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Q14643 (ITPR1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 159. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Inositol 1,4,5-trisphosphate receptor type 1
Alternative name(s):
IP3 receptor isoform 1
Short name=IP3R 1
Short name=InsP3R1
Type 1 inositol 1,4,5-trisphosphate receptor
Short name=Type 1 InsP3 receptor
Gene names
Name:ITPR1
Synonyms:INSP3R1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length2758 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Intracellular channel that mediates calcium release from the endoplasmic reticulum following stimulation by inositol 1,4,5-trisphosphate. Plays a role in ER stress-induced apoptosis. Cytoplasmic calcium released from the ER triggers apoptosis by the activation of CaM kinase II, eventually leading to the activation of downstream apoptosis pathways By similarity.

Subunit structure

Homotetramer. Interacts with TRPC4. The PPXXF motif binds HOM1, HOM2 and HOM3. Interacts with RYR1, RYR2, ITPR1, SHANK1 and SHANK3. Interacts with ERP44 in a pH-, redox state- and calcium-dependent manner which results in the inhibition the calcium channel activity. The strength of this interaction inversely correlates with calcium concentration. Part of cGMP kinase signaling complex at least composed of ACTA2/alpha-actin, CNN1/calponin H1, PLN/phospholamban, PRKG1 and ITPR1. Interacts with AHCYL1 By similarity. Interacts with MRVI1 and CABP1 (via N-terminus). Ref.7 Ref.8 Ref.9 Ref.11

Subcellular location

Endoplasmic reticulum membrane; Multi-pass membrane protein.

Tissue specificity

Widely expressed.

Domain

The receptor contains a calcium channel in its C-terminal extremity. Its large N-terminal cytoplasmic region has the ligand-binding site in the N-terminus and modulatory sites in the middle portion immediately upstream of the channel region.

Post-translational modification

Phosphorylated by cAMP kinase. Phosphorylation prevents the ligand-induced opening of the calcium channels By similarity. Ref.2

Phosphorylated on tyrosine residues. Ref.2

Ubiquitination at multiple lysines targets ITPR1 for proteasomal degradation. Approximately 40% of the ITPR1-associated ubiquitin is monoubiquitin, and polyubiquitins are both 'Lys-48'- and 'Lys-63'-linked By similarity.

Involvement in disease

Spinocerebellar ataxia 15 (SCA15) [MIM:606658]: Spinocerebellar ataxia is a clinically and genetically heterogeneous group of cerebellar disorders. Patients show progressive incoordination of gait and often poor coordination of hands, speech and eye movements, due to degeneration of the cerebellum with variable involvement of the brainstem and spinal cord. SCA15 is an autosomal dominant cerebellar ataxia (ADCA). It is very slow progressing form with a wide range of onset, ranging from childhood to adult. Most patients remain ambulatory.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.12 Ref.16

Spinocerebellar ataxia 29 (SCA29) [MIM:117360]: An autosomal dominant, congenital spinocerebellar ataxia characterized by early motor delay, hypotonia and mild cognitive delay. Affected individuals develop a very slowly progressive or non-progressive gait and limb ataxia associated with cerebellar atrophy on brain imaging. Additional variable features include nystagmus, dysarthria, and tremor.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.17

Miscellaneous

Calcium appears to inhibit ligand binding to the receptor, most probably by interacting with a distinct calcium-binding protein which then inhibits the receptor.

Sequence similarities

Belongs to the InsP3 receptor family.

Contains 5 MIR domains.

Caution

Alternative splice sites (AA 1053-1054) represent a non-canonical GA-AG donor-acceptor pair, but are well-supported by all available human transcripts, and by homologous transcripts in mouse, rat and cow.

