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0HIP1R_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
DescriptionHuntingtin-interacting protein 1-related protein (hip1-related) (hip 12).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0030136 clathrin-coated vesicle (NAS)
0005905 coated pit (NAS)
0003779 actin binding (NAS)

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schematic display of those terms with internal associations, click the node and browse the corresponding GO term
Domain Architecture (Details)
InterPro domains assigned to SynO:
AP180 is an endocytotic accessory protein that has been implicated in the formation of clathrin-coated pits. The domain is involved in phosphatidylinositol 4.-bisphosphate binding and is a universal adaptor for nucleation of clathrin coats .
Clathrin-mediated endocytosis plays a major role in retrieving synaptic vesicles from the plasma membrane following exocytosis. This endocytic process requires the clathrin coat assembly protein AP180 (or a homologue).hich promotes the assembly and restricts the size of clathrin-coated vesicles. The highly conserved 33 kDa amino-terminal domain of AP180 plays a critical role in binding to phosphoinositides and in regulating the clathrin assembly activity of AP180. The crystal structure of the amino-terminal domain reveals a novel fold consisting of a large double layer of sheets of ten alpha helices and a unique site for binding phosphoinositides. The clathrin-box motif is mostly buried and lies in a helix that participates in an intramolecular leucine zipper and a three-helix coiled coil .
  IPR008943:Phosphoinositide-binding clathrin adaptor, N-terminal
InterPro domains unassigned to SynO:
I/LWEQ domains bind to actin. It has been shown that the I/LWEQdomains from mouse talin and yeast Sla2p interact with F-actin . The domain has four conserved blocks.he name of the domain is derived from the initial conserved amino acid ofeach of the four blocks . I/LWEQ domains can beplaced into four major groups based on sequence similarity:Metazoan talin.Dictyostelium discoideum TalA/TalB and SLA110.Metazoan Hip1p .Saccharomyces cerevisiae Sla2p .
Tropomyosins .re a family of closely related proteins present in muscle and non-muscle cells. In striated muscle.ropomyosin mediate the interactions between the troponin complex and actin so as to regulate muscle contraction . The role of tropomyosin in smooth muscle and non-muscle tissues is not clear. Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites . There are multiple cell-specific isoforms.reated by differential splicing of the messenger RNA from one gene.ut the proportions of the isoforms vary between different cell types. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region.hereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.Some of the proteins in this family are allergens. Allergies are hypersensitivity reactions of the immune system to specific substances called allergens (such as pollen.tings.rugs.r food) that.n most people.esult in no symptoms. A nomenclature system has been established for antigens (allergens) that cause IgE-mediated atopic allergies in humans [WHO/IUIS Allergen Nomenclature Subcommittee King T.P..offmann D..oewenstein H..arsh D.G..latts-Mills T.A.E..homas W. Bull. World Health Organ. 72:797-806(1994)]. This nomenclature system is defined by a designation that is composed ofthe first three letters of the genus; a space; the first letter of thespecies name; a space and an arabic number. In the event that two speciesnames have identical designations.hey are discriminated from one anotherby adding one or more letters (as necessary) to each species designation. The allergens in this family include allergens with the following designations: Met e 1.
The ENTH (Epsin N-terminal homology) domain is approximately 150 amino acids in length and is always found located at the N-termini of proteins. The domain forms a compact globular structure.omposed of 9 alpha-helices connected by loops of varying length. The general topology is determined by three helical hairpins that are stacked consecutively with a right hand twist . An N-terminal helix folds back.orming a deep basic groove thatforms the binding pocket for the Ins(1..)P3 ligand . The ligand is coordinated by residues from surrounding alpha-helices and all three phosphates are multiply coordinated. The coordination of Ins(1..)P3 suggests that ENTH is specific for particular head groups. Proteins containing this domain have been found to bind PtdIns(4.)P2 and PtdIns(1..)P3 suggesting that the domain may be a membrane interacting module. The main function of proteins containing this domain appears to be to act as accessory clathrin adaptors in endocytosis.psin is able to recruit and promote clathrin polymerisation ona lipid monolayer.ut may have additional roles in signalling and actin regulation . Epsin causes a strong degree of membrane curvature andtubulation.ven fragmentation of membranes with a high PtdIns(4.)P2 content. Epsin binding tomembranes facilitates their deformation by insertion of the N-terminal helix into the outer leaflet of the bilayer.ushing the head groupsapart. This would reduce the energy needed to curve the membrane into a vesicle.aking it easier for the clathrin cage tofix and stabilise the curved membrane. This points to a pioneering role for epsin in vesiclebudding as it provides both a driving force and a link between membrane invagination and clathrin polymerisation.
