O15234 (CASC3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Protein CASC3

Alternative name(s):
Cancer susceptibility candidate gene 3 protein
Metastatic lymph node gene 51 protein
Short name=MLN 51
Protein barentsz
Short name=Btz

Gene names

Name:	CASC3
Synonyms:	MLN51

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	703 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Component of a splicing-dependent multiprotein exon junction complex (EJC) deposited at splice junction on mRNAs. The EJC is a dynamic structure consisting of a few core proteins and several more peripheral nuclear and cytoplasmic associated factors that join the complex only transiently either during EJC assembly or during subsequent mRNA metabolism. Core components of the EJC, that remains bound to spliced mRNAs throughout all stages of mRNA metabolism, functions to mark the position of the exon-exon junction in the mature mRNA and thereby influences downstream processes of gene expression including mRNA splicing, nuclear mRNA export, subcellular mRNA localization, translation efficiency and nonsense-mediated mRNA decay (NMD). Stimulates the ATPase and RNA-helicase activities of EIF4A3. Plays a role in the stress response by participating in cytoplasmic stress granules assembly and by favouring cell recovery following stress. Component of the dendritic ribonucleoprotein particles (RNPs) in hippocampal neurons By similarity. May play a role in mRNA transport By similarity. Binds spliced mRNA in sequence-independent manner, 20-24 nucleotides upstream of mRNA exon-exon junctions. Binds poly(G) and poly(U) RNA homopolymer. Ref.11 Ref.12
Subunit structure	Forms homooligomers By similarity. Interacts with STAU in an RNA-dependent manner By similarity. Part of the EJC core complex that contains CASC3, EIF4A3, MAGOH and RBM8A. Found in a mRNA splicing-dependent exon junction complex (EJC), at least composed of ACIN1, CASC3, EIF4A3, MAGOH, PNN, RBM8A, RNPS1, SAP18 and THOC4. Interacts with EIF4A3, MAGOH, NXF1 and RBM8A. Ref.7 Ref.8
Subcellular location	Cytoplasm › perinuclear region. Nucleus. Nucleus speckle. Note: Predominantly found in the perinuclear region By similarity. Shuttles between the nucleus and the cytoplasm in a CRM1-dependent manner. Travels to the cytoplasm as part of the exon junction complex (EJC) bound to mRNA. Shuttles between the cytoplasm and the stress granules. More specifically found in nuclear intrachromatin granules clusters (IGC), also called nuclear speckles, which are storage compartments for nuclear proteins involved in mRNA processing. Colocalizes in nuclear speckles with MAGOH. Under stress condition, colocalizes with FMR1 and TIA1, but not MAGOH and RBM8A EJC core factors, in cytoplasmic stress granules, which contain stored mRNAs whose translation is stopped in response to stress. Ref.2 Ref.7 Ref.8 Ref.11
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	ADP-ribosylated by tankyrase TNKS and TNKS2. Poly-ADP-ribosylated protein is recognized by RNF146, followed by ubiquitination. Ubiquitinated by RNF146 when poly-ADP-ribosylated, leading to its degradation. Ref.17
Sequence similarities	Belongs to the CASC3 family.

Ontologies

Keywords
Biological process	Nonsense-mediated mRNA decay Stress response Translation regulation Transport mRNA processing mRNA splicing mRNA transport
Cellular component	Cytoplasm Nucleus
Domain	Coiled coil
Ligand	RNA-binding
PTM	ADP-ribosylation Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	RNA splicing Inferred from electronic annotation. Source: UniProtKB-KW mRNA processing Inferred from electronic annotation. Source: UniProtKB-KW mRNA transport Inferred from electronic annotation. Source: UniProtKB-KW nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Inferred from electronic annotation. Source: UniProtKB-KW regulation of translation Inferred from electronic annotation. Source: UniProtKB-KW response to stress Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytosol Traceable author statement. Source: Reactome exon-exon junction complex Inferred from direct assay. Source: UniProtKB nuclear speck Inferred from electronic annotation. Source: UniProtKB-SubCell perinuclear region of cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	RNA binding Inferred from electronic annotation. Source: UniProtKB-KW identical protein binding Inferred from direct assay Ref.2. Source: MGI ubiquitin protein ligase binding Inferred from physical interaction Ref.17. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
EIF4A3	P38919	6	EBI-299118,EBI-299104
MAGOH	P61326	4	EBI-299118,EBI-299134

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 703

703

Protein CASC3

PRO_0000089324

Regions

Region

137 – 283

147

Necessary for RNA-binding, interaction with MAGOH and localization in nucleus speckles