Ontologies

Keywords
   Biological processApoptosis
Calcium transport
Ion transport
Transport
   Cellular componentEndoplasmic reticulum
Membrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
Neurodegeneration
Spinocerebellar ataxia
   DomainRepeat
Transmembrane
Transmembrane helix
   LigandCalcium
   Molecular functionCalcium channel
Ion channel
Ligand-gated ion channel
Receptor
   PTMGlycoprotein
Isopeptide bond
Phosphoprotein
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processFc-epsilon receptor signaling pathway

Traceable author statement. Source: Reactome

Fc-gamma receptor signaling pathway involved in phagocytosis

Traceable author statement. Source: Reactome

activation of phospholipase C activity

Traceable author statement. Source: Reactome

blood coagulation

Traceable author statement. Source: Reactome

calcium ion transport

Non-traceable author statement Ref.2. Source: UniProtKB

endoplasmic reticulum calcium ion homeostasis

Inferred from electronic annotation. Source: Ensembl

energy reserve metabolic process

Traceable author statement. Source: Reactome

epidermal growth factor receptor signaling pathway

Traceable author statement. Source: Reactome

fibroblast growth factor receptor signaling pathway

Traceable author statement. Source: Reactome

innate immune response

Traceable author statement. Source: Reactome

inositol phosphate-mediated signaling

Inferred from sequence or structural similarity. Source: GOC

intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress

Inferred from sequence or structural similarity. Source: UniProtKB

neurotrophin TRK receptor signaling pathway

Traceable author statement. Source: Reactome

platelet activation

Traceable author statement. Source: Reactome

post-embryonic development

Inferred from electronic annotation. Source: Ensembl

regulation of insulin secretion

Traceable author statement. Source: Reactome

release of sequestered calcium ion into cytosol

Inferred from sequence or structural similarity. Source: UniProtKB

response to hypoxia

Inferred from direct assay PubMed 19120137. Source: BHF-UCL

signal transduction

Non-traceable author statement Ref.6. Source: UniProtKB

small molecule metabolic process

Traceable author statement. Source: Reactome

voluntary musculoskeletal movement

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcalcineurin complex

Inferred from electronic annotation. Source: Ensembl

endoplasmic reticulum

Non-traceable author statement Ref.6. Source: UniProtKB

endoplasmic reticulum membrane

Traceable author statement. Source: Reactome

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

nuclear inner membrane

Inferred from electronic annotation. Source: Ensembl

nucleolus

Inferred from electronic annotation. Source: Ensembl

platelet dense granule membrane

Inferred from direct assay PubMed 10828023. Source: BHF-UCL

platelet dense tubular network

Inferred from direct assay PubMed 10828023. Source: BHF-UCL

platelet dense tubular network membrane

Traceable author statement. Source: Reactome

postsynaptic density

Inferred from electronic annotation. Source: Ensembl

sarcoplasmic reticulum

Inferred from electronic annotation. Source: Ensembl

   Molecular_functioncalcium ion transmembrane transporter activity

Traceable author statement Ref.4. Source: ProtInc

inositol 1,4,5-trisphosphate-sensitive calcium-release channel activity

Inferred from sequence or structural similarity. Source: UniProtKB

intracellular ligand-gated calcium channel activity

Inferred from sequence or structural similarity. Source: UniProtKB

phosphatidylinositol binding

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 8 isoforms produced by alternative splicing. [Align] [Select]

Note: There is a combination of three alternatively spliced domains at site SI, SIII and site SII (A and C). Experimental confirmation may be lacking for some isoforms.
Isoform 1 (identifier: Q14643-1)

Also known as: SISIIISIIAC;

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: Q14643-2)

Also known as: SI-SIIISIIAC;

The sequence of this isoform differs from the canonical sequence as follows:
     322-336: Missing.
Isoform 3 (identifier: Q14643-3)

Also known as: SISIII-SII;

The sequence of this isoform differs from the canonical sequence as follows:
     919-927: Missing.
     1702-1725: Missing.
     1726-1740: Missing.
Isoform 4 (identifier: Q14643-4)

Also known as: SI-SIII-SII;

