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Q9NZU7

- CABP1_HUMAN

UniProt

Q9NZU7 - CABP1_HUMAN

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Protein

Calcium-binding protein 1

Gene

CABP1

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

Functioni

Modulates calcium-dependent activity of inositol 1,4,5-triphosphate receptors (ITPRs). Inhibits agonist-induced intracellular calcium signaling. Enhances inactivation and does not support calcium-dependent facilitation of voltage-dependent P/Q-type calcium channels. Causes calcium-dependent facilitation and inhibits inactivation of L-type calcium channels by binding to the same sites as calmodulin in the C-terminal domain of CACNA1C, but resulting in an opposit effects on channel function. Suppresses the calcium-dependent inactivation of CACNA1D (By similarity). Inhibits TRPC5 channels. Prevents NMDA receptor-induced cellular degeneration (By similarity).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi238 – 2381Magnesium1 Publication
Metal bindingi240 – 2401Magnesium1 Publication
Metal bindingi242 – 2421Magnesium1 Publication
Metal bindingi244 – 2441Magnesium; via carbonyl oxygen1 Publication
Metal bindingi315 – 3151Calcium 11 Publication
Metal bindingi317 – 3171Calcium 11 Publication
Metal bindingi319 – 3191Calcium 11 Publication
Metal bindingi321 – 3211Calcium 1; via carbonyl oxygen1 Publication
Metal bindingi326 – 3261Calcium 11 Publication
Metal bindingi352 – 3521Calcium 21 Publication
Metal bindingi353 – 3531Calcium 2; via amide nitrogen1 Publication
Metal bindingi354 – 3541Calcium 21 Publication
Metal bindingi356 – 3561Calcium 21 Publication
Metal bindingi357 – 3571Calcium 2; via amide nitrogen1 Publication
Metal bindingi358 – 3581Calcium 2; via carbonyl oxygen1 Publication
Metal bindingi360 – 3601Calcium 21 Publication
Metal bindingi363 – 3631Calcium 21 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi238 – 249121Add
BLAST
Calcium bindingi315 – 326122Add
BLAST
Calcium bindingi352 – 363123Add
BLAST

GO - Molecular functioni

  1. calcium-dependent protein binding Source: UniProtKB
  2. calcium ion binding Source: ProtInc
  3. enzyme inhibitor activity Source: ProtInc
  4. nuclear localization sequence binding Source: UniProtKB

GO - Biological processi

  1. negative regulation of catalytic activity Source: GOC
  2. negative regulation of cell communication by electrical coupling Source: Ensembl
  3. negative regulation of protein import into nucleus Source: UniProtKB
  4. negative regulation of voltage-gated calcium channel activity Source: Ensembl
Complete GO annotation...

Keywords - Ligandi

Calcium, Magnesium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Calcium-binding protein 1
Short name:
CaBP1
Alternative name(s):
Calbrain
Caldendrin
Gene namesi
Name:CABP1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 12

Organism-specific databases

HGNCiHGNC:1384. CABP1.

Subcellular locationi

Cytoplasmcytoskeleton. Cytoplasmperinuclear region. Cell membrane; Lipid-anchor; Cytoplasmic side. Golgi apparatus. Cell junctionsynapsepostsynaptic cell membranepostsynaptic density
Note: L-CaBP1 is associated most likely with the cytoskeletal structures, whereas S-CaBP1 is localized at or near the plasma membrane.
Isoform L-CaBP1 : Cytoplasmcytoskeleton
Note: L-CaBP1 is associated most likely with the cytoskeletal structures.
Isoform S-CaBP1 : Cytoplasmcell cortex. Cell membrane Curated; Lipid-anchor Curated
Note: S-CaBP1 is localized at or near the plasma membrane.

