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Reviewed, UniProtKB/Swiss-Prot O15234 (CASC3_HUMAN)

Last modified June 16, 2009. Version 80. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Protein CASC3
Alternative name(s):
    Cancer susceptibility candidate gene 3 protein
    Metastatic lymph node protein 51
      Short name=Protein MLN 51
    Protein barentsz
      Short name=Btz
Gene names
Name: CASC3
Synonyms: MLN51
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length703 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Component of the dendritic ribonucleoprotein particles (RNPs) in hippocampal neurons. May play a role in mRNA transport.

Subunit structure

Interacts with STAU in an RNA-dependent manner By similarity. Forms homo-oligomers.

Subcellular location

Cytoplasmperinuclear region By similarity. Nucleus By similarity. Note: Predominantly found in the perinuclear region By similarity. Shuttles between the nucleus and the cytoplasm in a CRM1-dependent manner By similarity.

Tissue specificity

Widely expressed. Overexpressed in breast cancers and metastasis, as well as in gastric cancers. Ref.2

Domain

The coiled coil domain may be involved in oligomerization.

Post-translational modification

Phosphorylated. Ref.2 Ref.6 Ref.7

Ontologies

Keywords
   Biological processTransport
mRNA transport
   Cellular componentCytoplasm
Nucleus
   DomainCoiled coil
   PTMPhosphoprotein
   Technical term3D-structure
Gene Ontology (GO)
   Biological processmRNA transport

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentnucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

perinuclear region of cytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionidentical protein binding Ref.2

Inferred from direct assay. Source: MGI

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

EIF4A3P389192EBI-299118,EBI-299104
MAGOHP613261EBI-299118,EBI-299134

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 703703Protein CASC3
PRO_0000089324

Regions

Coiled coil95 – 13137 Potential
Motif204 – 2107Nuclear localization signal 1 Potential
Motif254 – 2629Nuclear localization signal 2 Potential
Motif462 – 4665Nuclear export signal
Compositional bias41 – 466Poly-Gly
Compositional bias392 – 3954Poly-Pro
Compositional bias425 – 4284Poly-Pro
Compositional bias643 – 6486Poly-Pro
Compositional bias692 – 6954Poly-Pro

Amino acid modifications

Modified residue1481Phosphoserine Ref.7
Modified residue3631Phosphoserine Ref.6
Modified residue3731Phosphoserine Ref.6
Modified residue4771Phosphoserine Ref.7

Secondary structure

....... 703
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O15234-1 [UniParc].

Last modified August 14, 2001. Version 2.
Checksum: 642A4C01C8DD3BE0

FASTA70376,278
        10         20         30         40         50         60 
MADRRRQRAS QDTEDEESGA SGSDSGGSPL RGGGSCSGSA GGGGSGSLPS QRGGRTGALH 

        70         80         90        100        110        120 
LRRVESGGAK SAEESECESE DGIEGDAVLS DYESAEDSEG EEGEYSEEEN SKVELKSEAN 

       130        140        150        160        170        180 
DAVNSSTKEE KGEEKPDTKS TVTGERQSGD GQESTEPVEN KVGKKGPKHL DDDEDRKNPA 

       190        200        210        220        230        240 
YIPRKGLFFE HDLRGQTQEE EVRPKGRQRK LWKDEGRWEH DKFREDEQAP KSRQELIALY 

       250        260        270        280        290        300 
GYDIRSAHNP DDIKPRRIRK PRYGSPPQRD PNWNGERLNK SHRHQGLGGT LPPRTFINRN 

       310        320        330        340        350        360 
AAGTGRMSAP RNYSRSGGFK EGRAGFRPVE AGGQHGGRSG ETVKHEISYR SRRLEQTSVR 

       370        380        390        400        410        420 
DPSPEADAPV LGSPEKEEAA SEPPAAAPDA APPPPDRPIE KKSYSRARRT RTKVGDAVKL 

       430        440        450        460        470        480 
AEEVPPPPEG LIPAPPVPET TPTPPTKTGT WEAPVDSSTS GLEQDVAQLN IAEQNWSPGQ 

       490        500        510        520        530        540 
PSFLQPRELR GMPNHIHMGA GPPPQFNRME EMGVQGGRAK RYSSQRQRPV PEPPAPPVHI 