The sequence of this isoform differs from the canonical sequence as follows:
     322-336: Missing.
     919-927: Missing.
     1702-1725: Missing.
     1726-1740: Missing.
Isoform 5 (identifier: Q14643-5)

Also known as: SI-SIII-SIIAC;

The sequence of this isoform differs from the canonical sequence as follows:
     322-336: Missing.
     919-927: Missing.
Isoform 6 (identifier: Q14643-6)

Also known as: SISIIISIIA;

The sequence of this isoform differs from the canonical sequence as follows:
     1726-1740: Missing.
Isoform 7 (identifier: Q14643-7)

Also known as: SI-SIII-SIIA;

The sequence of this isoform differs from the canonical sequence as follows:
     322-336: Missing.
     1726-1740: Missing.
Isoform 8 (identifier: Q14643-8)

Also known as: SI-SIII-SIIA;

The sequence of this isoform differs from the canonical sequence as follows:
     322-336: Missing.
     919-927: Missing.
     1726-1740: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 27582758Inositol 1,4,5-trisphosphate receptor type 1
PRO_0000153920

Regions

Topological domain1 – 22822282Cytoplasmic Potential
Transmembrane2283 – 230321Helical; Potential
Topological domain2304 – 231411Lumenal Potential
Transmembrane2315 – 233521Helical; Potential
Topological domain2336 – 236126Cytoplasmic Potential
Transmembrane2362 – 238221Helical; Potential
Topological domain2383 – 240523Lumenal Potential
Transmembrane2406 – 242621Helical; Potential
Topological domain2427 – 244822Cytoplasmic Potential
Transmembrane2449 – 246921Helical; Potential
Topological domain2470 – 2577108Lumenal Potential
Transmembrane2578 – 259821Helical; Potential
Topological domain2599 – 2758160Cytoplasmic Potential
Domain112 – 16655MIR 1
Domain173 – 22351MIR 2
Domain231 – 28757MIR 3
Domain294 – 37380MIR 4
Domain379 – 43557MIR 5
Region265 – 2695Inositol 1,4,5-trisphosphate binding By similarity
Region508 – 5114Inositol 1,4,5-trisphosphate binding By similarity
Region567 – 5693Inositol 1,4,5-trisphosphate binding By similarity
Region2472 – 253766Interaction with ERP44 By similarity

Amino acid modifications

Modified residue4821Phosphotyrosine Potential
Modified residue15981Phosphoserine Ref.10 Ref.13 Ref.15
Modified residue17641Phosphoserine Ref.13
Modified residue26641Phosphotyrosine Potential
Glycosylation25121N-linked (GlcNAc...) Ref.14
Cross-link917Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
Cross-link972Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
Cross-link1581Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
Cross-link1780Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
Cross-link1893Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
Cross-link1894Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
Cross-link1895Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
Cross-link1910Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
Cross-link1933Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
Cross-link2127Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
Cross-link2266Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity

Natural variations

Alternative sequence322 – 33615Missing in isoform 2, isoform 4, isoform 5, isoform 7 and isoform 8.
VSP_002687
Alternative sequence919 – 9279Missing in isoform 3, isoform 4, isoform 5 and isoform 8.
VSP_002688
Alternative sequence1702 – 172524Missing in isoform 3 and isoform 4.
VSP_002689
Alternative sequence1726 – 174015Missing in isoform 3, isoform 4, isoform 6, isoform 7 and isoform 8.
VSP_002690
Natural variant6021N → D in SCA29. Ref.17
VAR_069567
Natural variant7691M → V.
Corresponds to variant rs35789999 [ dbSNP | Ensembl ].
VAR_037005
Natural variant10591P → L in SCA15. Ref.16
VAR_069568
Natural variant14301I → V.
Corresponds to variant rs3749383 [ dbSNP | Ensembl ].
VAR_037006
Natural variant15621V → M in SCA29. Ref.17
VAR_069569

