Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Calcium-binding protein 1

Gene

CABP1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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 similarity5 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi238Magnesium1 Publication1
Metal bindingi240Magnesium1 Publication1
Metal bindingi242Magnesium1 Publication1
Metal bindingi244Magnesium; via carbonyl oxygen1 Publication1
Metal bindingi315Calcium 11 Publication1
Metal bindingi317Calcium 11 Publication1
Metal bindingi319Calcium 11 Publication1
Metal bindingi321Calcium 1; via carbonyl oxygen1 Publication1
Metal bindingi326Calcium 11 Publication1
Metal bindingi352Calcium 21 Publication1
Metal bindingi353Calcium 2; via amide nitrogen1 Publication1
Metal bindingi354Calcium 21 Publication1
Metal bindingi356Calcium 21 Publication1
Metal bindingi357Calcium 2; via amide nitrogen1 Publication1
Metal bindingi358Calcium 2; via carbonyl oxygen1 Publication1
Metal bindingi360Calcium 21 Publication1
Metal bindingi363Calcium 21 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Calcium bindingi238 – 2491Add BLAST12
Calcium bindingi315 – 3262Add BLAST12
Calcium bindingi352 – 3633Add BLAST12

GO - Molecular functioni

  • calcium-dependent protein binding Source: UniProtKB
  • calcium ion binding Source: ProtInc
  • enzyme inhibitor activity Source: ProtInc
  • nuclear localization sequence binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

Calcium, Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciZFISH:ENSG00000157782-MONOMER.

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
Proteomesi
  • UP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:1384. CABP1.

Subcellular locationi

Isoform L-CaBP1 :
Isoform S-CaBP1 :

GO - Cellular componenti

  • cell cortex Source: UniProtKB-SubCell
  • cell junction Source: UniProtKB-KW
  • cytoskeleton Source: UniProtKB-SubCell
  • extracellular space Source: UniProtKB
  • Golgi membrane Source: MGI
  • perinuclear region of cytoplasm Source: UniProtKB-SubCell
  • plasma membrane Source: MGI
  • postsynaptic density Source: UniProtKB
  • postsynaptic membrane Source: UniProtKB-KW
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)DescriptionActionsGraphical viewLength
Mutagenesisi238D → 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 Publications1
Mutagenesisi240D → 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 Publications1
Mutagenesisi242D → A: Loss of magnesium-binding. 1 Publication1
Mutagenesisi249D → A: No effect on magnesium-binding. 1 Publication1
Mutagenesisi315D → A: Loss of binding to ITPRs; when associated with A-238; A-240; A-317; A-352 and A-354. 1 Publication1
Mutagenesisi317N → A: Loss of binding to ITPRs; when associated with A-238; A-240; A-315; A-352 and A-354. 1 Publication1
Mutagenesisi323S → A: Loss of phosphorylation and loss of calcium release by InsP(3). 1 Publication1
Mutagenesisi352D → A: Loss of binding to ITPRs; when associated with A-238; A-240; A-315; A-317 and A-354. 1 Publication1
Mutagenesisi354N → A: Loss of binding to ITPRs; when associated with A-238; A-240; A-315; A-317 and A-352. 1 Publication1

Organism-specific databases

OpenTargetsiENSG00000157782.
PharmGKBiPA26000.

Polymorphism and mutation databases

BioMutaiCABP1.
DMDMi334302962.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedSequence analysis
ChainiPRO_00000735132 – 370Calcium-binding protein 1Add BLAST369

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Lipidationi2N-myristoyl glycineSequence analysis1
Modified residuei323Phosphoserine1 Publication1
Isoform L-CaBP1 (identifier: Q9NZU7-1)
Lipidationi2N-myristoyl glycine1
Isoform S-CaBP1 (identifier: Q9NZU7-2)
Lipidationi2N-myristoyl glycine1

Post-translational modificationi

Phosphorylated. The phosphorylation regulates the activity.1 Publication

Keywords - PTMi

Lipoprotein, Myristate, Phosphoprotein

Proteomic databases

PaxDbiQ9NZU7.
PeptideAtlasiQ9NZU7.
PRIDEiQ9NZU7.

PTM databases

iPTMnetiQ9NZU7.
PhosphoSitePlusiQ9NZU7.

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

BgeeiENSG00000157782.
CleanExiHS_CABP1.
ExpressionAtlasiQ9NZU7. baseline and differential.
GenevisibleiQ9NZU7. HS.

