SynDB Home Page
SynDB Home Page

blue bulletSynDB protein details  

Parse error: syntax error, unexpected T_VARIABLE in /home/kongl/syndb/www/sdb_nats.php on line 52
0SNIP1_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
DescriptionSmad nuclear interacting protein 1.
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
Domain Architecture (Details)
InterPro domains unassigned to SynO:
The forkhead-associated (FHA) domain is a phosphopeptide recognition domain found in many regulatory proteins. It displays specificity for phosphothreonine-containing epitopes but will also recognise phosphotyrosine with relatively high affinity. It spans approximately 80-100 amino acid residues folded into an 11-stranded beta sandwich.hich sometimes contain small helical insertions between the loops connecting the strands . To date.enes encoding FHA-containing proteins have been identified in eubacterial and eukaryotic but not archaeal genomes. The domain is present in a diverse range of proteins.uch as kinases.hosphatases.inesins.ranscription factors.NA-binding proteins and metabolic enzymes which partake in many different cellular processes - DNA repair.ignal transduction.esicular transport and protein degradation are just a few examples.
FHA and SMAD (MH2) domains share a common structure consisting of a sandwich of eleven beta strands in two sheets with Greek key topology. Forkhead-associated (FHA) domains were originally identified as a sequence profile of about 75 amino acids.hereas the full-length domain is closer to about 150 amino acids. FHA domains are found in transcription factors.inesin motors.nd in a variety of other signalling molecules in organisms ranging from eubacteria to humans. FHA domains are protein-protein interaction domains that are specific for phosphoproteins. FHA-containing proteins function in maintaining cell-cycle checkpoints.NA repair and transcriptional regulation. FHA domain proteins include the Chk2/Rad53/Cds1 family of proteins that contain one or more FHA domains.s well as a Ser/Thr kinase domain . SMAD domain proteins are found in a range of species from nematodes to humans. These highly conserved proteins contain an N-terminal MH1 domain that contacts DNA.nd is separated by a short linker region from the C-terminal MH2 domain.he later showing a striking similarity to FHA domains. SMAD proteins mediate signalling by the TGF-beta/activin/BMP-2/4 cytokines from receptor Ser/Thr protein kinases at the cell surface to the nucleus. SMAD proteins fall into three functional classes: the receptor-regulated SMADs (R-SMADs).ncluding SMAD1.2.3.5.nd -8.ach of which is involved in a ligand-specific signalling pathway ; the comediator SMADs (co-SMADs).ncluding SMAD4.hich interact with R-SMADs to participate in signalling ; and the inhibitory SMADs (I-SMADs).ncluding SMAD6 and -7.hich block the activation of R-SMADs and Co-SMADs.hereby negatively regulating signalling pathways . The SSF signature in this entry is currently under review. Please be aware that some of the protein hits may be false positives.
SequencesProtein: SNIP1_HUMAN (396 aa)
mRNA: NM_024700
Local Annotation
Synapse Ontology
calcium-regulated transcription factor
sdb:0215 calcium-regulated transcription factor  (Evidence:keywords)
KO assignmentNot mapped to KEGG
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 490 residues, 37774731-37776200Exon2: 201 residues, 37778344-37778943Exon3: 36 residues, 37790832-37790935Exon4: 101 residues, 37792193-37792490Exon5: 2 residues, -Jump to SNIP1_HUMAN  
Tune and view alternative isoforms