       550        560        570        580        590        600 
SIMEGHYYDP LQFQGPIYTH GDSPAPLPPQ GMLVQPGMNL PHPGLHPHQT PAPLPNPGLY 

       610        620        630        640        650        660 
PPPVSMSPGQ PPPQQLLAPT YFSAPGVMNF GNPSYPYAPG ALPPPPPPHL YPNTQAPSQV 

       670        680        690        700 
YGGVTYYNPA QQQVQPKPSP PRRTPQPVTI KPPPPEVVSR GSS 

« Hide

References

« Hide 'large scale' references
[1]"Identification of four novel human genes amplified and overexpressed in breast carcinoma and localized to the q11-q21.3 region of chromosome 17."
Tomasetto C.L., Regnier C.H., Moog-Lutz C., Mattei M.-G., Chenard M.-P., Lidereau R., Basset P., Rio M.-C.
Genomics 28:367-376(1995) [PubMed: 7490069] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Mammary carcinoma.
[2]"Metastatic lymph node 51, a novel nucleo-cytoplasmic protein overexpressed in breast cancer."
Degot S.F., Regnier C.H., Wendling C., Chenard M.-P., Rio M.-C., Tomasetto C.L.
Oncogene 21:4422-4434(2002) [PubMed: 12080473] [Abstract]
Cited for: SEQUENCE REVISION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, PHOSPHORYLATION.
Tissue: Mammary carcinoma.
[3]"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. expand/collapse author list , 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: 14702039] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Testis.
[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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Duodenum and Skin.
[5]"Targets of gene amplification and overexpression at 17q in gastric cancer."
Varis A., Wolf M., Monni O., Vakkari M.-L., Kokkola A., Moskaluk C., Frierson H.F. Jr., Powell S.M., Knuutila S., Kallioniemi A., El-Rifai W.
Cancer Res. 62:2625-2629(2002) [PubMed: 11980659] [Abstract]
Cited for: OVEREXPRESSION IN GASTRIC CANCERS.
[6]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed: 17081983] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-363 AND SER-373, MASS SPECTROMETRY.
Tissue: Epithelium.
[7]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-148 AND SER-477, MASS SPECTROMETRY.
[8]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

X80199 mRNA. Translation: CAC27699.1.
AK292425 mRNA. Translation: BAF85114.1.
BC044656 mRNA. Translation: AAH44656.1.
BC050526 mRNA. Translation: AAH50526.1.
IPIIPI00289491.
RefSeqNP_031385.2.
UniGeneHs.705465

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
2HYIX-ray2.30D/J170-246[»]
2J0QX-ray3.20I/T137-286[»]
2J0SX-ray2.21T137-286[»]
2J0UX-ray3.00T137-250[»]
3EX7X-ray2.30D/I138-283[»]
ModBaseSearch...

Protein-protein interaction databases

IntActO15234. 4 interactions.

Protein family/group databases

TCDB3.A.18.1.1. nuclear mRNA exporter (mRNA-E) family.

PTM databases

PhosphoSiteO15234.

Proteomic databases

PRIDEO15234.

Genome annotation databases

EnsemblENSG00000108349. Homo sapiens. [Contig view]
GeneID22794.
KEGGhsa:22794.

Organism-specific databases

GeneCardsGC17P035550.
H-InvDBHIX0013791.
HGNCHGNC:17040. CASC3.
MIM606504. gene.
PharmGKBPA134948596.
GenAtlasSearch...

Phylogenomic databases

HOGENOMO15234.
HOVERGENO15234.
OMAO15234. KSHRHQG.

Gene expression databases

ArrayExpressO15234.
BgeeO15234.
CleanExHS_CASC3.
GermOnlineENSG00000108349. Homo sapiens.

Family and domain databases

InterProIPR018545. CASC3/Barentsz_eIF4AIII-bd.
[Graphical view]
PfamPF09405. Btz. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio43124.
PMAP-CutDBO15234.
SOURCESearch...

Entry information

Entry nameCASC3_HUMAN
AccessionPrimary (citable) accession number: O15234
Secondary accession number(s): A8K8R0
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: August 14, 2001
Last modified: June 16, 2009
This is version 80 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM

MIM cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents