Q9NZU7 (CABP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Calcium-binding protein 1
Short name=CaBP1

Alternative name(s):
Calbrain
Caldendrin

Gene names

Name:

CABP1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	370 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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	Cytoplasm › cytoskeleton. Cytoplasm › perinuclear region. Cell membrane; Lipid-anchor; Cytoplasmic side. Golgi apparatus. Cell junction › synapse › postsynaptic cell membrane › postsynaptic 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: Cytoplasm › cytoskeleton. Note: L-CaBP1 is associated most likely with the cytoskeletal structures. Ref.8 Ref.9 Isoform S-CaBP1: Cytoplasm › cell 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 component	Cell junction Cell membrane Cytoplasm Cytoskeleton Golgi apparatus Membrane Postsynaptic cell membrane Synapse
Coding sequence diversity	Alternative splicing
Domain	Repeat
Ligand	Calcium Magnesium Metal-binding
PTM	Lipoprotein Myristate Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	negative regulation of protein import into nucleus Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	Golgi 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 neuronal cell body Inferred from electronic annotation. Source: Compara nucleus Inferred from electronic annotation. Source: Compara 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
Molecular_function	calcium ion binding Traceable author statement Ref.1. Source: ProtInc enzyme inhibitor activity Traceable author statement Ref.1. Source: ProtInc nuclear localization sequence binding Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CACNA1C	Q13936	4	EBI-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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Potential

Chain

2 – 370

369

Calcium-binding protein 1

PRO_0000073513

Regions

Domain

225 – 260

36

EF-hand 1

Domain

261 – 296

36

EF-hand 2

Domain

302 – 337

36

EF-hand 3

Domain

339 – 370

32

EF-hand 4

Calcium binding

238 – 249

12

1 Ref.14

Calcium binding

315 – 326

12

2 Ref.14

Calcium binding

352 – 363

12

3 Ref.14

Compositional bias

45 – 48

4

Poly-Pro

Compositional bias

74 – 79

6

Poly-Ala

Compositional bias

86 – 164

79

Pro-rich

Sites

Metal binding

238

1

Magnesium

Metal binding

240

1

Magnesium

Metal binding

242

1

Magnesium

Metal binding

244

1

Magnesium; via carbonyl oxygen

Metal binding

315

1

Calcium 1

Metal binding

317

1

Calcium 1

Metal binding

319

1

Calcium 1

Metal binding

321

1

Calcium 1; via carbonyl oxygen

Metal binding

326

1

Calcium 1

Metal binding

352

1

Calcium 2

Metal binding

353

1

Calcium 2; via amide nitrogen

Metal binding

354

1

Calcium 2

Metal binding

356

1

Calcium 2

Metal binding

357

1

Calcium 2; via amide nitrogen

Metal binding

358

1

Calcium 2; via carbonyl oxygen

Metal binding

360

1

Calcium 2

Metal binding

363

1

Calcium 2

Amino acid modifications

Modified residue

323

1

Phosphoserine Ref.8

Lipidation

2

1

N-myristoyl glycine Potential

Natural variations

Alternative sequence

1 – 300

300

Missing in isoform Calbrain.

VSP_037936

Alternative sequence

1 – 203

203

Missing in isoform S-CaBP1.

VSP_037937

Alternative sequence

1 – 143

143

Missing in isoform L-CaBP1.

VSP_037938

Alternative sequence

144 – 218

75

RPREA…SAFGQ → MGNCVKYPLRNLSRKMCQEE QTSYMVVQTSEEGLAADAEL PGPLLMLAQNCAVMHNLLGP ACIFLRKGFAENRQP in isoform L-CaBP1.

VSP_037939

Alternative sequence

204 – 218

15

FLHRL…SAFGQ → MGNCVKYPLRNLSRK in isoform S-CaBP1.

VSP_037940

Experimental info

Mutagenesis

238

1

D → 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

Mutagenesis

240

1

D → 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

Mutagenesis

242

1

D → A: Loss of magnesium-binding. Ref.15

Mutagenesis

249

1

D → A: No effect on magnesium-binding. Ref.15

Mutagenesis

315

1

D → A: Loss of binding to ITPRs; when associated with A-238; A-240; A-317; A-352 and A-354. Ref.6

Mutagenesis

317

1

N → A: Loss of binding to ITPRs; when associated with A-238; A-240; A-315; A-352 and A-354. Ref.6

Mutagenesis

323

1

S → A: Loss of phosphorylation and loss of calcium release by InsP(3). Ref.8

Mutagenesis

352

1

D → A: Loss of binding to ITPRs; when associated with A-238; A-240; A-315; A-317 and A-354. Ref.6

Mutagenesis

354

1

N → A: Loss of binding to ITPRs; when associated with A-238; A-240; A-315; A-317 and A-352. Ref.6

Sequence conflict

140

1

Q → R in AAH30201. Ref.4

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

370

Helix Strand Turn

Details...

Helix

224 – 240

17

Beta strand

242 – 244

3

Helix

247 – 256

10

Helix

263 – 274

12

Beta strand

277 – 279

3

Helix

283 – 294

12

Helix

299 – 302

4

Helix

304 – 314

11

Beta strand

319 – 322

4

Helix

324 – 335

12

Beta strand

337 – 339

3

Helix

341 – 351

11

Beta strand

353 – 359

7

Helix

361 – 367

7

Sequences

	Sequence		Length	Mass (Da)
	Isoform Caldendrin [UniParc]. Last modified May 31, 2011. Version 5. Checksum: 3444721152E01AA7	FASTA	370	39,838
	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
	Isoform L-CaBP1 (Caldendrin-S2) [UniParc]. Checksum: FF3F7A9B575486AB	FASTA	227	25,979
	10 20 30 40 50 60 MGNCVKYPLR NLSRKMCQEE QTSYMVVQTS EEGLAADAEL PGPLLMLAQN CAVMHNLLGP 70 80 90 100 110 120 ACIFLRKGFA ENRQPDRSLR PEEIEELREA FREFDKDKDG YINCRDLGNC MRTMGYMPTE 130 140 150 160 170 180 MELIELSQQI NMNLGGHVDF DDFVELMGPK LLAETADMIG VKELRDAFRE FDTNGDGEIS 190 200 210 220 TSELREAMRK LLGHQVGHRD IEEIIRDVDL NGDGRVDFEE FVRMMSR
	Isoform S-CaBP1 (Caldendrin-S1) [UniParc]. Checksum: B8C19D9E24D384FD	FASTA	167	19,430
	10 20 30 40 50 60 MGNCVKYPLR NLSRKDRSLR PEEIEELREA FREFDKDKDG YINCRDLGNC MRTMGYMPTE 70 80 90 100 110 120 MELIELSQQI NMNLGGHVDF DDFVELMGPK LLAETADMIG VKELRDAFRE FDTNGDGEIS 130 140 150 160 TSELREAMRK LLGHQVGHRD IEEIIRDVDL NGDGRVDFEE FVRMMSR
	Isoform Calbrain [UniParc]. Checksum: 2807BEB35ADCDA48	FASTA	70	8,139
	10 20 30 40 50 60 MIGVKELRDA FREFDTNGDG EISTSELREA MRKLLGHQVG HRDIEEIIRD VDLNGDGRVD 70 FEEFVRMMSR

References

	« Hide 'large scale' referencesShow '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. , 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.

IPI

IPI00003571.
IPI00220810.
IPI00297321.
IPI00472586.

RefSeq

NP_001028849.1. NM_001033677.1.
NP_004267.2. NM_004276.4.
NP_112482.1. NM_031205.3.

UniGene

Hs.458482.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

Q9NZU7.

SMR

Q9NZU7. Positions 219-370.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-35477N.

IntAct

Q9NZU7. 4 interactions.

STRING

9606.ENSP00000317310.

PTM databases

PhosphoSite

Q9NZU7.

Polymorphism databases

DMDM

257051082.

Proteomic databases

PaxDb

Q9NZU7.

PRIDE

Q9NZU7.

Protocols and materials databases

DNASU

9478.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000288616; ENSP00000288616; ENSG00000157782.
ENST00000316803; ENSP00000317310; ENSG00000157782.
ENST00000351200; ENSP00000288615; ENSG00000157782.

GeneID

9478.

KEGG

hsa:9478.

UCSC

uc001tyu.3. human.
uc001tyv.3. human.
uc001tyw.3. human.

Organism-specific databases

CTD

9478.

GeneCards

GC12P121078.

HGNC

HGNC:1384. CABP1.

HPA

HPA051438.

MIM

605563. gene.

neXtProt

NX_Q9NZU7.

PharmGKB

PA26000.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG5126.

HOGENOM

HOG000233018.

HOVERGEN

HBG012180.

OrthoDB

EOG44BB3F.

Gene expression databases

ArrayExpress

Q9NZU7.

Bgee

Q9NZU7.

CleanEx

HS_CABP1.

Genevestigator

Q9NZU7.

GermOnline

ENSG00000157782. Homo sapiens.

Family and domain databases

Gene3D

1.10.238.10. 2 hits.

InterPro

IPR011992. EF-hand-like_dom.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
[Graphical view]

Pfam

PF00036. efhand. 3 hits.
[Graphical view]

SMART

SM00054. EFh. 3 hits.
[Graphical view]

PROSITE

PS00018. EF_HAND_1. 3 hits.
PS50222. EF_HAND_2. 4 hits.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

CABP1. human.

EvolutionaryTrace

Q9NZU7.

GenomeRNAi

9478.

NextBio

35520.

SOURCE

Search...

Entry information

Entry name

CABP1_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 112 of the entry and version 5 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.