GO - Cellular componenti

  1. cell junction Source: UniProtKB-KW
  2. cytoplasmic side of plasma membrane Source: Ensembl
  3. cytosol Source: Ensembl
  4. dendrite Source: Ensembl
  5. extracellular space Source: UniProt
  6. Golgi membrane Source: MGI
  7. neuronal cell body Source: Ensembl
  8. nucleus Source: Ensembl
  9. perinuclear region of cytoplasm Source: Ensembl
  10. plasma membrane Source: MGI
  11. postsynaptic density Source: UniProtKB
  12. postsynaptic membrane Source: UniProtKB-KW
  13. protein complex Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cytoplasm, Cytoskeleton, Golgi apparatus, Membrane, Postsynaptic cell membrane, Synapse

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi238 – 2381D → A: Loss of magnesium-binding. Loss of binding to ITPRs; when associated with A-240; A-315; A-317; A-352 and A-354. 2 Publications
Mutagenesisi240 – 2401D → A: Loss of magnesium-binding. Loss of binding to ITPRs; when associated with A-238; A-315; A-317; A-352 and A-354. 2 Publications
Mutagenesisi242 – 2421D → A: Loss of magnesium-binding. 1 Publication
Mutagenesisi249 – 2491D → A: No effect on magnesium-binding. 1 Publication
Mutagenesisi315 – 3151D → A: Loss of binding to ITPRs; when associated with A-238; A-240; A-317; A-352 and A-354. 1 Publication
Mutagenesisi317 – 3171N → A: Loss of binding to ITPRs; when associated with A-238; A-240; A-315; A-352 and A-354. 1 Publication
Mutagenesisi323 – 3231S → A: Loss of phosphorylation and loss of calcium release by InsP(3). 1 Publication
Mutagenesisi352 – 3521D → A: Loss of binding to ITPRs; when associated with A-238; A-240; A-315; A-317 and A-354. 1 Publication
Mutagenesisi354 – 3541N → A: Loss of binding to ITPRs; when associated with A-238; A-240; A-315; A-317 and A-352. 1 Publication

Organism-specific databases

PharmGKBiPA26000.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedSequence Analysis
Chaini2 – 370369Calcium-binding protein 1PRO_0000073513Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi2 – 21N-myristoyl glycineSequence Analysis
Modified residuei323 – 3231Phosphoserine1 Publication

Post-translational modificationi

Phosphorylated. The phosphorylation regulates the activity.1 Publication

Keywords - PTMi

Lipoprotein, Myristate, Phosphoprotein

Proteomic databases

PaxDbiQ9NZU7.
PRIDEiQ9NZU7.

PTM databases

PhosphoSiteiQ9NZU7.

Expressioni

Tissue specificityi

Retina and brain. Somatodendritic compartment of neurons. Calbrain was found exclusively in brain where it is abundant in the hippocampus, habenular area in the epithalamus and in the cerebellum.

Gene expression databases

BgeeiQ9NZU7.
CleanExiHS_CABP1.
ExpressionAtlasiQ9NZU7. baseline and differential.
GenevestigatoriQ9NZU7.

Organism-specific databases

HPAiHPA051438.

Interactioni

Subunit structurei

Homodimer; when bound to calcium or magnesium. Interacts (via C-terminus) with ITPR1, ITPR2 and ITPR3. This binding is calcium dependent and the interaction correlates with calcium concentration. An additional calcium-independent interaction with the N-terminus of ITPR1 results in a decreased InsP3 binding to the receptor. Interacts with CACNA1A (via C-terminal CDB motif) in the pre- and postsynaptic membranes. Interacts with CACNA1C (via C-terminal C and IQ motifs). The binding to the C motif is calcium independent whereas the binding to IQ requires the presence of calcium and is mutually exclusive with calmodulin binding. Interacts with CACNA1D (By similarity). Interacts with TRPC5 (via C-terminus). Interacts (via EF-hands 1 and 2) at microtubules with MAP1LC3B. Interacts with MYO1C (By similarity). Interacts (via EF-hands 1 and 2) with NSMF (via the central NLS-containing motif region), the interaction occurs in a calcium dependent manner after synaptic NMDA receptor stimulation and prevents nuclear import of NSMF (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
CACNA1CQ139364EBI-907894,EBI-1038838

Protein-protein interaction databases

BioGridi114863. 8 interactions.
DIPiDIP-35477N.
IntActiQ9NZU7. 4 interactions.
STRINGi9606.ENSP00000317310.

Structurei

Secondary structure

1
370
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi224 – 24017Combined sources
Beta strandi242 – 2443Combined sources
Helixi247 – 25610Combined sources
Helixi263 – 27412Combined sources
Beta strandi277 – 2793Combined sources
Helixi283 – 29412Combined sources
Helixi299 – 3024Combined sources
Helixi304 – 31411Combined sources
Beta strandi319 – 3224Combined sources
Helixi324 – 33512Combined sources
Beta strandi337 – 3393Combined sources
Helixi341 – 35111Combined sources
Beta strandi353 – 3597Combined sources
Helixi361 – 3677Combined sources

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2K7BNMR-A219-294[»]
2K7CNMR-A299-370[»]
2K7DNMR-A299-370[»]
2LANNMR-A219-370[»]
2LAPNMR-A219-370[»]
3OX5X-ray2.90A/B/C/D/E/F219-370[»]
3OX6X-ray2.40A/B/C/D/E/F219-370[»]
ProteinModelPortaliQ9NZU7.
SMRiQ9NZU7. Positions 219-370.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9NZU7.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini225 – 26036EF-hand 1PROSITE-ProRule annotationAdd
BLAST
Domaini261 – 29636EF-hand 2PROSITE-ProRule annotationAdd
BLAST
Domaini302 – 33736EF-hand 3PROSITE-ProRule annotationAdd
BLAST
Domaini339 – 37032EF-hand 4PROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi45 – 484Poly-Pro
Compositional biasi74 – 796Poly-Ala
Compositional biasi86 – 16479Pro-richAdd
BLAST

Domaini

EF-1 binds magnesium constitutively under physiological conditions, EF-3 and EF-4 bind calcium cooperatively and EF-2 binds neither calcium nor magnesium.

Sequence similaritiesi

Contains 4 EF-hand domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG5126.
GeneTreeiENSGT00760000118901.
HOGENOMiHOG000233018.
HOVERGENiHBG012180.
InParanoidiQ9NZU7.
OrthoDBiEOG7XM303.
PhylomeDBiQ9NZU7.
TreeFamiTF334804.

Family and domain databases

Gene3Di1.10.238.10. 2 hits.
InterProiIPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
[Graphical view]
PfamiPF00036. EF-hand_1. 3 hits.
[Graphical view]
SMARTiSM00054. EFh. 3 hits.
[Graphical view]
PROSITEiPS00018. EF_HAND_1. 3 hits.
PS50222. EF_HAND_2. 4 hits.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

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

This entry describes 4 isoformsi produced by alternative splicing. Align

Note: Experimental confirmation may be lacking for some isoforms.

Isoform Caldendrin (identifier: Q9NZU7-4) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MGGGDGAAFK RPGDGARLQR VLGLGSRREP RSLPAGGPAP RRTAPPPPGH
60 70 80 90 100
ASAGPAAMSS HIAKSESKTS LLKAAAAAAS GGSRAPRHGP ARDPGLPSRR
110 120 130 140 150
LPGSCPATPQ SSGDPSSRRP LCRPAPREEG ARGSQRVLPQ AHCRPREALP
160 170 180 190 200
AAASRPSPSS PLPPARGRDG EERGLSPALG LRGSLRARGR GDSVPAAASE
210 220 230 240 250
ADPFLHRLRP MLSSAFGQDR SLRPEEIEEL REAFREFDKD KDGYINCRDL
260 270 280 290 300
GNCMRTMGYM PTEMELIELS QQINMNLGGH VDFDDFVELM GPKLLAETAD
310 320 330 340 350
MIGVKELRDA FREFDTNGDG EISTSELREA MRKLLGHQVG HRDIEEIIRD
360 370
VDLNGDGRVD FEEFVRMMSR
Length:370
Mass (Da):39,838
Last modified:May 31, 2011 - v5
Checksum:i3444721152E01AA7
GO
Isoform L-CaBP1 (identifier: Q9NZU7-1) [UniParc]FASTAAdd to Basket

Also known as: Caldendrin-S2

The sequence of this isoform differs from the canonical sequence as follows:
     1-143: Missing.
     144-218: RPREALPAAA...RPMLSSAFGQ → MGNCVKYPLR...RKGFAENRQP

Note: Myristoylated on Gly-2.

