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Protein

Voltage-dependent L-type calcium channel subunit beta-3

Gene

CACNB3

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

Functioni

The beta subunit of voltage-dependent calcium channels contributes to the function of the calcium channel by increasing peak calcium current, shifting the voltage dependencies of activation and inactivation, modulating G protein inhibition and controlling the alpha-1 subunit membrane targeting.

GO - Molecular functioni

  1. high voltage-gated calcium channel activity Source: GO_Central
  2. voltage-gated calcium channel activity Source: ProtInc

GO - Biological processi

  1. axon guidance Source: Reactome
  2. calcium ion transport Source: UniProtKB
  3. membrane depolarization Source: Reactome
  4. neuromuscular junction development Source: GO_Central
  5. regulation of voltage-gated calcium channel activity Source: GO_Central
  6. synaptic transmission Source: GO_Central
  7. T cell receptor signaling pathway Source: Ensembl
  8. transport Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Calcium channel, Ion channel, Voltage-gated channel

Keywords - Biological processi

Calcium transport, Ion transport, Transport

Keywords - Ligandi

Calcium

Enzyme and pathway databases

ReactomeiREACT_13606. Depolarization of the Presynaptic Terminal Triggers the Opening of Calcium Channels.
REACT_18312. NCAM1 interactions.
REACT_18325. Regulation of insulin secretion.
REACT_18339. Adrenaline,noradrenaline inhibits insulin secretion.

Protein family/group databases

TCDBi8.A.22.1.3. the ca(2+) channel auxiliary subunit types 1-4 (cca-) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Voltage-dependent L-type calcium channel subunit beta-3
Short name:
CAB3
Alternative name(s):
Calcium channel voltage-dependent subunit beta 3
Gene namesi
Name:CACNB3
Synonyms:CACNLB3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 12

Organism-specific databases

HGNCiHGNC:1403. CACNB3.

Subcellular locationi

GO - Cellular componenti

  1. apical plasma membrane Source: Ensembl
  2. cytosol Source: Reactome
  3. membrane Source: UniProtKB
  4. voltage-gated calcium channel complex Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA89.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 484484Voltage-dependent L-type calcium channel subunit beta-3PRO_0000144056Add
BLAST

Proteomic databases

MaxQBiP54284.
PaxDbiP54284.
PRIDEiP54284.

PTM databases

PhosphoSiteiP54284.

Expressioni

Tissue specificityi

Expressed mostly in brain, smooth muscle and ovary.

Gene expression databases

BgeeiP54284.
CleanExiHS_CACNB3.
ExpressionAtlasiP54284. baseline and differential.
GenevestigatoriP54284.

Interactioni

Subunit structurei

The L-type calcium channel is composed of four subunits: alpha-1, alpha-2, beta and gamma. Interacts with CACNA2D4. Interacts with FASLG.2 Publications

Protein-protein interaction databases

BioGridi107238. 3 interactions.
DIPiDIP-39138N.
IntActiP54284. 2 interactions.
STRINGi9606.ENSP00000301050.

Structurei

3D structure databases

ProteinModelPortaliP54284.
SMRiP54284. Positions 1-362.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini59 – 12062SH3Add
BLAST

Sequence similaritiesi

Contains 1 SH3 domain.Curated

Keywords - Domaini

SH3 domain

Phylogenomic databases

eggNOGiNOG326500.
GeneTreeiENSGT00390000002740.
HOGENOMiHOG000230979.
HOVERGENiHBG050765.
InParanoidiP54284.
KOiK04864.
OMAiDIYWRAT.
PhylomeDBiP54284.
TreeFamiTF316195.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR008145. GK/Ca_channel_bsu.
IPR027417. P-loop_NTPase.
IPR001452. SH3_domain.
IPR008079. VDCC_L_b3su.
IPR000584. VDCC_L_bsu.
[Graphical view]
PANTHERiPTHR11824. PTHR11824. 1 hit.
PfamiPF00625. Guanylate_kin. 1 hit.
PF12052. VGCC_beta4Aa_N. 1 hit.
[Graphical view]
PRINTSiPR01626. LCACHANNELB.
PR01696. LCACHANNELB3.
SMARTiSM00072. GuKc. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 1 hit.
SSF52540. SSF52540. 1 hit.

Sequences (5)i

Sequence statusi: Complete.

This entry describes 5 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P54284-1) [UniParc]FASTAAdd to Basket

Also known as: 3A

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
MYDDSYVPGF EDSEAGSADS YTSRPSLDSD VSLEEDRESA RREVESQAQQ
60 70 80 90 100
QLERAKHKPV AFAVRTNVSY CGVLDEECPV QGSGVNFEAK DFLHIKEKYS
110 120 130 140 150
NDWWIGRLVK EGGDIAFIPS PQRLESIRLK QEQKARRSGN PSSLSDIGNR
160 170 180 190 200
RSPPPSLAKQ KQKQAEHVPP YDVVPSMRPV VLVGPSLKGY EVTDMMQKAL
210 220 230 240 250
FDFLKHRFDG RISITRVTAD LSLAKRSVLN NPGKRTIIER SSARSSIAEV
260 270 280 290 300
QSEIERIFEL AKSLQLVVLD ADTINHPAQL AKTSLAPIIV FVKVSSPKVL
310 320 330 340 350
QRLIRSRGKS QMKHLTVQMM AYDKLVQCPP ESFDVILDEN QLEDACEHLA
360 370 380 390 400
EYLEVYWRAT HHPAPGPGLL GPPSAIPGLQ NQQLLGERGE EHSPLERDSL
410 420 430 440 450
MPSDEASESS RQAWTGSSQR SSRHLEEDYA DAYQDLYQPH RQHTSGLPSA
460 470 480
NGHDPQDRLL AQDSEHNHSD RNWQRNRPWP KDSY
Length:484
Mass (Da):54,532
Last modified:October 1, 1996 - v1
Checksum:i19CD3549F5A8E17A
GO
Isoform 2 (identifier: P54284-2) [UniParc]FASTAAdd to Basket

Also known as: 3B

The sequence of this isoform differs from the canonical sequence as follows:
     440-484: HRQHTSGLPSANGHDPQDRLLAQDSEHNHSDRNWQRNRPWPKDSY → QCQLLSLL

Show »
Length:447
Mass (Da):50,106
Checksum:iC2BCB90B9B4FEB3F
GO
Isoform 3 (identifier: P54284-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-15: MYDDSYVPGFEDSEA → ME

Note: No experimental confirmation available.

Show »
Length:471
Mass (Da):53,085
Checksum:i37BA075B29E7A52C
GO
Isoform 4 (identifier: P54284-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-15: MYDDSYVPGFEDSEA → MSFSDSSATFLLNE

Note: No experimental confirmation available.

Show »
Length:483
Mass (Da):54,356
Checksum:iC979431C760076AF
GO
Isoform 5 (identifier: P54284-5) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     57-97: Missing.

Note: Gene prediction based on EST data.

Show »
Length:443
Mass (Da):50,015
Checksum:i6A689973F8712530
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti7 – 71V → L in AAA19799. (PubMed:8119293)Curated
Sequence conflicti32 – 321Missing in AAA19799. (PubMed:8119293)Curated
Sequence conflicti60 – 601V → E in AAA19799. (PubMed:8119293)Curated
Sequence conflicti101 – 1011N → D in BAH14694. (PubMed:14702039)Curated
Sequence conflicti162 – 1621Q → R in BAH14209. (PubMed:14702039)Curated
Sequence conflicti196 – 1961M → T in BAH12637. (PubMed:14702039)Curated
Sequence conflicti245 – 2451S → P in BAH12637. (PubMed:14702039)Curated
Sequence conflicti320 – 3201Missing in AAA19799. (PubMed:8119293)Curated
Sequence conflicti348 – 3481H → L in AAA19799. (PubMed:8119293)Curated
Sequence conflicti421 – 4211S → T in AAA19799. (PubMed:8119293)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti423 – 4231R → H.
Corresponds to variant rs2229954 [ dbSNP | Ensembl ].
VAR_024384

