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

Beta-catenin-like protein 1

Gene

CTNNBL1

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

Functioni

Component of the PRP19-CDC5L complex that forms an integral part of the spliceosome and is required for activating pre-mRNA splicing. Participates in AID/AICDA-mediated Ig class switching recombination (CSR). May induce apoptosis.

GO - Molecular functioni

  • enzyme binding Source: UniProtKB

GO - Biological processi

  • apoptotic process Source: UniProtKB-KW
  • gene expression Source: Reactome
  • mRNA splicing, via spliceosome Source: Reactome
  • positive regulation of apoptotic process Source: UniProtKB
  • RNA splicing Source: Reactome
  • somatic diversification of immunoglobulins Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Apoptosis, mRNA processing, mRNA splicing

Enzyme and pathway databases

ReactomeiREACT_467. mRNA Splicing - Major Pathway.

Names & Taxonomyi

Protein namesi
Recommended name:
Beta-catenin-like protein 1
Alternative name(s):
Nuclear-associated protein
Short name:
NAP
Testis development protein NYD-SP19
Gene namesi
Name:CTNNBL1
Synonyms:C20orf33
ORF Names:PP8304
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 20

Organism-specific databases

HGNCiHGNC:15879. CTNNBL1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB-SubCell
  • membrane Source: UniProtKB
  • nucleoplasm Source: HPA
  • nucleus Source: UniProtKB
  • Prp19 complex Source: UniProtKB
  • spliceosomal complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Spliceosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi16 – 3318Missing : Nuclear and cytoplasmic localization. 1 PublicationAdd
BLAST
Mutagenesisi521 – 56343Missing : No change in NLS binding nor folding. 1 PublicationAdd
BLAST

Organism-specific databases

PharmGKBiPA27015.

Polymorphism and mutation databases

DMDMi29840792.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 563563Beta-catenin-like protein 1PRO_0000079490Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine2 Publications
Modified residuei91 – 911N6-acetyllysine1 Publication
Modified residuei389 – 3891Phosphoserine1 Publication
Modified residuei545 – 5451Phosphoserine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ8WYA6.
PaxDbiQ8WYA6.
PRIDEiQ8WYA6.

PTM databases

PhosphoSiteiQ8WYA6.

Expressioni

Tissue specificityi

Widely expressed with highest levels in skeletal muscle, placenta, heart, spleen, testis and thyroid.1 Publication

Gene expression databases

BgeeiQ8WYA6.
ExpressionAtlasiQ8WYA6. baseline and differential.
GenevisibleiQ8WYA6. HS.

Organism-specific databases

HPAiHPA004742.
HPA027907.

Interactioni

Subunit structurei

Component of the PRP19-CDC5L splicing complex composed of a core complex comprising a homotetramer of PRPF19, CDC5L, PLRG1 and BCAS2, and at least three less stably associated proteins CTNNBL1, CWC15 and HSPA8. Interacts directly with CWC15 and CDC5L in the complex. Interacts with AICDA; the interaction is important for the antibody diversification activity of AICDA. Interacts with PRPF31 (via its NLS). Interacts (via its N-terminal NLS) with KPNA1 and KPNA2.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CATIPQ7Z7H33EBI-748128,EBI-10258233
CDC5LQ994592EBI-748128,EBI-374880
CDCA7LQ96GN53EBI-748128,EBI-5278764
CREBZFQ9NS373EBI-748128,EBI-632965
LDOC1O957513EBI-748128,EBI-740738
MED4Q9NPJ63EBI-748128,EBI-394607
MEOX2A4D1273EBI-748128,EBI-10172134
NGFRAP1Q009943EBI-748128,EBI-741753
PRDM4Q9UKN53EBI-748128,EBI-2803427
SNW1Q135732EBI-748128,EBI-632715

Protein-protein interaction databases

BioGridi121123. 49 interactions.
IntActiQ8WYA6. 26 interactions.
MINTiMINT-1444671.
STRINGi9606.ENSP00000355050.

