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P31415

- CASQ1_HUMAN

UniProt

P31415 - CASQ1_HUMAN

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Protein

Calsequestrin-1

Gene

CASQ1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Calsequestrin is a high-capacity, moderate affinity, calcium-binding protein and thus acts as an internal calcium store in muscle. Calcium ions are bound by clusters of acidic residues at the protein surface, often at the interface between subunits. Can bind around 80 Ca2+ ions. Regulates the release of lumenal Ca2+ via the calcium release channel RYR1; this plays an important role in triggering muscle contraction.1 Publication1 Publication

GO - Molecular functioni

  1. calcium ion binding Source: UniProtKB

GO - Biological processi

  1. endoplasmic reticulum organization Source: Ensembl
  2. ion transmembrane transport Source: Reactome
  3. protein polymerization Source: UniProtKB
  4. regulation of sequestering of calcium ion Source: Ensembl
  5. regulation of skeletal muscle contraction by regulation of release of sequestered calcium ion Source: UniProtKB
  6. response to denervation involved in regulation of muscle adaptation Source: Ensembl
  7. response to heat Source: Ensembl
  8. response to organic substance Source: Ensembl
  9. sarcomere organization Source: UniProtKB
  10. skeletal muscle tissue development Source: Ensembl
  11. transmembrane transport Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Muscle protein

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_160189. Stimuli-sensing channels.

Names & Taxonomyi

Protein namesi
Recommended name:
Calsequestrin-1
Alternative name(s):
Calmitine1 Publication
Calsequestrin, skeletal muscle isoform
Gene namesi
Name:CASQ1
Synonyms:CASQ
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:1512. CASQ1.

Subcellular locationi

Sarcoplasmic reticulum lumen By similarity. Sarcoplasmic reticulum membrane; Peripheral membrane protein; Lumenal side By similarity. Mitochondrion matrix By similarity
Note: This isoform of calsequestrin occurs in the sarcoplasmic reticulum's terminal cisternae luminal spaces of fast skeletal muscle cells.By similarity

GO - Cellular componenti

  1. endoplasmic reticulum Source: ProtInc
  2. Golgi apparatus Source: Ensembl
  3. I band Source: Ensembl
  4. mitochondrial matrix Source: UniProtKB
  5. mitochondrion Source: UniProt
  6. sarcoplasmic reticulum Source: UniProtKB
  7. sarcoplasmic reticulum lumen Source: UniProtKB
  8. sarcoplasmic reticulum membrane Source: Reactome
  9. smooth endoplasmic reticulum Source: ProtInc
  10. terminal cisterna lumen Source: Ensembl
  11. T-tubule Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Sarcoplasmic reticulum

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA26095.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3434Sequence AnalysisAdd
BLAST
Chaini35 – 396362Calsequestrin-1PRO_0000004212Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi350 – 3501N-linked (GlcNAc...)Sequence Analysis

Post-translational modificationi

N-glycosylated.By similarity

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiP31415.
PaxDbiP31415.
PRIDEiP31415.

PTM databases

PhosphoSiteiP31415.

Expressioni

Gene expression databases

BgeeiP31415.
CleanExiHS_CASQ1.
ExpressionAtlasiP31415. baseline and differential.
GenevestigatoriP31415.

Organism-specific databases

HPAiCAB015170.
HPA007845.
HPA026823.

Interactioni

Subunit structurei

Interacts with ASPH and TRDN (By similarity). Monomer, homodimer, homotetramer and homopolymer. Can form linear homooligomers. Ca2+ ions promote oligomerization.By similarity1 Publication

Protein-protein interaction databases

STRINGi9606.ENSP00000357058.