Region

137 – 283

147

Sufficient to form the EJC

Region

377 – 703

327

Necessary for localization in cytoplasmic stress granules

Coiled coil

95 – 131

37

Potential

Motif

204 – 210

7

Nuclear localization signal 1 Potential

Motif

254 – 262

9

Nuclear localization signal 2 Potential

Motif

462 – 466

5

Nuclear export signal

Compositional bias

41 – 46

6

Poly-Gly

Compositional bias

392 – 395

4

Poly-Pro

Compositional bias

425 – 428

4

Poly-Pro

Compositional bias

643 – 648

6

Poly-Pro

Compositional bias

692 – 695

4

Poly-Pro

Amino acid modifications

Modified residue

37

1

Phosphoserine Ref.14

Modified residue

45

1

Phosphoserine Ref.14

Modified residue

148

1

Phosphoserine Ref.13 Ref.14 Ref.15

Modified residue

363

1

Phosphoserine Ref.10

Modified residue

373

1

Phosphoserine Ref.10

Modified residue

477

1

Phosphoserine Ref.13

Experimental info

Mutagenesis

181

1

Y → A: Does not affect EJC formation. Ref.8

Mutagenesis

184 – 185

2

RK → AA: Does not affect EJC formation.

Mutagenesis

188

1

F → A: Does not affect EJC formation. Ref.8

Mutagenesis

218

1

W → A: Abolishes interaction with EIF4A3, EJC formation and localization in nucleus speckles. Ref.8

Mutagenesis

220 – 221

2

HD → AA: Abolishes interaction with EIF4A3, EJC formation and localization in nucleus speckles.

Mutagenesis

240 – 241

2

YG → AA: Abolishes interaction with EIF4A3, EJC formation and localization in nucleus speckles.

Secondary structure

1

.

.

.

.

.

.

.

703

Helix Strand Turn

Details...

Helix

172 – 174

3

Helix

226 – 228

3

Helix

233 – 240

8

Sequences

	Sequence		Length	Mass (Da)
	O15234 [UniParc]. Last modified August 14, 2001. Version 2. Checksum: 642A4C01C8DD3BE0	FASTA	703	76,278
	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

References

	« Hide 'large scale' referencesShow '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. , 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]	"DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage." Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L. , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C. Nature 440:1045-1049(2006) [PubMed: 16625196] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"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.
[6]	"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.
[7]	"Association of the breast cancer protein MLN51 with the exon junction complex via its speckle localizer and RNA binding module." Degot S., Le Hir H., Alpy F., Kedinger V., Stoll I., Wendling C., Seraphin B., Rio M.-C., Tomasetto C. J. Biol. Chem. 279:33702-33715(2004) [PubMed: 15166247] [Abstract] Cited for: INTERACTION WITH MAGOH; NXF1 AND RBM8A, RNA-BINDING, SUBCELLULAR LOCATION.
[8]	"The exon junction core complex is locked onto RNA by inhibition of eIF4AIII ATPase activity." Ballut L., Marchadier B., Baguet A., Tomasetto C., Seraphin B., Le Hir H. Nat. Struct. Mol. Biol. 12:861-869(2005) [PubMed: 16170325] [Abstract] Cited for: IDENTIFICATION IN THE CORE EXON JUNCTION COMPLEX, INTERACTION WITH EIF4A3, MUTAGENESIS OF TYR-181; 184-ARG-LYS-185; PHE-188; TRP-218; 220-HIS-ASP-221 AND 240-TYR-GLY-241, SUBCELLULAR LOCATION, RNA-BINDING.
[9]	"Biochemical analysis of the EJC reveals two new factors and a stable tetrameric protein core." Tange T.O., Shibuya T., Jurica M.S., Moore M.J. RNA 11:1869-1883(2005) [PubMed: 16314458] [Abstract] Cited for: IDENTIFICATION IN THE CORE EXON JUNCTION COMPLEX, IDENTIFICATION IN A MRNA SPLICING-DEPENDENT EXON JUNCTION COMPLEX, MASS SPECTROMETRY.
[10]	"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: Cervix carcinoma.
[11]	"The exon-junction-complex-component metastatic lymph node 51 functions in stress-granule assembly." Baguet A., Degot S., Cougot N., Bertrand E., Chenard M.P., Wendling C., Kessler P., Le Hir H., Rio M.C., Tomasetto C. J. Cell Sci. 120:2774-2784(2007) [PubMed: 17652158] [Abstract] Cited for: FUNCTION IN STRESS RESPONSE, SUBCELLULAR LOCATION.
[12]	"MLN51 stimulates the RNA-helicase activity of eIF4AIII." Noble C.G., Song H. PLoS ONE 2:E303-E303(2007) [PubMed: 17375189] [Abstract] Cited for: FUNCTION IN EIF4A3 ATPASE AND RNA-HELICASE ACTIVITY.
[13]	"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. Tissue: Cervix carcinoma.
[14]	"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach." Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S. Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37; SER-45 AND SER-148, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[15]	"Large-scale proteomics analysis of the human kinome." Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H. Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed: 19369195] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-148, MASS SPECTROMETRY.
[16]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[17]	"RNF146 is a poly(ADP-ribose)-directed E3 ligase that regulates axin degradation and Wnt signalling." Zhang Y., Liu S., Mickanin C., Feng Y., Charlat O., Michaud G.A., Schirle M., Shi X., Hild M., Bauer A., Myer V.E., Finan P.M., Porter J.A., Huang S.M., Cong F. Nat. Cell Biol. 13:623-629(2011) [PubMed: 21478859] [Abstract] Cited for: ADP-RIBOSYLATION, UBIQUITINATION.
[18]	"The crystal structure of the exon junction complex reveals how it maintains a stable grip on mRNA." Bono F., Ebert J., Lorentzen E., Conti E. Cell 126:713-725(2006) [PubMed: 16923391] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.21 ANGSTROMS) OF 137-286 IN THE EJC COMPLEX WITH EIF4A3; MAGOH; RBM8A AND AMP-PNP.
[19]	"Structure of the exon junction core complex with a trapped DEAD-box ATPase bound to RNA." Andersen C.B., Ballut L., Johansen J.S., Chamieh H., Nielsen K.H., Oliveira C.L., Pedersen J.S., Seraphin B., Le Hir H., Andersen G.R. Science 313:1968-1972(2006) [PubMed: 16931718] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 170-246 IN THE EJC COMPLEX WITH EIF4A3; MAGOH; RBM8A AND ADP-NP.
[20]	"Mechanism of ATP turnover inhibition in the EJC." Nielsen K.H., Chamieh H., Andersen C.B., Fredslund F., Hamborg K., Le Hir H., Andersen G.R. RNA 15:67-75(2009) [PubMed: 19033377] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 138-283 IN THE EJC COMPLEX WITH EIF4A3; MAGOH; RBM8A AND TRANSITION STATE ANALOG ADP-ALF3.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X80199 mRNA. Translation: CAC27699.1.
AK292425 mRNA. Translation: BAF85114.1.
AC068669 Genomic DNA. No translation available.
BC044656 mRNA. Translation: AAH44656.1.
BC050526 mRNA. Translation: AAH50526.1.