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 1515MYDDS…EDSEA → ME in isoform 3. 1 PublicationVSP_046708Add
BLAST
Alternative sequencei1 – 1515MYDDS…EDSEA → MSFSDSSATFLLNE in isoform 4. 1 PublicationVSP_046709Add
BLAST
Alternative sequencei57 – 9741Missing in isoform 5. CuratedVSP_046710Add
BLAST
Alternative sequencei440 – 48445HRQHT…PKDSY → QCQLLSLL in isoform 2. 1 PublicationVSP_000634Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X76555 mRNA. Translation: CAA54055.1.
X76556 mRNA. Translation: CAA54056.1.
D43704 Genomic DNA. Translation: BAA07803.1.
U07139 mRNA. Translation: AAA95958.1.
L27584 mRNA. Translation: AAA19799.1.
AK289709 mRNA. Translation: BAF82398.1.
AK297639 mRNA. Translation: BAH12637.1.
AK304537 mRNA. Translation: BAH14209.1.
AK316323 mRNA. Translation: BAH14694.1.
AC117498 Genomic DNA. No translation available.
CH471111 Genomic DNA. Translation: EAW58008.1.
BC041811 mRNA. Translation: AAH41811.1.
CCDSiCCDS55821.1. [P54284-3]
CCDS55822.1. [P54284-4]
CCDS55823.1. [P54284-5]
CCDS8769.1. [P54284-1]
PIRiS39315.
S39316.
S41211.
RefSeqiNP_000716.2. NM_000725.3. [P54284-1]
NP_001193844.1. NM_001206915.1. [P54284-5]
NP_001193845.1. NM_001206916.1. [P54284-4]
NP_001193846.1. NM_001206917.1. [P54284-3]
UniGeneiHs.250712.
Hs.737291.

Genome annotation databases

EnsembliENST00000301050; ENSP00000301050; ENSG00000167535. [P54284-1]
ENST00000536187; ENSP00000444160; ENSG00000167535. [P54284-4]
ENST00000540990; ENSP00000445495; ENSG00000167535. [P54284-3]
ENST00000547230; ENSP00000448304; ENSG00000167535. [P54284-5]
GeneIDi784.
KEGGihsa:784.
UCSCiuc001rsk.2. human. [P54284-1]

Polymorphism databases

DMDMi1705683.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X76555 mRNA. Translation: CAA54055.1.
X76556 mRNA. Translation: CAA54056.1.
D43704 Genomic DNA. Translation: BAA07803.1.
U07139 mRNA. Translation: AAA95958.1.
L27584 mRNA. Translation: AAA19799.1.
AK289709 mRNA. Translation: BAF82398.1.
AK297639 mRNA. Translation: BAH12637.1.
AK304537 mRNA. Translation: BAH14209.1.
AK316323 mRNA. Translation: BAH14694.1.
AC117498 Genomic DNA. No translation available.
CH471111 Genomic DNA. Translation: EAW58008.1.
BC041811 mRNA. Translation: AAH41811.1.
CCDSiCCDS55821.1. [P54284-3]
CCDS55822.1. [P54284-4]
CCDS55823.1. [P54284-5]
CCDS8769.1. [P54284-1]
PIRiS39315.
S39316.
S41211.
RefSeqiNP_000716.2. NM_000725.3. [P54284-1]
NP_001193844.1. NM_001206915.1. [P54284-5]
NP_001193845.1. NM_001206916.1. [P54284-4]
NP_001193846.1. NM_001206917.1. [P54284-3]
UniGeneiHs.250712.
Hs.737291.

3D structure databases

ProteinModelPortaliP54284.
SMRiP54284. Positions 1-362.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107238. 3 interactions.
DIPiDIP-39138N.
IntActiP54284. 2 interactions.
STRINGi9606.ENSP00000301050.

Chemistry

ChEMBLiCHEMBL2363032.
DrugBankiDB04855. Dronedarone.
DB00393. Nimodipine.
DB00421. Spironolactone.
DB00661. Verapamil.

Protein family/group databases

TCDBi8.A.22.1.3. the ca(2+) channel auxiliary subunit types 1-4 (cca-) family.

PTM databases

PhosphoSiteiP54284.

Polymorphism databases

DMDMi1705683.

Proteomic databases

MaxQBiP54284.
PaxDbiP54284.
PRIDEiP54284.