Experimental info

Sequence conflict1557 – 158125AIAIP…SIVQK → HCHSRGPGQPSQQPLSQVPQ HCAE in AAD14386. Ref.6
Sequence conflict23021F → L in AAB04947. Ref.2
Sequence conflict23051F → L in AAB04947. Ref.2
Sequence conflict24481S → A in U23850. Ref.4

Sequences

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

Last modified June 26, 2013. Version 3.
Checksum: D29B072252B0D8E7

FASTA2,758313,929
        10         20         30         40         50         60 
MSDKMSSFLH IGDICSLYAE GSTNGFISTL GLVDDRCVVQ PETGDLNNPP KKFRDCLFKL 

        70         80         90        100        110        120 
CPMNRYSAQK QFWKAAKPGA NSTTDAVLLN KLHHAADLEK KQNETENRKL LGTVIQYGNV 

       130        140        150        160        170        180 
IQLLHLKSNK YLTVNKRLPA LLEKNAMRVT LDEAGNEGSW FYIQPFYKLR SIGDSVVIGD 

       190        200        210        220        230        240 
KVVLNPVNAG QPLHASSHQL VDNPGCNEVN SVNCNTSWKI VLFMKWSDNK DDILKGGDVV 

       250        260        270        280        290        300 
RLFHAEQEKF LTCDEHRKKQ HVFLRTTGRQ SATSATSSKA LWEVEVVQHD PCRGGAGYWN 

       310        320        330        340        350        360 
SLFRFKHLAT GHYLAAEVDP DFEEECLEFQ PSVDPDQDAS RSRLRNAQEK MVYSLVSVPE 

       370        380        390        400        410        420 
GNDISSIFEL DPTTLRGGDS LVPRNSYVRL RHLCTNTWVH STNIPIDKEE EKPVMLKIGT 

       430        440        450        460        470        480 
SPVKEDKEAF AIVPVSPAEV RDLDFANDAS KVLGSIAGKL EKGTITQNER RSVTKLLEDL 

       490        500        510        520        530        540 
VYFVTGGTNS GQDVLEVVFS KPNRERQKLM REQNILKQIF KLLQAPFTDC GDGPMLRLEE 

       550        560        570        580        590        600 
LGDQRHAPFR HICRLCYRVL RHSQQDYRKN QEYIAKQFGF MQKQIGYDVL AEDTITALLH 

       610        620        630        640        650        660 
NNRKLLEKHI TAAEIDTFVS LVRKNREPRF LDYLSDLCVS MNKSIPVTQE LICKAVLNPT 

       670        680        690        700        710        720 
NADILIETKL VLSRFEFEGV SSTGENALEA GEDEEEVWLF WRDSNKEIRS KSVRELAQDA 

       730        740        750        760        770        780 
KEGQKEDRDV LSYYRYQLNL FARMCLDRQY LAINEISGQL DVDLILRCMS DENLPYDLRA 

       790        800        810        820        830        840 
SFCRLMLHMH VDRDPQEQVT PVKYARLWSE IPSEIAIDDY DSSGASKDEI KERFAQTMEF 

       850        860        870        880        890        900 
VEEYLRDVVC QRFPFSDKEK NKLTFEVVNL ARNLIYFGFY NFSDLLRLTK ILLAILDCVH 

       910        920        930        940        950        960 
VTTIFPISKM AKGEENKGNN DVEKLKSSNV MRSIHGVGEL MTQVVLRGGG FLPMTPMAAA 

       970        980        990       1000       1010       1020 
PEGNVKQAEP EKEDIMVMDT KLKIIEILQF ILNVRLDYRI SCLLCIFKRE FDESNSQTSE 

      1030       1040       1050       1060       1070       1080 
TSSGNSSQEG PSNVPGALDF EHIEEQAEGI FGGSEENTPL DLDDHGGRTF LRVLLHLTMH 