Show »
Length:227
Mass (Da):25,979
Checksum:iFF3F7A9B575486AB
GO
Isoform S-CaBP1 (identifier: Q9NZU7-2) [UniParc]FASTAAdd to Basket

Also known as: Caldendrin-S1

The sequence of this isoform differs from the canonical sequence as follows:
     1-203: Missing.
     204-218: FLHRLRPMLSSAFGQ → MGNCVKYPLRNLSRK

Note: Myristoylated on Gly-2.

Show »
Length:167
Mass (Da):19,430
Checksum:iB8C19D9E24D384FD
GO
Isoform Calbrain (identifier: Q9NZU7-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-300: Missing.

Note: It is currently uncertain whether calbrain represent a spliced isoform.

Show »
Length:70
Mass (Da):8,139
Checksum:i2807BEB35ADCDA48
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti140 – 1401Q → R in AAH30201. (PubMed:15489334)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 300300Missing in isoform Calbrain. 1 PublicationVSP_037936Add
BLAST
Alternative sequencei1 – 203203Missing in isoform S-CaBP1. 1 PublicationVSP_037937Add
BLAST
Alternative sequencei1 – 143143Missing in isoform L-CaBP1. 1 PublicationVSP_037938Add
BLAST
Alternative sequencei144 – 21875RPREA…SAFGQ → MGNCVKYPLRNLSRKMCQEE QTSYMVVQTSEEGLAADAEL PGPLLMLAQNCAVMHNLLGP ACIFLRKGFAENRQP in isoform L-CaBP1. 1 PublicationVSP_037939Add
BLAST
Alternative sequencei204 – 21815FLHRL…SAFGQ → MGNCVKYPLRNLSRK in isoform S-CaBP1. 1 PublicationVSP_037940Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X94700 mRNA. Translation: CAA64361.1.
AF169148 mRNA. Translation: AAF25782.1.
AF169149 mRNA. Translation: AAF25783.1.
AC069234 Genomic DNA. No translation available.
BC030201 mRNA. Translation: AAH30201.2.
CCDSiCCDS31913.1. [Q9NZU7-4]
CCDS9204.1. [Q9NZU7-2]
CCDS9205.1. [Q9NZU7-1]
RefSeqiNP_001028849.1. NM_001033677.1. [Q9NZU7-4]
NP_004267.2. NM_004276.4. [Q9NZU7-2]
NP_112482.1. NM_031205.3. [Q9NZU7-1]
UniGeneiHs.458482.

Genome annotation databases

EnsembliENST00000288616; ENSP00000288616; ENSG00000157782. [Q9NZU7-1]
ENST00000316803; ENSP00000317310; ENSG00000157782. [Q9NZU7-4]
ENST00000351200; ENSP00000288615; ENSG00000157782. [Q9NZU7-2]
GeneIDi9478.
KEGGihsa:9478.
UCSCiuc001tyu.3. human. [Q9NZU7-4]
uc001tyv.4. human. [Q9NZU7-1]
uc001tyw.4. human. [Q9NZU7-2]

Polymorphism databases

DMDMi334302962.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X94700 mRNA. Translation: CAA64361.1 .
AF169148 mRNA. Translation: AAF25782.1 .
AF169149 mRNA. Translation: AAF25783.1 .
AC069234 Genomic DNA. No translation available.
BC030201 mRNA. Translation: AAH30201.2 .
CCDSi CCDS31913.1. [Q9NZU7-4 ]
CCDS9204.1. [Q9NZU7-2 ]
CCDS9205.1. [Q9NZU7-1 ]
RefSeqi NP_001028849.1. NM_001033677.1. [Q9NZU7-4 ]
NP_004267.2. NM_004276.4. [Q9NZU7-2 ]
NP_112482.1. NM_031205.3. [Q9NZU7-1 ]
UniGenei Hs.458482.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2K7B NMR - A 219-294 [» ]
2K7C NMR - A 299-370 [» ]
2K7D NMR - A 299-370 [» ]
2LAN NMR - A 219-370 [» ]
2LAP NMR - A 219-370 [» ]
3OX5 X-ray 2.90 A/B/C/D/E/F 219-370 [» ]
3OX6 X-ray 2.40 A/B/C/D/E/F 219-370 [» ]
ProteinModelPortali Q9NZU7.
SMRi Q9NZU7. Positions 219-370.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 114863. 8 interactions.
DIPi DIP-35477N.
IntActi Q9NZU7. 4 interactions.
STRINGi 9606.ENSP00000317310.

PTM databases

PhosphoSitei Q9NZU7.

Polymorphism databases

DMDMi 334302962.

Proteomic databases

PaxDbi Q9NZU7.
PRIDEi Q9NZU7.

Protocols and materials databases

DNASUi 9478.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000288616 ; ENSP00000288616 ; ENSG00000157782 . [Q9NZU7-1 ]
ENST00000316803 ; ENSP00000317310 ; ENSG00000157782 . [Q9NZU7-4 ]
ENST00000351200 ; ENSP00000288615 ; ENSG00000157782 . [Q9NZU7-2 ]
GeneIDi 9478.
KEGGi hsa:9478.
UCSCi uc001tyu.3. human. [Q9NZU7-4 ]
uc001tyv.4. human. [Q9NZU7-1 ]
uc001tyw.4. human. [Q9NZU7-2 ]

Organism-specific databases

CTDi 9478.
GeneCardsi GC12P121078.
HGNCi HGNC:1384. CABP1.
HPAi HPA051438.
MIMi 605563. gene.
neXtProti NX_Q9NZU7.
PharmGKBi PA26000.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5126.
GeneTreei ENSGT00760000118901.
HOGENOMi HOG000233018.
HOVERGENi HBG012180.
InParanoidi Q9NZU7.
OrthoDBi EOG7XM303.
PhylomeDBi Q9NZU7.
TreeFami TF334804.

Miscellaneous databases

ChiTaRSi CABP1. human.
EvolutionaryTracei Q9NZU7.
GenomeRNAii 9478.
NextBioi 35520.
PROi Q9NZU7.
SOURCEi Search...

Gene expression databases

Bgeei Q9NZU7.
CleanExi HS_CABP1.
ExpressionAtlasi Q9NZU7. baseline and differential.
Genevestigatori Q9NZU7.