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. Interacts with SPACA9 (By similarity).By similarity6 Publications

Binary interactionsi

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

GO - Molecular functioni

  • calcium-dependent protein binding Source: UniProtKB

Protein-protein interaction databases

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

Structurei

Secondary structure

1370
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi224 – 240Combined sources17
Beta strandi242 – 244Combined sources3
Helixi247 – 256Combined sources10
Helixi263 – 274Combined sources12
Beta strandi277 – 279Combined sources3
Helixi283 – 294Combined sources12
Helixi299 – 302Combined sources4
Helixi304 – 314Combined sources11
Beta strandi319 – 322Combined sources4
Helixi324 – 335Combined sources12
Beta strandi337 – 339Combined sources3
Helixi341 – 351Combined sources11
Beta strandi353 – 359Combined sources7
Helixi361 – 367Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9NZU7.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini225 – 260EF-hand 1PROSITE-ProRule annotationAdd BLAST36
Domaini261 – 296EF-hand 2PROSITE-ProRule annotationAdd BLAST36
Domaini302 – 337EF-hand 3PROSITE-ProRule annotationAdd BLAST36
Domaini339 – 370EF-hand 4PROSITE-ProRule annotationAdd BLAST32

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi45 – 48Poly-Pro4
Compositional biasi74 – 79Poly-Ala6
Compositional biasi86 – 164Pro-richAdd BLAST79

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

eggNOGiKOG0027. Eukaryota.
COG5126. LUCA.
GeneTreeiENSGT00760000118901.
HOGENOMiHOG000233018.
HOVERGENiHBG012180.
InParanoidiQ9NZU7.
OrthoDBiEOG091G0PB4.
PhylomeDBiQ9NZU7.
TreeFamiTF334804.

Family and domain databases

CDDicd00051. EFh. 2 hits.
Gene3Di1.10.238.10. 2 hits.
InterProiIPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
[Graphical view]
PfamiPF13499. EF-hand_7. 2 hits.
[Graphical view]
SMARTiSM00054. EFh. 3 hits.
[Graphical view]
SUPFAMiSSF47473. SSF47473. 1 hit.
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. AlignAdd to basket

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: Deamidated on Asn-3. S-palmitoylated on Cys-4.
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: Deamidated on Asn-3. S-palmitoylated on Cys-4.
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)DescriptionActionsGraphical viewLength
Sequence conflicti140Q → R in AAH30201 (PubMed:15489334).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0379361 – 300Missing in isoform Calbrain. 1 PublicationAdd BLAST300
Alternative sequenceiVSP_0379371 – 203Missing in isoform S-CaBP1. 1 PublicationAdd BLAST203
Alternative sequenceiVSP_0379381 – 143Missing in isoform L-CaBP1. 1 PublicationAdd BLAST143
Alternative sequenceiVSP_037939144 – 218RPREA…SAFGQ → MGNCVKYPLRNLSRKMCQEE QTSYMVVQTSEEGLAADAEL PGPLLMLAQNCAVMHNLLGP ACIFLRKGFAENRQP in isoform L-CaBP1. 1 PublicationAdd BLAST75
Alternative sequenceiVSP_037940204 – 218FLHRL…SAFGQ → MGNCVKYPLRNLSRK in isoform S-CaBP1. 1 PublicationAdd BLAST15

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.4. human. [Q9NZU7-4]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

PTM databases

iPTMnetiQ9NZU7.
PhosphoSitePlusiQ9NZU7.

Polymorphism and mutation databases

BioMutaiCABP1.
DMDMi334302962.

Proteomic databases

PaxDbiQ9NZU7.
PeptideAtlasiQ9NZU7.
PRIDEiQ9NZU7.

Protocols and materials databases

DNASUi9478.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi9478.
GeneCardsiCABP1.
HGNCiHGNC:1384. CABP1.
HPAiHPA051438.
MIMi605563. gene.
neXtProtiNX_Q9NZU7.
OpenTargetsiENSG00000157782.
PharmGKBiPA26000.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0027. Eukaryota.
COG5126. LUCA.
GeneTreeiENSGT00760000118901.
HOGENOMiHOG000233018.
HOVERGENiHBG012180.
InParanoidiQ9NZU7.
OrthoDBiEOG091G0PB4.
PhylomeDBiQ9NZU7.
TreeFamiTF334804.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000157782-MONOMER.

Miscellaneous databases

ChiTaRSiCABP1. human.
EvolutionaryTraceiQ9NZU7.
GenomeRNAii9478.
PROiQ9NZU7.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000157782.
CleanExiHS_CABP1.
ExpressionAtlasiQ9NZU7. baseline and differential.
GenevisibleiQ9NZU7. HS.

Family and domain databases

CDDicd00051. EFh. 2 hits.
Gene3Di1.10.238.10. 2 hits.
InterProiIPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
[Graphical view]
PfamiPF13499. EF-hand_7. 2 hits.
[Graphical view]
SMARTiSM00054. EFh. 3 hits.
[Graphical view]
SUPFAMiSSF47473. SSF47473. 1 hit.
PROSITEiPS00018. EF_HAND_1. 3 hits.
PS50222. EF_HAND_2. 4 hits.
[Graphical view]
ProtoNetiSearch...

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: November 30, 2016
This is version 144 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

Caution

The interaction with CACNA1A is described as calcium independent in PubMed:11865310 while it is shown to be acutely calcium dependent in PubMed:14570872. PubMed:12032348 describes a stimulatory effect of CABP1 during agonist-induced intracellular calcium signaling while PubMed:14570872 and PubMed:11865310 show an inhibitory effect.Curated

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.