IPI

IPI00289491.

RefSeq

NP_031385.2. NM_007359.4.

UniGene

Hs.592129.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2HYI	X-ray	2.30	D/J	170-246	[»]
2J0Q	X-ray	3.20	I/T	137-286	[»]
2J0S	X-ray	2.21	T	137-286	[»]
2J0U	X-ray	3.00	T	137-250	[»]
2XB2	X-ray	3.40	S/T	137-286	[»]
3EX7	X-ray	2.30	D/I	138-283	[»]

ProteinModelPortal

O15234.

SMR

O15234. Positions 168-248.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-33288N.

IntAct

O15234. 7 interactions.

STRING

O15234.

Protein family/group databases

TCDB

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

PTM databases

PhosphoSite

O15234.

Proteomic databases

PRIDE

O15234.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000264645; ENSP00000264645; ENSG00000108349.
ENST00000394114; ENSP00000377673; ENSG00000108349.

GeneID

22794.

KEGG

hsa:22794.

UCSC

uc002hue.1. human.

Organism-specific databases

CTD

22794.

GeneCards

GC17P038296.

H-InvDB

HIX0202457.

HGNC

HGNC:17040. CASC3.

HPA

HPA024592.

MIM

606504. gene.

neXtProt

NX_O15234.

PharmGKB

PA134948596.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG08646.

GeneTree

ENSGT00390000006930.

HOGENOM

HBG715340.

HOVERGEN

HBG050799.

InParanoid

O15234.

OMA

RSGGFKE.

OrthoDB

EOG4P5K9B.

PhylomeDB

O15234.

Enzyme and pathway databases

Reactome

REACT_111217. Metabolism.

Gene expression databases

ArrayExpress

O15234.

Bgee

O15234.

CleanEx

HS_CASC3.

Genevestigator

O15234.

GermOnline

ENSG00000108349. Homo sapiens.

Family and domain databases

InterPro

IPR018545. Btz_dom.
[Graphical view]

KO

K14323.

Pfam

PF09405. Btz. 1 hit.
[Graphical view]

SMART

SM01044. Btz. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

43124.

PMAP-CutDB

O15234.

SOURCE

Search...

Entry information

Entry name

CASC3_HUMAN

Accession

Primary (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:	January 25, 2012
This is version 111 of the entry and version 2 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.