Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9NZU7 (CABP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 123. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Calcium-binding protein 1

Short name=CaBP1
Alternative name(s):
Calbrain
Caldendrin
Gene names
Name:CABP1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length370 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.7 Ref.9 Ref.11 Ref.12 Ref.13

Subunit structure

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. Ref.6 Ref.7 Ref.8 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14

Subcellular location

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. Ref.8 Ref.9

Isoform L-CaBP1: Cytoplasmcytoskeleton. Note: L-CaBP1 is associated most likely with the cytoskeletal structures. Ref.8 Ref.9

Isoform S-CaBP1: Cytoplasmcell cortex. Cell membrane; Lipid-anchor Probable. Note: S-CaBP1 is localized at or near the plasma membrane. Ref.8 Ref.9

Tissue specificity

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.

Domain

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

Post-translational modification

Phosphorylated. The phosphorylation regulates the activity. Ref.8

Sequence similarities

Contains 4 EF-hand domains.

Caution

The interaction with CACNA1A is described as calcium independent in Ref.7 while it is shown to be acutely calcium dependent in Ref.9. Ref.6 describes a stimulatory effect of CABP1 during agonist-induced intracellular calcium signaling while Ref.9 and Ref.7 show an inhibitory effect.

Ontologies

Keywords
   Cellular componentCell junction
Cell membrane
Cytoplasm
Cytoskeleton
Golgi apparatus
Membrane
Postsynaptic cell membrane
Synapse
   Coding sequence diversityAlternative splicing
   DomainRepeat
   LigandCalcium
Magnesium
Metal-binding
   PTMLipoprotein
Myristate
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processnegative regulation of catalytic activity

Traceable author statement Ref.1. Source: GOC

negative regulation of cell communication by electrical coupling

Inferred from electronic annotation. Source: Ensembl

negative regulation of protein import into nucleus

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of voltage-gated calcium channel activity

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentGolgi membrane

Inferred from direct assay PubMed 19338761. Source: MGI

cell cortex

Inferred from electronic annotation. Source: UniProtKB-SubCell

cell junction

Inferred from electronic annotation. Source: UniProtKB-KW

cytoplasmic side of plasma membrane

Inferred from electronic annotation. Source: Ensembl

cytosol

Inferred from electronic annotation. Source: Ensembl

dendrite

Inferred from electronic annotation. Source: Ensembl

extracellular space

Inferred from direct assay PubMed 22664934. Source: UniProt

neuronal cell body

Inferred from electronic annotation. Source: Ensembl

nucleus

Inferred from electronic annotation. Source: Ensembl

perinuclear region of cytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Inferred from direct assay PubMed 19338761. Source: MGI

postsynaptic density

Inferred from direct assay Ref.11. Source: UniProtKB

postsynaptic membrane

Inferred from electronic annotation. Source: UniProtKB-KW

protein complex

Inferred from electronic annotation. Source: Ensembl

   Molecular_functioncalcium ion binding

Traceable author statement Ref.1. Source: ProtInc

calcium-dependent protein binding

Inferred from physical interaction Ref.12. Source: UniProtKB

enzyme inhibitor activity

Traceable author statement Ref.1. Source: ProtInc

nuclear localization sequence binding

Inferred from sequence or structural similarity. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.11Ref.7. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

CACNA1CQ139364EBI-907894,EBI-1038838

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Note: Experimental confirmation may be lacking for some isoforms.
Isoform Caldendrin (identifier: Q9NZU7-4)

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 L-CaBP1 (identifier: Q9NZU7-1)

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.
Isoform S-CaBP1 (identifier: Q9NZU7-2)

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.
Isoform Calbrain (identifier: Q9NZU7-3)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Potential
Chain2 – 370369Calcium-binding protein 1
PRO_0000073513