Structurei

Secondary structure

1
563
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni54 – 563Combined sources
Helixi57 – 637Combined sources
Helixi81 – 10222Combined sources
Beta strandi105 – 1073Combined sources
Helixi111 – 12515Combined sources
Turni126 – 1294Combined sources
Helixi131 – 1344Combined sources
Helixi135 – 1395Combined sources
Helixi142 – 1498Combined sources
Helixi155 – 17016Combined sources
Helixi171 – 1733Combined sources
Beta strandi174 – 1763Combined sources
Helixi179 – 19012Combined sources
Helixi193 – 20311Combined sources
Helixi209 – 22820Combined sources
Helixi232 – 2398Combined sources
Helixi241 – 25010Combined sources
Helixi257 – 27014Combined sources
Helixi274 – 2829Combined sources
Helixi285 – 29410Combined sources
Beta strandi297 – 2993Combined sources
Helixi304 – 32219Combined sources
Helixi325 – 3328Combined sources
Helixi335 – 34410Combined sources
Helixi350 – 36112Combined sources
Helixi364 – 3663Combined sources
Helixi367 – 3759Combined sources
Helixi378 – 38710Combined sources
Helixi393 – 3964Combined sources
Helixi401 – 41717Combined sources
Helixi420 – 42910Combined sources
Helixi432 – 46938Combined sources
Helixi475 – 48713Combined sources
Helixi490 – 50415Combined sources
Helixi509 – 52012Combined sources
Turni521 – 5233Combined sources
Helixi526 – 53914Combined sources
Beta strandi542 – 5443Combined sources
Helixi546 – 55914Combined sources
Turni560 – 5623Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4CB8X-ray2.90A77-563[»]
4CB9X-ray3.00A1-563[»]
4CBAX-ray3.10A77-563[»]
4HM9X-ray3.10A1-563[»]
4HNMX-ray2.90A75-563[»]
4MFUX-ray2.74A77-563[»]
4MFVX-ray2.92A/B33-563[»]
ProteinModelPortaliQ8WYA6.
SMRiQ8WYA6. Positions 77-563.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati79 – 12951HEAT 1Add
BLAST
Repeati134 – 17643HEAT 2Add
BLAST
Repeati178 – 22851ARM 1Add
BLAST
Repeati229 – 27345ARM 2Add
BLAST
Repeati274 – 32350ARM 3Add
BLAST
Repeati325 – 36339ARM 4Add
BLAST
Repeati364 – 41754ARM 5Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili476 – 540651 PublicationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi16 – 3318Nuclear localization signalAdd
BLAST
Motifi130 – 14011Nuclear export signal (NES)CuratedAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi22 – 254Poly-Glu
Compositional biasi68 – 758Poly-Glu

Domaini

The surface residues of the concave side of the superhelical ARM repeat region contribute to, but are not essential for NLS binding.1 Publication

Sequence similaritiesi

Contains 5 ARM repeats.Curated
Contains 2 HEAT repeats.Curated

Keywords - Domaini

Coiled coil, Repeat

Phylogenomic databases

eggNOGiNOG283719.
GeneTreeiENSGT00390000006931.
HOVERGENiHBG051212.
InParanoidiQ8WYA6.
KOiK12864.
OrthoDBiEOG7353WH.
PhylomeDBiQ8WYA6.
TreeFamiTF314294.

Family and domain databases

Gene3Di1.25.10.10. 2 hits.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR013180. CTNNBL1_N.
[Graphical view]
PfamiPF08216. CTNNBL. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 2 hits.

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q8WYA6-1) [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
MDVGELLSYQ PNRGTKRPRD DEEEEQKMRR KQTGTRERGR YREEEMTVVE
60 70 80 90 100
EADDDKKRLL QIIDRDGEEE EEEEEPLDES SVKKMILTFE KRSYKNQELR
110 120 130 140 150
IKFPDNPEKF MESELDLNDI IQEMHVVATM PDLYHLLVEL NAVQSLLGLL
160 170 180 190 200
GHDNTDVSIA VVDLLQELTD IDTLHESEEG AEVLIDALVD GQVVALLVQN
210 220 230 240 250
LERLDESVKE EADGVHNTLA IVENMAEFRP EMCTEGAQQG LLQWLLKRLK
260 270 280 290 300
AKMPFDANKL YCSEVLAILL QDNDENRELL GELDGIDVLL QQLSVFKRHN
310 320 330 340 350
PSTAEEQEMM ENLFDSLCSC LMLSSNRERF LKGEGLQLMN LMLREKKISR
360 370 380 390 400
SSALKVLDHA MIGPEGTDNC HKFVDILGLR TIFPLFMKSP RKIKKVGTTE
410 420 430 440 450
KEHEEHVCSI LASLLRNLRG QQRTRLLNKF TENDSEKVDR LMELHFKYLG
460 470 480 490 500
AMQVADKKIE GEKHDMVRRG EIIDNDTEEE FYLRRLDAGL FVLQHICYIM
510 520 530 540 550
AEICNANVPQ IRQRVHQILN MRGSSIKIVR HIIKEYAENI GDGRSPEFRE
560
NEQKRILGLL ENF
Length:563
Mass (Da):65,173
Last modified:March 1, 2002 - v1
Checksum:i791BAFCEC5916B5A
GO
Isoform 2 (identifier: Q8WYA6-2) [UniParc]FASTAAdd to basket

Also known as: NYD-SP19

The sequence of this isoform differs from the canonical sequence as follows:
     1-187: Missing.
     188-188: L → M

Show »
Length:376
Mass (Da):43,392
Checksum:i54E26219D2AA8496
GO
Isoform 3 (identifier: Q8WYA6-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-252: Missing.

Note: Gene prediction based on EST data.
Show »
Length:311
Mass (Da):36,103
Checksum:iBEF11FF9CAF56C86
GO
Isoform 4 (identifier: Q8WYA6-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-27: Missing.

Note: No experimental confirmation available.
Show »
Length:536
Mass (Da):61,971
Checksum:i6508EC207D3688FB
GO

Sequence cautioni

The sequence AAQ15267.1 differs from that shown. Reason: Frameshift at position 96. Curated
The sequence BAB14992.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti222 – 2221V → A in AAI21006 (PubMed:15489334).Curated
Sequence conflicti329 – 3291R → L in BAB14992 (PubMed:14702039).Curated
Sequence conflicti340 – 3401N → Y in BAC11121 (PubMed:14702039).Curated
Sequence conflicti439 – 4391D → N in BAB14992 (PubMed:14702039).Curated
Sequence conflicti439 – 4391D → N in BAD96312 (Ref. 7) Curated
Sequence conflicti445 – 4451H → Q in BAB14992 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti507 – 5071N → D.
Corresponds to variant rs4811236 [ dbSNP | Ensembl ].
VAR_059638

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 252252Missing in isoform 3. CuratedVSP_015182Add
BLAST
Alternative sequencei1 – 187187Missing in isoform 2. 1 PublicationVSP_004058Add
BLAST
Alternative sequencei1 – 2727Missing in isoform 4. 1 PublicationVSP_055261Add
BLAST
Alternative sequencei188 – 1881L → M in isoform 2. 1 PublicationVSP_004059

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF239607 mRNA. Translation: AAL69567.1.
AF367471 mRNA. Translation: AAK53407.1.
AF370431 mRNA. Translation: AAQ15267.1. Frameshift.
AK074663 mRNA. Translation: BAC11121.1.
AK293420 mRNA. Translation: BAG56927.1.
AK024761 mRNA. Translation: BAB14992.1. Different initiation.
AL118499, AL023804, AL109964 Genomic DNA. Translation: CAI19331.1.
AL118499, AL023804, AL109964 Genomic DNA. Translation: CAI19332.1.
AL109964, AL023804, AL118499 Genomic DNA. Translation: CAI42203.1.
AL109964, AL023804 Genomic DNA. Translation: CAI42204.1.
AL109964, AL023804, AL118499 Genomic DNA. Translation: CAI42208.1.
AL023804, AL109964, AL118499 Genomic DNA. Translation: CAI42984.1.
AL023804, AL109964 Genomic DNA. Translation: CAI42985.1.
AL023804, AL109964, AL118499 Genomic DNA. Translation: CAI42986.1.
BC022802 mRNA. Translation: AAH22802.1.
BC121005 mRNA. Translation: AAI21006.1.
BC121006 mRNA. Translation: AAI21007.1.
AK222592 mRNA. Translation: BAD96312.1.
CCDSiCCDS13298.1. [Q8WYA6-1]
CCDS63269.1. [Q8WYA6-4]
RefSeqiNP_001268424.1. NM_001281495.1. [Q8WYA6-4]
NP_110517.2. NM_030877.4. [Q8WYA6-1]
XP_011527219.1. XM_011528917.1.
UniGeneiHs.472667.