Structurei

Secondary structure

1
396
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi49 – 513Combined sources
Turni54 – 563Combined sources
Helixi57 – 637Combined sources
Beta strandi65 – 728Combined sources
Helixi79 – 9921Combined sources
Helixi100 – 1023Combined sources
Beta strandi104 – 1107Combined sources
Turni111 – 1144Combined sources
Helixi115 – 1217Combined sources
Beta strandi125 – 1339Combined sources
Beta strandi136 – 1394Combined sources
Helixi146 – 15712Combined sources
Beta strandi160 – 1634Combined sources
Helixi167 – 1759Combined sources
Beta strandi181 – 1855Combined sources
Helixi192 – 20413Combined sources
Turni205 – 2073Combined sources
Beta strandi210 – 2134Combined sources
Helixi216 – 2227Combined sources
Beta strandi229 – 2324Combined sources
Beta strandi243 – 2464Combined sources
Helixi249 – 25810Combined sources
Beta strandi263 – 2664Combined sources
Helixi269 – 2713Combined sources
Helixi272 – 2765Combined sources
Beta strandi280 – 2889Combined sources
Helixi294 – 30815Combined sources
Beta strandi318 – 3214Combined sources
Helixi323 – 3253Combined sources
Helixi327 – 3293Combined sources
Helixi330 – 3378Combined sources
Beta strandi345 – 3506Combined sources
Turni351 – 3544Combined sources
Beta strandi355 – 3584Combined sources
Helixi370 – 38213Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3UOMX-ray2.02A/B/C/D/E/F35-396[»]
ProteinModelPortaliP31415.
SMRiP31415. Positions 37-388.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi15 – 2511Poly-LeuAdd
BLAST
Compositional biasi353 – 39644Asp-richAdd
BLAST

Sequence similaritiesi

Belongs to the calsequestrin family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG77804.
GeneTreeiENSGT00390000019377.
HOGENOMiHOG000049047.
HOVERGENiHBG050805.
InParanoidiP31415.
OMAiEVAEDNT.
OrthoDBiEOG725DHM.
PhylomeDBiP31415.
TreeFamiTF313796.

Family and domain databases

Gene3Di3.40.30.10. 3 hits.
InterProiIPR001393. Calsequestrin.
IPR018233. Calsequestrin_CS.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF01216. Calsequestrin. 1 hit.
[Graphical view]
PRINTSiPR00312. CALSEQUESTRN.
SUPFAMiSSF52833. SSF52833. 3 hits.
PROSITEiPS00863. CALSEQUESTRIN_1. 1 hit.
PS00864. CALSEQUESTRIN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P31415-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSATDRMGPR AVPGLRLALL LLLVLGTPKS GVQGQEGLDF PEYDGVDRVI
60 70 80 90 100
NVNAKNYKNV FKKYEVLALL YHEPPEDDKA SQRQFEMEEL ILELAAQVLE
110 120 130 140 150
DKGVGFGLVD SEKDAAVAKK LGLTEVDSMY VFKGDEVIEY DGEFSADTIV
160 170 180 190 200
EFLLDVLEDP VELIEGEREL QAFENIEDEI KLIGYFKSKD SEHYKAFEDA
210 220 230 240 250
AEEFHPYIPF FATFDSKVAK KLTLKLNEID FYEAFMEEPV TIPDKPNSEE
260 270 280 290 300
EIVNFVEEHR RSTLRKLKPE SMYETWEDDM DGIHIVAFAE EADPDGFEFL
310 320 330 340 350
ETLKAVAQDN TENPDLSIIW IDPDDFPLLV PYWEKTFDID LSAPQIGVVN
360 370 380 390
VTDADSVWME MDDEEDLPSA EELEDWLEDV LEGEINTEDD DDDDDD
Length:396
Mass (Da):45,160
Last modified:July 27, 2011 - v3
Checksum:iC20388AD8870E12D
GO

Sequence cautioni

The sequence AAB32063.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAH22289.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAG36060.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti356 – 3572SV → RL in AAB32063. (PubMed:7945294)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti140 – 1401Y → F.
Corresponds to variant rs34489853 [ dbSNP | Ensembl ].
VAR_053021

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S73775 mRNA. Translation: AAB32063.1. Different initiation.
AK313250 mRNA. Translation: BAG36060.1. Different initiation.
AL121987 Genomic DNA. Translation: CAI15276.1.
CH471121 Genomic DNA. Translation: EAW52736.1.
BC022289 mRNA. Translation: AAH22289.1. Different initiation.
CCDSiCCDS1198.2.
PIRiA60424.
RefSeqiNP_001222.3. NM_001231.4.
UniGeneiHs.632476.