Regions

Domain225 – 26036EF-hand 1
Domain261 – 29636EF-hand 2
Domain302 – 33736EF-hand 3
Domain339 – 37032EF-hand 4
Calcium binding238 – 249121 Ref.14
Calcium binding315 – 326122 Ref.14
Calcium binding352 – 363123 Ref.14
Compositional bias45 – 484Poly-Pro
Compositional bias74 – 796Poly-Ala
Compositional bias86 – 16479Pro-rich

Sites

Metal binding2381Magnesium
Metal binding2401Magnesium
Metal binding2421Magnesium
Metal binding2441Magnesium; via carbonyl oxygen
Metal binding3151Calcium 1
Metal binding3171Calcium 1
Metal binding3191Calcium 1
Metal binding3211Calcium 1; via carbonyl oxygen
Metal binding3261Calcium 1
Metal binding3521Calcium 2
Metal binding3531Calcium 2; via amide nitrogen
Metal binding3541Calcium 2
Metal binding3561Calcium 2
Metal binding3571Calcium 2; via amide nitrogen
Metal binding3581Calcium 2; via carbonyl oxygen
Metal binding3601Calcium 2
Metal binding3631Calcium 2

Amino acid modifications

Modified residue3231Phosphoserine Ref.8
Lipidation21N-myristoyl glycine Potential

Natural variations

Alternative sequence1 – 300300Missing in isoform Calbrain.
VSP_037936
Alternative sequence1 – 203203Missing in isoform S-CaBP1.
VSP_037937
Alternative sequence1 – 143143Missing in isoform L-CaBP1.
VSP_037938
Alternative sequence144 – 21875RPREA…SAFGQ → MGNCVKYPLRNLSRKMCQEE QTSYMVVQTSEEGLAADAEL PGPLLMLAQNCAVMHNLLGP ACIFLRKGFAENRQP in isoform L-CaBP1.
VSP_037939
Alternative sequence204 – 21815FLHRL…SAFGQ → MGNCVKYPLRNLSRK in isoform S-CaBP1.
VSP_037940

Experimental info

Mutagenesis2381D → A: Loss of magnesium-binding. Loss of binding to ITPRs; when associated with A-240; A-315; A-317; A-352 and A-354. Ref.6 Ref.15
Mutagenesis2401D → A: Loss of magnesium-binding. Loss of binding to ITPRs; when associated with A-238; A-315; A-317; A-352 and A-354. Ref.6 Ref.15
Mutagenesis2421D → A: Loss of magnesium-binding. Ref.15
Mutagenesis2491D → A: No effect on magnesium-binding. Ref.15
Mutagenesis3151D → A: Loss of binding to ITPRs; when associated with A-238; A-240; A-317; A-352 and A-354. Ref.6
Mutagenesis3171N → A: Loss of binding to ITPRs; when associated with A-238; A-240; A-315; A-352 and A-354. Ref.6
Mutagenesis3231S → A: Loss of phosphorylation and loss of calcium release by InsP(3). Ref.8
Mutagenesis3521D → A: Loss of binding to ITPRs; when associated with A-238; A-240; A-315; A-317 and A-354. Ref.6
Mutagenesis3541N → A: Loss of binding to ITPRs; when associated with A-238; A-240; A-315; A-317 and A-352. Ref.6
Sequence conflict1401Q → R in AAH30201. Ref.4

Secondary structure

............................. 370
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform Caldendrin [UniParc].

Last modified May 31, 2011. Version 5.
Checksum: 3444721152E01AA7

FASTA37039,838
        10         20         30         40         50         60 
MGGGDGAAFK RPGDGARLQR VLGLGSRREP RSLPAGGPAP RRTAPPPPGH ASAGPAAMSS 

        70         80         90        100        110        120 
HIAKSESKTS LLKAAAAAAS GGSRAPRHGP ARDPGLPSRR LPGSCPATPQ SSGDPSSRRP 

       130        140        150        160        170        180 
LCRPAPREEG ARGSQRVLPQ AHCRPREALP AAASRPSPSS PLPPARGRDG EERGLSPALG 

