RBCC

Full text data of ENDOD1

ENDOD1 (KIAA0830) [Confidence: high (present in two of the MS resources)]
Endonuclease domain-containing 1 protein; 3.1.30.-; Flags: Precursor

hRBCD IPI00001952
IPI00001952 KIAA0830 protein KIAA0830 protein membrane 1 2 2 n/a 2 1 n/a 1 4 n/a 9 6 3 5 2 4 6 2 4 3 integral membrane protein n/a found at its expected molecular weight found at molecular weight

UniProt O94919
ID ENDD1_HUMAN Reviewed; 500 AA.
AC O94919; Q6GQY5; Q8TAQ8;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 19-JUL-2004, sequence version 2.
DT 22-JAN-2014, entry version 95.
DE RecName: Full=Endonuclease domain-containing 1 protein;
DE EC=3.1.30.-;
DE Flags: Precursor;
GN Name=ENDOD1; Synonyms=KIAA0830;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=10048485; DOI=10.1093/dnares/5.6.355;
RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M.,
RA Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XII.
RT The complete sequences of 100 new cDNA clones from brain which code
RT for large proteins in vitro.";
RL DNA Res. 5:355-364(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Platelet;
RX PubMed=11921445;
RX DOI=10.1002/1615-9861(200203)2:3<288::AID-PROT288>3.0.CO;2-0;
RA O'Neill E.E., Brock C.J., von Kriegsheim A.F., Pearce A.C., Dwek R.A.,
RA Watson S.P., Hebestreit H.F.;
RT "Towards complete analysis of the platelet proteome.";
RL Proteomics 2:288-305(2002).
RN [4]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-407, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
CC -!- FUNCTION: May act as a DNase and a RNase (Potential).
CC -!- SUBCELLULAR LOCATION: Secreted (Potential).
CC -!- SIMILARITY: Belongs to the DNA/RNA non-specific endonuclease
CC family.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA74853.1; Type=Erroneous initiation;
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AB020637; BAA74853.1; ALT_INIT; mRNA.
DR EMBL; BC026191; AAH26191.1; -; mRNA.
DR EMBL; BC071171; AAH71171.1; -; mRNA.
DR RefSeq; NP_055851.1; NM_015036.2.
DR UniGene; Hs.167115; -.
DR ProteinModelPortal; O94919; -.
DR IntAct; O94919; 1.
DR MINT; MINT-5003939; -.
DR PhosphoSite; O94919; -.
DR OGP; O94919; -.
DR PaxDb; O94919; -.
DR PeptideAtlas; O94919; -.
DR PRIDE; O94919; -.
DR Ensembl; ENST00000278505; ENSP00000278505; ENSG00000149218.
DR Ensembl; ENST00000577165; ENSP00000461026; ENSG00000262523.
DR GeneID; 23052; -.
DR KEGG; hsa:23052; -.
DR UCSC; uc001pfh.3; human.
DR CTD; 23052; -.
DR GeneCards; GC11P094823; -.
DR HGNC; HGNC:29129; ENDOD1.
DR HPA; HPA008932; -.
DR HPA; HPA010517; -.
DR neXtProt; NX_O94919; -.
DR PharmGKB; PA143485454; -.
DR eggNOG; NOG128256; -.
DR HOGENOM; HOG000112371; -.
DR HOVERGEN; HBG081477; -.
DR InParanoid; O94919; -.
DR KO; K15049; -.
DR OMA; SIPWKVL; -.
DR OrthoDB; EOG7V766K; -.
DR GenomeRNAi; 23052; -.
DR NextBio; 44099; -.
DR PRO; PR:O94919; -.
DR Bgee; O94919; -.
DR CleanEx; HS_ENDOD1; -.
DR Genevestigator; O94919; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0090305; P:nucleic acid phosphodiester bond hydrolysis; IEA:GOC.
DR Gene3D; 3.40.570.10; -; 1.
DR InterPro; IPR001604; DNA/RNA_non-sp_Endonuclease.
DR InterPro; IPR020821; Extracellular_endonuc_su_A.
DR Pfam; PF01223; Endonuclease_NS; 1.
DR SMART; SM00892; Endonuclease_NS; 1.
DR SMART; SM00477; NUC; 1.
PE 1: Evidence at protein level;
KW Acetylation; Complete proteome; Endonuclease; Hydrolase; Nuclease;
KW Polymorphism; Reference proteome; Secreted; Signal.
FT SIGNAL 1 21 Potential.
FT CHAIN 22 500 Endonuclease domain-containing 1 protein.
FT /FTId=PRO_0000019924.
FT MOD_RES 407 407 N6-acetyllysine.
FT VARIANT 350 350 V -> M (in dbSNP:rs3740862).
FT /FTId=VAR_022044.
FT VARIANT 446 446 G -> V (in dbSNP:rs3740861).
FT /FTId=VAR_022045.
SQ SEQUENCE 500 AA; 55017 MW; 5B62754FE2E9AD9C CRC64;
MGTARWLALG SLFALAGLLE GRLVGEEEAG FGECDKFFYA GTPPAGLAAD SHVKICQRAE
GAERFATLYS TRDRIPVYSA FRAPRPAPGG AEQRWLVEPQ IDDPNSNLEE AINEAEAITS
VNSLGSKQAL NTDYLDSDYQ RGQLYPFSLS SDVQVATFTL TNSAPMTQSF QERWYVNLHS
LMDRALTPQC GSGEDLYILT GTVPSDYRVK DKVAVPEFVW LAACCAVPGG GWAMGFVKHT
RDSDIIEDVM VKDLQKLLPF NPQLFQNNCG ETEQDTEKMK KILEVVNQIQ DEERMVQSQK
SSSPLSSTRS KRSTLLPPEA SEGSSSFLGK LMGFIATPFI KLFQLIYYLV VAILKNIVYF
LWCVTKQVIN GIESCLYRLG SATISYFMAI GEELVSIPWK VLKVVAKVIR ALLRILCCLL
KAICRVLSIP VRVLVDVATF PVYTMGAIPI VCKDIALGLG GTVSLLFDTA FGTLGGLFQV
VFSVCKRIGY KVTFDNSGEL
//

RBCC Red Blood Cell Collection

Full text data of ENDOD1