Protocols and materials databases

DNASUi784.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000301050; ENSP00000301050; ENSG00000167535. [P54284-1]
ENST00000536187; ENSP00000444160; ENSG00000167535. [P54284-4]
ENST00000540990; ENSP00000445495; ENSG00000167535. [P54284-3]
ENST00000547230; ENSP00000448304; ENSG00000167535. [P54284-5]
GeneIDi784.
KEGGihsa:784.
UCSCiuc001rsk.2. human. [P54284-1]

Organism-specific databases

CTDi784.
GeneCardsiGC12P049212.
HGNCiHGNC:1403. CACNB3.
MIMi601958. gene.
neXtProtiNX_P54284.
PharmGKBiPA89.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG326500.
GeneTreeiENSGT00390000002740.
HOGENOMiHOG000230979.
HOVERGENiHBG050765.
InParanoidiP54284.
KOiK04864.
OMAiDIYWRAT.
PhylomeDBiP54284.
TreeFamiTF316195.

Enzyme and pathway databases

ReactomeiREACT_13606. Depolarization of the Presynaptic Terminal Triggers the Opening of Calcium Channels.
REACT_18312. NCAM1 interactions.
REACT_18325. Regulation of insulin secretion.
REACT_18339. Adrenaline,noradrenaline inhibits insulin secretion.

Miscellaneous databases

ChiTaRSiCACNB3. human.
GeneWikiiCACNB3.
GenomeRNAii784.
NextBioi3190.
PROiP54284.
SOURCEiSearch...

Gene expression databases

BgeeiP54284.
CleanExiHS_CACNB3.
ExpressionAtlasiP54284. baseline and differential.
GenevestigatoriP54284.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR008145. GK/Ca_channel_bsu.
IPR027417. P-loop_NTPase.
IPR001452. SH3_domain.
IPR008079. VDCC_L_b3su.
IPR000584. VDCC_L_bsu.
[Graphical view]
PANTHERiPTHR11824. PTHR11824. 1 hit.
PfamiPF00625. Guanylate_kin. 1 hit.
PF12052. VGCC_beta4Aa_N. 1 hit.
[Graphical view]
PRINTSiPR01626. LCACHANNELB.
PR01696. LCACHANNELB3.
SMARTiSM00072. GuKc. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 1 hit.
SSF52540. SSF52540. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Murakami M., Klugbauer N., Flockerzi V.
    Submitted (DEC-1993) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
  2. "The structures of the human calcium channel alpha 1 subunit (CACNL1A2) and beta subunit (CACNLB3) genes."
    Yamada Y., Masuda K., Li Q., Ihara Y., Kubota A., Miura T., Nakamura K., Fujii Y., Seino S., Seino Y.
    Genomics 27:312-319(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. Furneaux H.M.
    Submitted (FEB-1994) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Fetal brain.
  4. "Cloning, chromosomal location and functional expression of the human voltage-dependent calcium-channel beta 3 subunit."
    Collin T., Lory P., Taviaux S., Courtieu C., Guilbault P., Berta P., Nargeot J.
    Eur. J. Biochem. 220:257-262(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  5. "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] (ISOFORMS 1; 3 AND 4).
    Tissue: Brain, Small intestine and Uterus.
  6. "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].
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "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 1).
    Tissue: Brain.
  9. "Molecular cloning and characterization of the human voltage-gated calcium channel alpha(2)delta-4 subunit."
    Qin N., Yagel S., Momplaisir M.-L., Codd E.E., D'Andrea M.R.
    Mol. Pharmacol. 62:485-496(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CACNA2D4.
  10. "Identification of SH3 domain interaction partners of human FasL (CD178) by phage display screening."
    Voss M., Lettau M., Janssen O.
    BMC Immunol. 10:53-53(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FASLG.

Entry informationi

Entry nameiCACB3_HUMAN
AccessioniPrimary (citable) accession number: P54284
Secondary accession number(s): A8K0Z4
, B7Z4Q1, B7Z973, B7ZAK8, F5GZW7, F5H2P6, F8VSG3, Q13913
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: February 4, 2015
This is version 145 of the entry and version 1 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.