      1090       1100       1110       1120       1130       1140 
DYPPLVSGAL QLLFRHFSQR QEVLQAFKQV QLLVTSQDVD NYKQIKQDLD QLRSIVEKSE 

      1150       1160       1170       1180       1190       1200 
LWVYKGQGPD ETMDGASGEN EHKKTEEGNN KPQKHESTSS YNYRVVKEIL IRLSKLCVQE 

      1210       1220       1230       1240       1250       1260 
SASVRKSRKQ QQRLLRNMGA HAVVLELLQI PYEKAEDTKM QEIMRLAHEF LQNFCAGNQQ 

      1270       1280       1290       1300       1310       1320 
NQALLHKHIN LFLNPGILEA VTMQHIFMNN FQLCSEINER VVQHFVHCIE THGRNVQYIK 

      1330       1340       1350       1360       1370       1380 
FLQTIVKAEG KFIKKCQDMV MAELVNSGED VLVFYNDRAS FQTLIQMMRS ERDRMDENSP 

      1390       1400       1410       1420       1430       1440 
LMYHIHLVEL LAVCTEGKNV YTEIKCNSLL PLDDIVRVVT HEDCIPEVKI AYINFLNHCY 

      1450       1460       1470       1480       1490       1500 
VDTEVEMKEI YTSNHMWKLF ENFLVDICRA CNNTSDRKHA DSILEKYVTE IVMSIVTTFF 

      1510       1520       1530       1540       1550       1560 
SSPFSDQSTT LQTRQPVFVQ LLQGVFRVYH CNWLMPSQKA SVESCIRVLS DVAKSRAIAI 

      1570       1580       1590       1600       1610       1620 
PVDLDSQVNN LFLKSHSIVQ KTAMNWRLSA RNAARRDSVL AASRDYRNII ERLQDIVSAL 

      1630       1640       1650       1660       1670       1680 
EDRLRPLVQA ELSVLVDVLH RPELLFPENT DARRKCESGG FICKLIKHTK QLLEENEEKL 

      1690       1700       1710       1720       1730       1740 
CIKVLQTLRE MMTKDRGYGE KLISIDELDN AELPPAPDSE NATEELEPSP PLRQLEDHKR 

      1750       1760       1770       1780       1790       1800 
GEALRQVLVN RYYGNVRPSG RRESLTSFGN GPLSAGGPGK PGGGGGGSGS SSMSRGEMSL 

      1810       1820       1830       1840       1850       1860 
AEVQCHLDKE GASNLVIDLI MNASSDRVFH ESILLAIALL EGGNTTIQHS FFCRLTEDKK 

      1870       1880       1890       1900       1910       1920 
SEKFFKVFYD RMKVAQQEIK ATVTVNTSDL GNKKKDDEVD RDAPSRKKAK EPTTQITEEV 

      1930       1940       1950       1960       1970       1980 
RDQLLEASAA TRKAFTTFRR EADPDDHYQP GEGTQATADK AKDDLEMSAV ITIMQPILRF 

      1990       2000       2010       2020       2030       2040 
LQLLCENHNR DLQNFLRCQN NKTNYNLVCE TLQFLDCICG STTGGLGLLG LYINEKNVAL 

      2050       2060       2070       2080       2090       2100 
INQTLESLTE YCQGPCHENQ NCIATHESNG IDIITALILN DINPLGKKRM DLVLELKNNA 

      2110       2120       2130       2140       2150       2160 
SKLLLAIMES RHDSENAERI LYNMRPKELV EVIKKAYMQG EVEFEDGENG EDGAASPRNV 

      2170       2180       2190       2200       2210       2220 
GHNIYILAHQ LARHNKELQS MLKPGGQVDG DEALEFYAKH TAQIEIVRLD RTMEQIVFPV 

      2230       2240       2250       2260       2270       2280 
PSICEFLTKE SKLRIYYTTE RDEQGSKIND FFLRSEDLFN EMNWQKKLRA QPVLYWCARN 

      2290       2300       2310       2320       2330       2340 
MSFWSSISFN LAVLMNLLVA FFYPFKGVRG GTLEPHWSGL LWTAMLISLA IVIALPKPHG 

      2350       2360       2370       2380       2390       2400 
IRALIASTIL RLIFSVGLQP TLFLLGAFNV CNKIIFLMSF VGNCGTFTRG YRAMVLDVEF 

      2410       2420       2430       2440       2450       2460 
LYHLLYLVIC AMGLFVHEFF YSLLLFDLVY REETLLNVIK SVTRNGRSII LTAVLALILV 

      2470       2480       2490       2500       2510       2520 
YLFSIVGYLF FKDDFILEVD RLPNETAVPE TGESLASEFL FSDVCRVESG ENCSSPAPRE 

      2530       2540       2550       2560       2570       2580 
ELVPAEETEQ DKEHTCETLL MCIVTVLSHG LRSGGGVGDV LRKPSKEEPL FAARVIYDLL 

      2590       2600       2610       2620       2630       2640 
FFFMVIIIVL NLIFGVIIDT FADLRSEKQK KEEILKTTCF ICGLERDKFD NKTVTFEEHI 

      2650       2660       2670       2680       2690       2700 
KEEHNMWHYL CFIVLVKVKD STEYTGPESY VAEMIKERNL DWFPRMRAMS LVSSDSEGEQ 

      2710       2720       2730       2740       2750 
NELRNLQEKL ESTMKLVTNL SGQLSELKDQ MTEQRKQKQR IGLLGHPPHM NVNPQQPA 

« Hide

Isoform 2 (SI-SIIISIIAC) [UniParc].

Checksum: D0AA6DEC837C28AB
Show »

FASTA2,743312,163
Isoform 3 (SISIII-SII) [UniParc].

Checksum: C24313548F4DCBFC
Show »

FASTA2,710308,539
Isoform 4 (SI-SIII-SII) [UniParc].

Checksum: 92B35C092276D178
Show »

FASTA2,695306,773
Isoform 5 (SI-SIII-SIIAC) [UniParc].

Checksum: 5D714D3692B19AA3
Show »

FASTA2,734311,135
Isoform 6 (SISIIISIIA) [UniParc].

Checksum: EAFD59A4EFF360A5
Show »

FASTA2,743312,132
Isoform 7 (SI-SIII-SIIA) [UniParc].

Checksum: 01927170B33E0F70
Show »

FASTA2,728310,366
Isoform 8 (SI-SIII-SIIA) [UniParc].

Checksum: 35A642696397A7EF
Show »