Genome annotation databases

EnsembliENST00000361383; ENSP00000355050; ENSG00000132792.
ENST00000373469; ENSP00000362568; ENSG00000132792. [Q8WYA6-3]
ENST00000373473; ENSP00000362572; ENSG00000132792. [Q8WYA6-2]
ENST00000405275; ENSP00000384355; ENSG00000132792. [Q8WYA6-4]
ENST00000628103; ENSP00000487198; ENSG00000132792. [Q8WYA6-4]
GeneIDi56259.
KEGGihsa:56259.
UCSCiuc002xhh.3. human. [Q8WYA6-2]
uc002xhj.3. human. [Q8WYA6-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF239607 mRNA. Translation: AAL69567.1.
AF367471 mRNA. Translation: AAK53407.1.
AF370431 mRNA. Translation: AAQ15267.1. Frameshift.
AK074663 mRNA. Translation: BAC11121.1.
AK293420 mRNA. Translation: BAG56927.1.
AK024761 mRNA. Translation: BAB14992.1. Different initiation.
AL118499, AL023804, AL109964 Genomic DNA. Translation: CAI19331.1.
AL118499, AL023804, AL109964 Genomic DNA. Translation: CAI19332.1.
AL109964, AL023804, AL118499 Genomic DNA. Translation: CAI42203.1.
AL109964, AL023804 Genomic DNA. Translation: CAI42204.1.
AL109964, AL023804, AL118499 Genomic DNA. Translation: CAI42208.1.
AL023804, AL109964, AL118499 Genomic DNA. Translation: CAI42984.1.
AL023804, AL109964 Genomic DNA. Translation: CAI42985.1.
AL023804, AL109964, AL118499 Genomic DNA. Translation: CAI42986.1.
BC022802 mRNA. Translation: AAH22802.1.
BC121005 mRNA. Translation: AAI21006.1.
BC121006 mRNA. Translation: AAI21007.1.
AK222592 mRNA. Translation: BAD96312.1.
CCDSiCCDS13298.1. [Q8WYA6-1]
CCDS63269.1. [Q8WYA6-4]
RefSeqiNP_001268424.1. NM_001281495.1. [Q8WYA6-4]
NP_110517.2. NM_030877.4. [Q8WYA6-1]
XP_011527219.1. XM_011528917.1.
UniGeneiHs.472667.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4CB8X-ray2.90A77-563[»]
4CB9X-ray3.00A1-563[»]
4CBAX-ray3.10A77-563[»]
4HM9X-ray3.10A1-563[»]
4HNMX-ray2.90A75-563[»]
4MFUX-ray2.74A77-563[»]
4MFVX-ray2.92A/B33-563[»]
ProteinModelPortaliQ8WYA6.
SMRiQ8WYA6. Positions 77-563.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi121123. 49 interactions.
IntActiQ8WYA6. 26 interactions.
MINTiMINT-1444671.
STRINGi9606.ENSP00000355050.

PTM databases

PhosphoSiteiQ8WYA6.

Polymorphism and mutation databases

DMDMi29840792.

Proteomic databases

MaxQBiQ8WYA6.
PaxDbiQ8WYA6.
PRIDEiQ8WYA6.

Protocols and materials databases

DNASUi56259.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000361383; ENSP00000355050; ENSG00000132792.
ENST00000373469; ENSP00000362568; ENSG00000132792. [Q8WYA6-3]
ENST00000373473; ENSP00000362572; ENSG00000132792. [Q8WYA6-2]
ENST00000405275; ENSP00000384355; ENSG00000132792. [Q8WYA6-4]
ENST00000628103; ENSP00000487198; ENSG00000132792. [Q8WYA6-4]
GeneIDi56259.
KEGGihsa:56259.
UCSCiuc002xhh.3. human. [Q8WYA6-2]
uc002xhj.3. human. [Q8WYA6-1]

Organism-specific databases

CTDi56259.
GeneCardsiGC20P036322.
HGNCiHGNC:15879. CTNNBL1.
HPAiHPA004742.
HPA027907.
MIMi611537. gene.
neXtProtiNX_Q8WYA6.
PharmGKBiPA27015.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG283719.
GeneTreeiENSGT00390000006931.
HOVERGENiHBG051212.
InParanoidiQ8WYA6.
KOiK12864.
OrthoDBiEOG7353WH.
PhylomeDBiQ8WYA6.
TreeFamiTF314294.