Genome annotation databases

EnsembliENST00000368078; ENSP00000357057; ENSG00000143318.
GeneIDi844.
KEGGihsa:844.
UCSCiuc010pja.2. human.

Polymorphism databases

DMDMi341940551.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Wikipedia

Calsequestrin entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S73775 mRNA. Translation: AAB32063.1 . Different initiation.
AK313250 mRNA. Translation: BAG36060.1 . Different initiation.
AL121987 Genomic DNA. Translation: CAI15276.1 .
CH471121 Genomic DNA. Translation: EAW52736.1 .
BC022289 mRNA. Translation: AAH22289.1 . Different initiation.
CCDSi CCDS1198.2.
PIRi A60424.
RefSeqi NP_001222.3. NM_001231.4.
UniGenei Hs.632476.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3UOM X-ray 2.02 A/B/C/D/E/F 35-396 [» ]
ProteinModelPortali P31415.
SMRi P31415. Positions 37-388.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 9606.ENSP00000357058.

PTM databases

PhosphoSitei P31415.

Polymorphism databases

DMDMi 341940551.

Proteomic databases

MaxQBi P31415.
PaxDbi P31415.
PRIDEi P31415.

Protocols and materials databases

DNASUi 844.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000368078 ; ENSP00000357057 ; ENSG00000143318 .
GeneIDi 844.
KEGGi hsa:844.
UCSCi uc010pja.2. human.

Organism-specific databases

CTDi 844.
GeneCardsi GC01P160160.
HGNCi HGNC:1512. CASQ1.
HPAi CAB015170.
HPA007845.
HPA026823.
MIMi 114250. gene.
neXtProti NX_P31415.
PharmGKBi PA26095.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG77804.
GeneTreei ENSGT00390000019377.
HOGENOMi HOG000049047.
HOVERGENi HBG050805.
InParanoidi P31415.
OMAi EVAEDNT.
OrthoDBi EOG725DHM.
PhylomeDBi P31415.
TreeFami TF313796.

Enzyme and pathway databases

Reactomei REACT_160189. Stimuli-sensing channels.

Miscellaneous databases

GenomeRNAii 844.
NextBioi 3538.
PROi P31415.
SOURCEi Search...

Gene expression databases

Bgeei P31415.
CleanExi HS_CASQ1.
ExpressionAtlasi P31415. baseline and differential.
Genevestigatori P31415.

Family and domain databases

Gene3Di 3.40.30.10. 3 hits.
InterProi IPR001393. Calsequestrin.
IPR018233. Calsequestrin_CS.
IPR012336. Thioredoxin-like_fold.
[Graphical view ]
Pfami PF01216. Calsequestrin. 1 hit.
[Graphical view ]
PRINTSi PR00312. CALSEQUESTRN.
SUPFAMi SSF52833. SSF52833. 3 hits.
PROSITEi PS00863. CALSEQUESTRIN_1. 1 hit.
PS00864. CALSEQUESTRIN_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Characterization and localization to human chromosome 1 of human fast-twitch skeletal muscle calsequestrin gene."
    Fujii J., Willard H.F., Maclennan D.H.
    Somat. Cell Mol. Genet. 16:185-189(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Molecular cloning of human calmitine, a mitochondrial calcium binding protein, reveals identity with calsequestrine."
    Bataille N., Schmitt N., Aumercier-Maes P., Ollivier B., Lucas-Heron B., Lestienne P.
    Biochem. Biophys. Res. Commun. 203:1477-1482(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
    Tissue: Skeletal muscle.
  3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Pericardium.
  4. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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].
    Tissue: Skeletal muscle.
  7. "High-capacity Ca2+ binding of human skeletal calsequestrin."
    Sanchez E.J., Lewis K.M., Danna B.R., Kang C.
    J. Biol. Chem. 287:11592-11601(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.02 ANGSTROMS) OF 35-396 IN COMPLEX WITH CALCIUM, FUNCTION, SUBUNIT.

Entry informationi

Entry nameiCASQ1_HUMAN
AccessioniPrimary (citable) accession number: P31415
Secondary accession number(s): B1AKZ2, B2R863, Q8TBW7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 27, 2011
Last modified: November 26, 2014
This is version 132 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3