FASTA2,719309,338

References

« Hide 'large scale' references
[1]"Human inositol 1,4,5-trisphosphate type-1 receptor, InsP3R1: structure, function, regulation of expression and chromosomal localization."
Yamada N., Makino Y., Clark R.A., Pearson D.W., Mattei M.-G., Guenet J.-L., Ohama E., Fujino I., Miyawaki A., Furuichi T., Mikoshiba K.
Biochem. J. 302:781-790(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
Tissue: Myeloid and Uterus.
[2]"The human type 1 inositol 1,4,5-trisphosphate receptor from T lymphocytes. Structure, localization, and tyrosine phosphorylation."
Harnick D.J., Jayaraman T., Ma Y., Mulieri P., Go L.O., Marks A.R.
J. Biol. Chem. 270:2833-2840(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), PHOSPHORYLATION.
Tissue: T-cell.
[3]Marks A.
Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION TO 431; 1012-1017; 1460; 1823; 2324; 2330; 2334; 2337; 2346; 2358; 2361; 2372; 2396; 2418; 2426; 2434 AND 2741.
[4]"Molecular cloning of a cDNA for the human inositol 1,4,5-trisphosphate receptor type 1, and the identification of a third alternatively spliced variant."
Nucifora F.C. Jr., Li S.-H., Danoff S., Ullrich A., Ross C.A.
Brain Res. Mol. Brain Res. 32:291-296(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), ALTERNATIVE SPLICING.
Tissue: Brain.
[5]"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].
[6]"Induction of inositol 1,4,5 trisphosphate receptor genes by ionizing radiation."
Yan J., Khanna K.K., Lavin M.F.
Int. J. Radiat. Biol. 69:539-546(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1548-1723 (ISOFORMS 3 AND 4).
[7]"Identification of a family of calcium sensors as protein ligands of inositol trisphosphate receptor Ca(2+) release channels."
Yang J., McBride S., Mak D.-O.D., Vardi N., Palczewski K., Haeseleer F., Foskett J.K.
Proc. Natl. Acad. Sci. U.S.A. 99:7711-7716(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CABP1.
[8]"Regulation of InsP3 receptor activity by neuronal Ca2+-binding proteins."
Kasri N.N., Holmes A.M., Bultynck G., Parys J.B., Bootman M.D., Rietdorf K., Missiaen L., McDonald F., De Smedt H., Conway S.J., Holmes A.B., Berridge M.J., Roderick H.L.
EMBO J. 23:312-321(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CABP1.
[9]"Subtype-specific and ER lumenal environment-dependent regulation of inositol 1,4,5-trisphosphate receptor type 1 by ERp44."
Higo T., Hattori M., Nakamura T., Natsume T., Michikawa T., Mikoshiba K.
Cell 120:85-98(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ERP44.
[10]"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1598, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"IRAG mediates NO/cGMP-dependent inhibition of platelet aggregation and thrombus formation."
Antl M., von Bruehl M.-L., Eiglsperger C., Werner M., Konrad I., Kocher T., Wilm M., Hofmann F., Massberg S., Schlossmann J.
Blood 109:552-559(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MRVI1.
[12]"Deletion at ITPR1 underlies ataxia in mice and spinocerebellar ataxia 15 in humans."
van de Leemput J., Chandran J., Knight M.A., Holtzclaw L.A., Scholz S., Cookson M.R., Houlden H., Gwinn-Hardy K., Fung H.-C., Lin X., Hernandez D., Simon-Sanchez J., Wood N.W., Giunti P., Rafferty I., Hardy J., Storey E., Gardner R.J.M. expand/collapse author list , Forrest S.M., Fisher E.M.C., Russell J.T., Cai H., Singleton A.B.
PLoS Genet. 3:1076-1082(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN SCA15.
[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-1598 AND SER-1764, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[14]"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-2512.
Tissue: Liver.
[15]"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-1598, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[16]"Total deletion and a missense mutation of ITPR1 in Japanese SCA15 families."
Hara K., Shiga A., Nozaki H., Mitsui J., Takahashi Y., Ishiguro H., Yomono H., Kurisaki H., Goto J., Ikeuchi T., Tsuji S., Nishizawa M., Onodera O.
Neurology 71:547-551(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT SCA15 LEU-1059.
[17]"Missense mutations in ITPR1 cause autosomal dominant congenital nonprogressive spinocerebellar ataxia."
Huang L., Chardon J.W., Carter M.T., Friend K.L., Dudding T.E., Schwartzentruber J., Zou R., Schofield P.W., Douglas S., Bulman D.E., Boycott K.M.
Orphanet J. Rare Dis. 7:67-67(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS SCA29 ASP-602 AND MET-1562.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D26070 mRNA. Translation: BAA05065.1.
L38019 mRNA. Translation: AAB04947.2.
U23850 mRNA. No translation available.
AC018816 Genomic DNA. No translation available.
AC024168 Genomic DNA. No translation available.
AC069248 Genomic DNA. No translation available.
AC090944 Genomic DNA. No translation available.
S82269 mRNA. Translation: AAD14386.1.
PIRA55713.
S54974.
RefSeqNP_001093422.2. NM_001099952.2.
NP_002213.5. NM_002222.5.
UniGeneHs.567295.
Hs.715765.