Family and domain databases

Gene3Di 1.10.238.10. 2 hits.
InterProi IPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
[Graphical view ]
Pfami PF00036. EF-hand_1. 3 hits.
[Graphical view ]
SMARTi SM00054. EFh. 3 hits.
[Graphical view ]
PROSITEi PS00018. EF_HAND_1. 3 hits.
PS50222. EF_HAND_2. 4 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Calbrain, a novel two EF-hand calcium-binding protein that suppresses Ca2+/calmodulin-dependent protein kinase II activity in the brain."
    Yamaguchi K., Yamaguchi F., Miyamoto O., Sugimoto K., Konishi R., Hatase O.
    J. Biol. Chem. 274:3610-3616(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM CALBRAIN).
    Tissue: Cerebellum.
  2. "Five members of a novel Ca(2+)-binding protein (CABP) subfamily with similarity to calmodulin."
    Haeseleer F., Sokal I., Verlinde C.L.M.J., Erdjument-Bromage H., Tempst P., Pronin A.N., Benovic J.L., Fariss R.N., Palczewski K.
    J. Biol. Chem. 275:1247-1260(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS L-CABP1 AND S-CABP1), MYRISTOYLATION (ISOFORMS L-CABP1 AND S-CABP1).
    Tissue: Retina.
  3. "The finished DNA sequence of human chromosome 12."
    Scherer S.E., Muzny D.M., 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., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
    , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
    Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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] (ISOFORM CALDENDRIN).
  5. "Caldendrin, a novel neuronal calcium-binding protein confined to the somato-dendritic compartment."
    Seidenbecher C.I., Langnaese K., Sanmarti-Vila L., Boeckers T.M., Smalla K.-H., Sabel B.A., Garner C.C., Gundelfinger E.D., Kreutz M.R.
    J. Biol. Chem. 273:21324-21331(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: ALTERNATIVE SPLICING (ISOFORM CALDENDRIN).
  6. "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 ITPR1; ITPR2 AND ITPR3, MUTAGENESIS OF ASP-238; ASP-240; ASP-315; ASN-317; ASP-352 AND ASN-354.
  7. "Differential modulation of Ca(v)2.1 channels by calmodulin and Ca2+-binding protein 1."
    Lee A., Westenbroek R.E., Haeseleer F., Palczewski K., Scheuer T., Catterall W.A.
    Nat. Neurosci. 5:210-217(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH CACNA1A.
  8. Cited for: PHOSPHORYLATION AT SER-323, MUTAGENESIS OF SER-323, SUBCELLULAR LOCATION, INTERACTION WITH ITPR1.
  9. "Calcium-binding protein 1 is an inhibitor of agonist-evoked, inositol 1,4,5-trisphosphate-mediated calcium signaling."
    Haynes L.P., Tepikin A.V., Burgoyne R.D.
    J. Biol. Chem. 279:547-555(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  10. "Caldendrin but not calmodulin binds to light chain 3 of MAP1A/B: an association with the microtubule cytoskeleton highlighting exclusive binding partners for neuronal Ca(2+)-sensor proteins."
    Seidenbecher C.I., Landwehr M., Smalla K.H., Kreutz M., Dieterich D.C., Zuschratter W., Reissner C., Hammarback J.A., Bockers T.M., Gundelfinger E.D., Kreutz M.R.
    J. Mol. Biol. 336:957-970(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MAP1LC3B.
  11. "Ca2+-binding protein-1 facilitates and forms a postsynaptic complex with Cav1.2 (L-type) Ca2+ channels."
    Zhou H., Kim S.-A., Kirk E.A., Tippens A.L., Sun H., Haeseleer F., Lee A.
    J. Neurosci. 24:4698-4708(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH CACNA1C.
  12. "Molecular mechanism for divergent regulation of Cav1.2 Ca2+ channels by calmodulin and Ca2+-binding protein-1."
    Zhou H., Yu K., McCoy K.L., Lee A.
    J. Biol. Chem. 280:29612-29619(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH CACNA1C.
  13. "Inhibition of TRPC5 channels by Ca2+-binding protein 1 in Xenopus oocytes."
    Kinoshita-Kawada M., Tang J., Xiao R., Kaneko S., Foskett J.K., Zhu M.X.
    Pflugers Arch. 450:345-354(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH TRPC5.
  14. "Structural analysis of Mg2+ and Ca2+ binding to CaBP1, a neuron-specific regulator of calcium channels."
    Wingard J.N., Chan J., Bosanac I., Haeseleer F., Palczewski K., Ikura M., Ames J.B.
    J. Biol. Chem. 280:37461-37470(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT, CALCIUM-BINDING, MAGNESIUM-BINDING.
  15. "Structural insights into Ca2+-dependent regulation of inositol 1,4,5-trisphosphate receptors by CaBP1."
    Li C., Chan J., Haeseleer F., Mikoshiba K., Palczewski K., Ikura M., Ames J.B.
    J. Biol. Chem. 284:2472-2481(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 219-294 AND 299-370 IN COMPLEX WITH MAGNESIUM AND CALCIUM, MUTAGENESIS OF ASP-238; ASP-240; ASP-242 AND ASP-249.

Entry informationi

Entry nameiCABP1_HUMAN
AccessioniPrimary (citable) accession number: Q9NZU7
Secondary accession number(s): O95663, Q8N6H5, Q9NZU8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: May 31, 2011
Last modified: October 29, 2014
This is version 125 of the entry and version 5 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, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3