  IPR013809:Epsin-like, N-terminal
SequencesProtein: HIP1R_HUMAN (1068 aa)
mRNA: NM_003959
Local Annotation
Synapse Ontology
the clathrin located in the surface of the endocytotic intermediate.
sdb:0115 clathrin-coated pit  (Evidence:keywords,domains)
endocytotic reaction via coated pits
sdb:0119 endocytotic reaction  (Evidence:keywords,domains)
clathrin-coat uncoating means clathrin was shed from the budding vesicle membrane.
sdb:0122 clathrin-coat uncoating  (Evidence:keywords,domains)
the molecules that link the clathrin lattice to the membrane.
sdb:0259 clathrin adapter  (Evidence:keywords,domains)
sdb:0260 coat recruitment  (Evidence:keywords,domains)
all the components of the clathrin coat, major ones are clathrin and clathrin adaptors.
sdb:0261 clathrin coat component  (Evidence:keywords,domains)
Calcium release from RyR (Ryanodine Receptor) in the SR (Sarcoplasmic Reticulum) is activated by the calcium induced-calcium-release
sdb:0325 RyR-CICR  (Evidence:keywords,domains)
sdb:0329 actin in synaptic vesicle cycling  (Evidence:keywords,domains)
KO assignmentNot mapped to KEGG
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 51 residues, 121885991-121886143Exon2: 23 residues, 121898530-121898594Exon3: 49 residues, 121898965-121899108Exon4: 21 residues, 121899295-121899352Exon5: 29 residues, 121900374-121900455Exon6: 27 residues, 121901334-121901411Exon7: 22 residues, 121901735-121901797Exon8: 49 residues, 121904542-121904683Exon9: 21 residues, 121905404-121905462Exon10: 27 residues, 121905552-121905628Exon11: 49 residues, 121905764-121905905Exon12: 22 residues, 121906050-121906112Exon13: 26 residues, 121906330-121906403Exon14: 63 residues, 121906479-121906663Exon15: 31 residues, 121906755-121906844Exon16: 41 residues, 121906931-121907048Exon17: 36 residues, 121907124-121907226Exon18: 67 residues, 121907520-121907715Exon19: 51 residues, 121908601-121908749Exon20: 31 residues, 121908848-121908935Exon21: 38 residues, 121909337-121909445Exon22: 47 residues, 121909560-121909697Exon23: 39 residues, 121909925-121910036Exon24: 21 residues, 121910271-121910330Exon25: 12 residues, 121910546-121910577Exon26: 23 residues, 121910647-121910710Exon27: 35 residues, 121910922-121911023Exon28: 37 residues, 121911178-121911284Exon29: 43 residues, 121911415-121911539Exon30: 22 residues, 121911630-121911692Exon31: 71 residues, 121911807-121912014Exon32: 420 residues, 121912205-121913460Exon33: 2 residues, -Jump to HIP1R_HUMAN  
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Loci Cluster (Details)Loci: 4084 121282046-121316970 ~-35K 9906(VPS33A)(-)Loci: 2797 121577761-121676899 ~-99K 9919(KNTC1)(+)Loci: 2798 121885991-121913460 ~-27K 9929(HIP1R)(+)Loci: 4083 121258162-121276552 ~-18K 9902(DIABLO)(-)Link out to UCSC