3D structure databases

ProteinModelPortalQ14643.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109913. 30 interactions.
DIPDIP-29714N.
IntActQ14643. 3 interactions.
MINTMINT-4991320.
STRING9606.ENSP00000405934.

Chemistry

BindingDBQ14643.
ChEMBLCHEMBL2111451.
GuidetoPHARMACOLOGY743.

Protein family/group databases

TCDB1.A.3.2.6. the ryanodine-inositol 1,4,5-triphosphate receptor ca(2+) channel (rir-cac) family.

PTM databases

PhosphoSiteQ14643.

Polymorphism databases

DMDM519668682.

Proteomic databases

PaxDbQ14643.
PRIDEQ14643.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000302640; ENSP00000306253; ENSG00000150995. [Q14643-2]
ENST00000357086; ENSP00000349597; ENSG00000150995. [Q14643-3]
ENST00000443694; ENSP00000401671; ENSG00000150995. [Q14643-2]
ENST00000456211; ENSP00000397885; ENSG00000150995. [Q14643-4]
GeneID3708.
KEGGhsa:3708.
UCSCuc021wsi.1. human. [Q14643-3]
uc021wsj.1. human. [Q14643-4]

Organism-specific databases

CTD3708.
GeneCardsGC03P004486.
HGNCHGNC:6180. ITPR1.
HPAHPA014765.
HPA016487.
MIM117360. phenotype.
147265. gene.
606658. phenotype.
neXtProtNX_Q14643.
Orphanet98769. Spinocerebellar ataxia type 15/16.
208513. Spinocerebellar ataxia type 29.
PharmGKBPA29978.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG280601.
HOGENOMHOG000007660.
HOVERGENHBG052158.
InParanoidQ14643.
KOK04958.
OMAGENEHKK.
OrthoDBEOG76HQ0M.
TreeFamTF312815.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_111217. Metabolism.
REACT_116125. Disease.
REACT_604. Hemostasis.
REACT_6900. Immune System.
SignaLinkQ14643.

Gene expression databases

ArrayExpressQ14643.
BgeeQ14643.
CleanExHS_ITPR1.
GenevestigatorQ14643.

Family and domain databases

Gene3D1.25.10.30. 2 hits.
InterProIPR016024. ARM-type_fold.
IPR014821. Ins145_P3_rcpt.
IPR000493. InsP3_rcpt-bd.
IPR005821. Ion_trans_dom.
IPR016093. MIR_motif.
IPR013662. RIH_assoc-dom.
IPR000699. RIH_dom.
IPR015925. Ryanodine_recept-rel.
[Graphical view]
PANTHERPTHR13715. PTHR13715. 1 hit.
PfamPF08709. Ins145_P3_rec. 1 hit.
PF00520. Ion_trans. 1 hit.
PF02815. MIR. 1 hit.
PF08454. RIH_assoc. 1 hit.
PF01365. RYDR_ITPR. 2 hits.
[Graphical view]
PRINTSPR00779. INSP3RECEPTR.
SMARTSM00472. MIR. 4 hits.
[Graphical view]
SUPFAMSSF100909. SSF100909. 2 hits.
SSF48371. SSF48371. 4 hits.
SSF82109. SSF82109. 2 hits.
PROSITEPS50919. MIR. 5 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSITPR1. human.
GeneWikiITPR1.
GenomeRNAi3708.
NextBio14533.
PROQ14643.
SOURCESearch...

Entry information

Entry nameITPR1_HUMAN
AccessionPrimary (citable) accession number: Q14643
Secondary accession number(s): E7EPX7 expand/collapse secondary AC list , E9PDE9, Q14660, Q99897
Entry history
Integrated into UniProtKB/Swiss-Prot: November 2, 2001
Last sequence update: June 26, 2013
Last modified: April 16, 2014
This is version 159 of the entry and version 3 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

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