domains (antibody variable domain-like).1-set domains (antibody constant domain-like).2-set domains.nd I-set domains (antibody intermediate domain-like). Proteins can contain more than one of these types of Ig-like domains. For example.n the human T-cell receptor antigen CD2.omain 1 (D1) is a V-set domain.hile domain 2 (D2) is a C2-set domain.oth domains having the same Ig-like fold .Domains with an Ig-like fold can be found in many.iverse proteins in addition to immunoglobulin molecules. For example.g-like domains occur in several different types of receptors (such as various T-cell antigen receptors).everal cell adhesion molecules.HC class I and II antigens.s well as the hemolymph protein hemolin.nd the muscle proteins titin.elokin and twitchin.
  IPR013783:Immunoglobulin-like fold
IPR013098:I-set 
Evalue:-30.6575775146484 
Location:225-310IPR013783:Ig-like_fold 
Evalue:-22.6989707946777 
Location:412-507IPR003961:fn3 
Evalue:-18.4685211181641 
Location:522-607IPR013098:I-set 
Evalue:-16.5850257873535 
Location:314-408IPR013098:I-set 
Evalue:-16 
Location:31-128IPR003961:fn3 
Evalue:-15.795880317688 
Location:736-826IPR013098:I-set 
Evalue:-10.1739253997803 
Location:133-221IPR003961:fn3 
Evalue:-6.46852111816406 
Location:648-713IPR008957:FN_III-like 
Evalue:0 
Location:14-23
SequencesProtein: ROBO2_HUMAN (1378 aa)
mRNA: NM_002942
Local Annotation
Synapse Ontology
A process that increases long-term neuronal synaptic plasticity, the ability of neuronal synapses to change long-term as circumstances require. Long-term neuronal synaptic plasticity generally involves increase or decrease in actual synapse numbers.
sdb:0039 positive regulation of long-term neuronal synaptic plasticity  (Evidence:keywords)
KO assignmentK06754
  Level 3 annotation:
    roundabout, axon guidance receptor, homolog 2 (Drosophila)
  Level 2 annotation:
    Cell adhesion molecules (CAMs)
    Axon guidance
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 23 residues, 77172620-77172687Exon2: 111 residues, 77229854-77230181Exon3: 54 residues, 77609254-77609412Exon4: 42 residues, 77612939-77613060Exon5: 48 residues, 77625084-77625223Exon6: 44 residues, 77654615-77654743Exon7: 43 residues, 77678178-77678303Exon8: 59 residues, 77682658-77682830Exon9: 70 residues, 77689784-77689990Exon10: 29 residues, 77694491-77694573Exon11: 56 residues, 77695007-77695170Exon12: 57 residues, 77696794-77696961Exon13: 42 residues, 77700153-77700275Exon14: 79 residues, 77706339-77706571Exon15: 43 residues, 77709330-77709455Exon16: 59 residues, 77711787-77711959Exon17: 63 residues, 77720591-77720774Exon18: 16 residues, 77726982-77727025Exon19: 44 residues, 77728463-77728591Exon20: 96 residues, 77734050-77734332Exon21: 54 residues, 77739638-77739795Exon22: 89 residues, 77749353-77749614Exon23: 70 residues, 77754067-77754273Exon24: 60 residues, 77766710-77766884Exon25: 69 residues, 77776544-77776745Exon26: 487 residues, 77777894-77779351Exon27: 2 residues, -Jump to ROBO2_HUMAN