Enzyme and pathway databases

ReactomeiREACT_467. mRNA Splicing - Major Pathway.

Miscellaneous databases

ChiTaRSiCTNNBL1. human.
GeneWikiiCTNNBL1.
GenomeRNAii56259.
NextBioi35471085.
PROiQ8WYA6.
SOURCEiSearch...

Gene expression databases

BgeeiQ8WYA6.
ExpressionAtlasiQ8WYA6. baseline and differential.
GenevisibleiQ8WYA6. HS.

Family and domain databases

Gene3Di1.25.10.10. 2 hits.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR013180. CTNNBL1_N.
[Graphical view]
PfamiPF08216. CTNNBL. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 2 hits.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence, gene structure, and expression pattern of CTNNBL1, a minor-class intron-containing gene - evidence for a role in apoptosis."
    Jabbour L.S., Welter J.F., Kollar J., Hering T.M.
    Genomics 81:292-303(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, SUBCELLULAR LOCATION, POSSIBLE FUNCTION.
  2. "A new testis development gene NYD-SP19 from human testes."
    Sha J.H., Li J.M., Zhou Z.M.
    Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    Tissue: Testis.
  3. "Large-scale cDNA transfection screening for genes related to cancer development and progression."
    Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X., Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X.
    , Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.
    Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  4. "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 AND 4).
    Tissue: Aortic smooth muscle and Mammary gland.
  5. "The DNA sequence and comparative analysis of human chromosome 20."
    Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E.
    , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
    Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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: Skin.
  7. Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
    Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 327-563.
    Tissue: Coronary artery.
  8. "Interaction between antibody-diversification enzyme AID and spliceosome-associated factor CTNNBL1."
    Conticello S.G., Ganesh K., Xue K., Lu M., Rada C., Neuberger M.S.
    Mol. Cell 31:474-484(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH AICDA, SUBCELLULAR LOCATION, POSSIBLE FUNCTION, MUTAGENESIS OF 16-LYS--LYS-33.
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-389, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-91, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. Cited for: IDENTIFICATION AS A COMPONENT OF THE PRP19-CDC5L COMPLEX, SUBCELLULAR LOCATION, INTERACTION WITH CWC15 AND CDC5L.
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "CTNNBL1 is a novel nuclear localization sequence-binding protein that recognizes RNA-splicing factors CDC5L and Prp31."
    Ganesh K., Adam S., Taylor B., Simpson P., Rada C., Neuberger M.
    J. Biol. Chem. 286:17091-17102(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH AICDA; CDC5L; PRPF31; KPNA1 AND KPNA2, SUBCELLULAR LOCATION.
  14. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-545, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  17. "The structure of full-length human CTNNBL1 reveals a distinct member of the armadillo-repeat protein family."
    Huang X., Wang G., Wu Y., Du Z.
    Acta Crystallogr. D 69:1598-1608(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS), ARM REPEATS.
  18. "Structural and mutational analysis reveals that CTNNBL1 binds NLSs in a manner distinct from that of its closest armadillo-relative, karyopherin alpha."
    Ganesh K., van Maldegem F., Telerman S.B., Simpson P., Johnson C.M., Williams R.L., Neuberger M.S., Rada C.
    FEBS Lett. 588:21-27(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS), NUCLEAR EXPORT SIGNAL, HEAT REPEATS, MUTAGENESIS OF 521-MET--PHE-563, COILED-COIL.

Entry informationi

Entry nameiCTBL1_HUMAN
AccessioniPrimary (citable) accession number: Q8WYA6
Secondary accession number(s): B4DE16
, Q0VAL9, Q0VAM0, Q53HI8, Q5JWZ2, Q5JWZ3, Q5JWZ7, Q5JWZ8, Q8N454, Q8NCL2, Q8TBD6, Q96KD2, Q9H7A5, Q9NQF9, Q9NTX0, Q9Y3M7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 28, 2003
Last sequence update: March 1, 2002
Last modified: July 22, 2015
This is version 122 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 20
    Human chromosome 20: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. 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.