Full text data of EFHD2
EFHD2
(SWS1)
[Confidence: low (only semi-automatic identification from reviews)]
EF-hand domain-containing protein D2 (Swiprosin-1)
EF-hand domain-containing protein D2 (Swiprosin-1)
UniProt
Q96C19
ID EFHD2_HUMAN Reviewed; 240 AA.
AC Q96C19; Q5JYW9;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-DEC-2001, sequence version 1.
DT 22-JAN-2014, entry version 105.
DE RecName: Full=EF-hand domain-containing protein D2;
DE AltName: Full=Swiprosin-1;
GN Name=EFHD2; Synonyms=SWS1;
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 GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung, Muscle, Testis, and Uterus;
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 [4]
RP PROTEIN SEQUENCE OF 2-12; 62-78; 103-118; 124-134; 139-159; 177-188
RP AND 230-240, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2,
RP AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RA Bienvenut W.V., Calvo F.;
RL Submitted (FEB-2008) to UniProtKB.
RN [5]
RP PROTEIN SEQUENCE OF 63-77; 79-87; 160-176 AND 207-218, AND MASS
RP SPECTROMETRY.
RC TISSUE=Fetal brain cortex;
RA Lubec G., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [6]
RP IDENTIFICATION, AND TISSUE SPECIFICITY.
RX PubMed=11788997;
RX DOI=10.1002/1615-9861(200201)2:1<105::AID-PROT105>3.3.CO;2-6;
RA Vuadens F., Gasparini D., Deon C., Sanchez J.-C., Hochstrasser D.F.,
RA Schneider P., Tissot J.-D.;
RT "Identification of specific proteins in different lymphocyte
RT populations by proteomic tools.";
RL Proteomics 2:105-111(2002).
RN [7]
RP MASS SPECTROMETRY, AND TISSUE SPECIFICITY.
RX PubMed=15274114; DOI=10.1002/pmic.200300779;
RA Vuadens F., Rufer N., Kress A., Corthesy P., Schneider P.,
RA Tissot J.-D.;
RT "Identification of swiprosin 1 in human lymphocytes.";
RL Proteomics 4:2216-2220(2004).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-74, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein
RT phosphorylation analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-74 AND SER-76, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [13]
RP INTERACTION WITH CASP9, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=19118655; DOI=10.1016/j.jprot.2008.11.016;
RA Checinska A., Giaccone G., Rodriguez J.A., Kruyt F.A.E., Jimenez C.R.;
RT "Comparative proteomics analysis of caspase-9-protein complexes in
RT untreated and cytochrome c/dATP stimulated lysates of NSCLC cells.";
RL J. Proteomics 72:575-585(2009).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-74, AND MASS
RP SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-233, 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).
RN [16]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE
RP SCALE ANALYSIS] AT SER-11; SER-74 AND SER-76, AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [18]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: May regulate B-cell receptor (BCR)-induced immature and
CC primary B-cell apoptosis (By similarity). Plays a role as negative
CC regulator of the canonical NF-kappa-B-activating branch (By
CC similarity). Controls spontaneous apoptosis through the regulation
CC of BCL2L1 abundance (By similarity).
CC -!- SUBUNIT: Interacts with CASP9; with inactive form.
CC -!- SUBCELLULAR LOCATION: Membrane raft (By similarity). Note=In a
CC mouse immature B-cell line WEHI-231 (By similarity).
CC -!- TISSUE SPECIFICITY: Found in lymphocytes; preferentially expressed
CC in CD8+ cells.
CC -!- SIMILARITY: Contains 2 EF-hand domains.
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DR EMBL; AL031283; CAI21431.1; -; Genomic_DNA.
DR EMBL; CH471167; EAW51720.1; -; Genomic_DNA.
DR EMBL; BC007233; AAH07233.1; -; mRNA.
DR EMBL; BC014923; AAH14923.1; -; mRNA.
DR EMBL; BC023611; AAH23611.1; -; mRNA.
DR EMBL; BC068473; AAH68473.1; -; mRNA.
DR RefSeq; NP_077305.2; NM_024329.5.
DR UniGene; Hs.465374; -.
DR ProteinModelPortal; Q96C19; -.
DR SMR; Q96C19; 91-195.
DR IntAct; Q96C19; 1.
DR MINT; MINT-2730606; -.
DR STRING; 9606.ENSP00000365147; -.
DR PhosphoSite; Q96C19; -.
DR DMDM; 20140139; -.
DR REPRODUCTION-2DPAGE; IPI00060181; -.
DR SWISS-2DPAGE; Q96C19; -.
DR PaxDb; Q96C19; -.
DR PRIDE; Q96C19; -.
DR Ensembl; ENST00000375980; ENSP00000365147; ENSG00000142634.
DR GeneID; 79180; -.
DR KEGG; hsa:79180; -.
DR UCSC; uc001awh.2; human.
DR CTD; 79180; -.
DR GeneCards; GC01P015736; -.
DR HGNC; HGNC:28670; EFHD2.
DR HPA; HPA048961; -.
DR neXtProt; NX_Q96C19; -.
DR PharmGKB; PA134942316; -.
DR eggNOG; NOG259396; -.
DR HOGENOM; HOG000007978; -.
DR HOVERGEN; HBG051446; -.
DR InParanoid; Q96C19; -.
DR OMA; HILNRRQ; -.
DR OrthoDB; EOG7H1JNV; -.
DR PhylomeDB; Q96C19; -.
DR GenomeRNAi; 79180; -.
DR NextBio; 68166; -.
DR PRO; PR:Q96C19; -.
DR Bgee; Q96C19; -.
DR CleanEx; HS_EFHD2; -.
DR Genevestigator; Q96C19; -.
DR GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:Ensembl.
DR Gene3D; 1.10.238.10; -; 1.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR002048; EF_hand_dom.
DR Pfam; PF13499; EF-hand_7; 1.
DR SMART; SM00054; EFh; 2.
DR PROSITE; PS00018; EF_HAND_1; FALSE_NEG.
DR PROSITE; PS50222; EF_HAND_2; 2.
PE 1: Evidence at protein level;
KW Acetylation; Calcium; Complete proteome; Direct protein sequencing;
KW Membrane; Metal-binding; Phosphoprotein; Reference proteome; Repeat.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 240 EF-hand domain-containing protein D2.
FT /FTId=PRO_0000073645.
FT DOMAIN 92 127 EF-hand 1.
FT DOMAIN 128 163 EF-hand 2.
FT CA_BIND 105 116 1 (Potential).
FT CA_BIND 141 152 2 (Potential).
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 11 11 Phosphoserine.
FT MOD_RES 74 74 Phosphoserine.
FT MOD_RES 76 76 Phosphoserine.
FT MOD_RES 83 83 Phosphotyrosine (By similarity).
FT MOD_RES 233 233 N6-acetyllysine.
SQ SEQUENCE 240 AA; 26697 MW; 9FE3FEC3007A8FC2 CRC64;
MATDELATKL SRRLQMEGEG GGETPEQPGL NGAAAAAAGA PDEAAEALGS ADCELSAKLL
RRADLNQGIG EPQSPSRRVF NPYTEFKEFS RKQIKDMEKM FKQYDAGRDG FIDLMELKLM
MEKLGAPQTH LGLKNMIKEV DEDFDSKLSF REFLLIFRKA AAGELQEDSG LCVLARLSEI
DVSSEGVKGA KSFFEAKVQA INVSSRFEEE IKAEQEERKK QAEEMKQRKA AFKELQSTFK
//
ID EFHD2_HUMAN Reviewed; 240 AA.
AC Q96C19; Q5JYW9;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-DEC-2001, sequence version 1.
DT 22-JAN-2014, entry version 105.
DE RecName: Full=EF-hand domain-containing protein D2;
DE AltName: Full=Swiprosin-1;
GN Name=EFHD2; Synonyms=SWS1;
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 GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung, Muscle, Testis, and Uterus;
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 [4]
RP PROTEIN SEQUENCE OF 2-12; 62-78; 103-118; 124-134; 139-159; 177-188
RP AND 230-240, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2,
RP AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RA Bienvenut W.V., Calvo F.;
RL Submitted (FEB-2008) to UniProtKB.
RN [5]
RP PROTEIN SEQUENCE OF 63-77; 79-87; 160-176 AND 207-218, AND MASS
RP SPECTROMETRY.
RC TISSUE=Fetal brain cortex;
RA Lubec G., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [6]
RP IDENTIFICATION, AND TISSUE SPECIFICITY.
RX PubMed=11788997;
RX DOI=10.1002/1615-9861(200201)2:1<105::AID-PROT105>3.3.CO;2-6;
RA Vuadens F., Gasparini D., Deon C., Sanchez J.-C., Hochstrasser D.F.,
RA Schneider P., Tissot J.-D.;
RT "Identification of specific proteins in different lymphocyte
RT populations by proteomic tools.";
RL Proteomics 2:105-111(2002).
RN [7]
RP MASS SPECTROMETRY, AND TISSUE SPECIFICITY.
RX PubMed=15274114; DOI=10.1002/pmic.200300779;
RA Vuadens F., Rufer N., Kress A., Corthesy P., Schneider P.,
RA Tissot J.-D.;
RT "Identification of swiprosin 1 in human lymphocytes.";
RL Proteomics 4:2216-2220(2004).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-74, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein
RT phosphorylation analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-74 AND SER-76, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [13]
RP INTERACTION WITH CASP9, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=19118655; DOI=10.1016/j.jprot.2008.11.016;
RA Checinska A., Giaccone G., Rodriguez J.A., Kruyt F.A.E., Jimenez C.R.;
RT "Comparative proteomics analysis of caspase-9-protein complexes in
RT untreated and cytochrome c/dATP stimulated lysates of NSCLC cells.";
RL J. Proteomics 72:575-585(2009).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-74, AND MASS
RP SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-233, 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).
RN [16]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE
RP SCALE ANALYSIS] AT SER-11; SER-74 AND SER-76, AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [18]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: May regulate B-cell receptor (BCR)-induced immature and
CC primary B-cell apoptosis (By similarity). Plays a role as negative
CC regulator of the canonical NF-kappa-B-activating branch (By
CC similarity). Controls spontaneous apoptosis through the regulation
CC of BCL2L1 abundance (By similarity).
CC -!- SUBUNIT: Interacts with CASP9; with inactive form.
CC -!- SUBCELLULAR LOCATION: Membrane raft (By similarity). Note=In a
CC mouse immature B-cell line WEHI-231 (By similarity).
CC -!- TISSUE SPECIFICITY: Found in lymphocytes; preferentially expressed
CC in CD8+ cells.
CC -!- SIMILARITY: Contains 2 EF-hand domains.
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DR EMBL; AL031283; CAI21431.1; -; Genomic_DNA.
DR EMBL; CH471167; EAW51720.1; -; Genomic_DNA.
DR EMBL; BC007233; AAH07233.1; -; mRNA.
DR EMBL; BC014923; AAH14923.1; -; mRNA.
DR EMBL; BC023611; AAH23611.1; -; mRNA.
DR EMBL; BC068473; AAH68473.1; -; mRNA.
DR RefSeq; NP_077305.2; NM_024329.5.
DR UniGene; Hs.465374; -.
DR ProteinModelPortal; Q96C19; -.
DR SMR; Q96C19; 91-195.
DR IntAct; Q96C19; 1.
DR MINT; MINT-2730606; -.
DR STRING; 9606.ENSP00000365147; -.
DR PhosphoSite; Q96C19; -.
DR DMDM; 20140139; -.
DR REPRODUCTION-2DPAGE; IPI00060181; -.
DR SWISS-2DPAGE; Q96C19; -.
DR PaxDb; Q96C19; -.
DR PRIDE; Q96C19; -.
DR Ensembl; ENST00000375980; ENSP00000365147; ENSG00000142634.
DR GeneID; 79180; -.
DR KEGG; hsa:79180; -.
DR UCSC; uc001awh.2; human.
DR CTD; 79180; -.
DR GeneCards; GC01P015736; -.
DR HGNC; HGNC:28670; EFHD2.
DR HPA; HPA048961; -.
DR neXtProt; NX_Q96C19; -.
DR PharmGKB; PA134942316; -.
DR eggNOG; NOG259396; -.
DR HOGENOM; HOG000007978; -.
DR HOVERGEN; HBG051446; -.
DR InParanoid; Q96C19; -.
DR OMA; HILNRRQ; -.
DR OrthoDB; EOG7H1JNV; -.
DR PhylomeDB; Q96C19; -.
DR GenomeRNAi; 79180; -.
DR NextBio; 68166; -.
DR PRO; PR:Q96C19; -.
DR Bgee; Q96C19; -.
DR CleanEx; HS_EFHD2; -.
DR Genevestigator; Q96C19; -.
DR GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:Ensembl.
DR Gene3D; 1.10.238.10; -; 1.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR002048; EF_hand_dom.
DR Pfam; PF13499; EF-hand_7; 1.
DR SMART; SM00054; EFh; 2.
DR PROSITE; PS00018; EF_HAND_1; FALSE_NEG.
DR PROSITE; PS50222; EF_HAND_2; 2.
PE 1: Evidence at protein level;
KW Acetylation; Calcium; Complete proteome; Direct protein sequencing;
KW Membrane; Metal-binding; Phosphoprotein; Reference proteome; Repeat.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 240 EF-hand domain-containing protein D2.
FT /FTId=PRO_0000073645.
FT DOMAIN 92 127 EF-hand 1.
FT DOMAIN 128 163 EF-hand 2.
FT CA_BIND 105 116 1 (Potential).
FT CA_BIND 141 152 2 (Potential).
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 11 11 Phosphoserine.
FT MOD_RES 74 74 Phosphoserine.
FT MOD_RES 76 76 Phosphoserine.
FT MOD_RES 83 83 Phosphotyrosine (By similarity).
FT MOD_RES 233 233 N6-acetyllysine.
SQ SEQUENCE 240 AA; 26697 MW; 9FE3FEC3007A8FC2 CRC64;
MATDELATKL SRRLQMEGEG GGETPEQPGL NGAAAAAAGA PDEAAEALGS ADCELSAKLL
RRADLNQGIG EPQSPSRRVF NPYTEFKEFS RKQIKDMEKM FKQYDAGRDG FIDLMELKLM
MEKLGAPQTH LGLKNMIKEV DEDFDSKLSF REFLLIFRKA AAGELQEDSG LCVLARLSEI
DVSSEGVKGA KSFFEAKVQA INVSSRFEEE IKAEQEERKK QAEEMKQRKA AFKELQSTFK
//