       190        200        210        220        230        240 
LRGSLRARGR GDSVPAAASE ADPFLHRLRP MLSSAFGQDR SLRPEEIEEL REAFREFDKD 

       250        260        270        280        290        300 
KDGYINCRDL GNCMRTMGYM PTEMELIELS QQINMNLGGH VDFDDFVELM GPKLLAETAD 

       310        320        330        340        350        360 
MIGVKELRDA FREFDTNGDG EISTSELREA MRKLLGHQVG HRDIEEIIRD VDLNGDGRVD 

       370 
FEEFVRMMSR 

« Hide

Isoform L-CaBP1 (Caldendrin-S2) [UniParc].

Checksum: FF3F7A9B575486AB
Show »

FASTA22725,979
Isoform S-CaBP1 (Caldendrin-S1) [UniParc].

Checksum: B8C19D9E24D384FD
Show »

FASTA16719,430
Isoform Calbrain [UniParc].

Checksum: 2807BEB35ADCDA48
Show »

FASTA708,139

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"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: 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS31913.1. [Q9NZU7-4]
CCDS9204.1. [Q9NZU7-2]
CCDS9205.1. [Q9NZU7-1]
RefSeqNP_001028849.1. NM_001033677.1. [Q9NZU7-4]
NP_004267.2. NM_004276.4. [Q9NZU7-2]
NP_112482.1. NM_031205.3. [Q9NZU7-1]
UniGeneHs.458482.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalQ9NZU7.
SMRQ9NZU7. Positions 219-370.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114863. 8 interactions.
DIPDIP-35477N.
IntActQ9NZU7. 4 interactions.
STRING9606.ENSP00000317310.

PTM databases

PhosphoSiteQ9NZU7.

Polymorphism databases

DMDM334302962.

Proteomic databases

PaxDbQ9NZU7.
PRIDEQ9NZU7.

Protocols and materials databases

DNASU9478.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000288616; ENSP00000288616; ENSG00000157782. [Q9NZU7-1]
ENST00000316803; ENSP00000317310; ENSG00000157782. [Q9NZU7-4]
ENST00000351200; ENSP00000288615; ENSG00000157782. [Q9NZU7-2]
GeneID9478.
KEGGhsa:9478.
UCSCuc001tyu.3. human. [Q9NZU7-4]
uc001tyv.4. human. [Q9NZU7-1]
uc001tyw.4. human. [Q9NZU7-2]

Organism-specific databases

CTD9478.
GeneCardsGC12P121078.
HGNCHGNC:1384. CABP1.
HPAHPA051438.
MIM605563. gene.
neXtProtNX_Q9NZU7.
PharmGKBPA26000.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5126.
HOGENOMHOG000233018.
HOVERGENHBG012180.
OrthoDBEOG7XM303.
PhylomeDBQ9NZU7.
TreeFamTF334804.

Gene expression databases

ArrayExpressQ9NZU7.
BgeeQ9NZU7.
CleanExHS_CABP1.
GenevestigatorQ9NZU7.

Family and domain databases

Gene3D1.10.238.10. 2 hits.
InterProIPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
[Graphical view]
PfamPF00036. EF-hand_1. 3 hits.
[Graphical view]
SMARTSM00054. EFh. 3 hits.
[Graphical view]
PROSITEPS00018. EF_HAND_1. 3 hits.
PS50222. EF_HAND_2. 4 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCABP1. human.
EvolutionaryTraceQ9NZU7.
GenomeRNAi9478.
NextBio35520.
PROQ9NZU7.
SOURCESearch...

Entry information

Entry nameCABP1_HUMAN
AccessionPrimary (citable) accession number: Q9NZU7
Secondary accession number(s): O95663, Q8N6H5, Q9NZU8
Entry history
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: May 31, 2011
Last modified: July 9, 2014
This is version 123 of the entry and version 5 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM