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Protein

EF-hand domain-containing protein D2

Gene

EFHD2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

May regulate B-cell receptor (BCR)-induced immature and primary B-cell apoptosis. Plays a role as negative regulator of the canonical NF-kappa-B-activating branch. Controls spontaneous apoptosis through the regulation of BCL2L1 abundance.By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi105 – 116121PROSITE-ProRule annotationAdd
BLAST
Calcium bindingi141 – 152122PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

Complete GO annotation...

Keywords - Ligandi

Calcium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
EF-hand domain-containing protein D2
Alternative name(s):
Swiprosin-1
Gene namesi
Name:EFHD2
Synonyms:SWS1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:28670. EFHD2.

Subcellular locationi

  • Membrane raft By similarity

  • Note: In a mouse immature B-cell line WEHI-231.By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134942316.

Polymorphism and mutation databases

BioMutaiEFHD2.
DMDMi20140139.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources1 Publication
Chaini2 – 240239EF-hand domain-containing protein D2PRO_0000073645Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineCombined sources1 Publication
Modified residuei11 – 111PhosphoserineCombined sources
Modified residuei74 – 741PhosphoserineCombined sources
Modified residuei76 – 761PhosphoserineCombined sources
Modified residuei83 – 831PhosphotyrosineBy similarity
Modified residuei233 – 2331N6-acetyllysineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ96C19.
MaxQBiQ96C19.
PaxDbiQ96C19.
PRIDEiQ96C19.
TopDownProteomicsiQ96C19.

2D gel databases

REPRODUCTION-2DPAGEIPI00060181.
SWISS-2DPAGEQ96C19.

PTM databases

iPTMnetiQ96C19.
PhosphoSiteiQ96C19.
SwissPalmiQ96C19.

Expressioni

Tissue specificityi

Found in lymphocytes; preferentially expressed in CD8+ cells.2 Publications

Gene expression databases

BgeeiQ96C19.
CleanExiHS_EFHD2.
ExpressionAtlasiQ96C19. baseline and differential.
GenevisibleiQ96C19. HS.

Organism-specific databases

HPAiHPA048961.

Interactioni

Subunit structurei

Interacts with CASP9; with inactive form.1 Publication

Protein-protein interaction databases

BioGridi122597. 31 interactions.
IntActiQ96C19. 7 interactions.
MINTiMINT-2730606.
STRINGi9606.ENSP00000365147.

Structurei

3D structure databases

ProteinModelPortaliQ96C19.
SMRiQ96C19. Positions 91-195.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini92 – 12736EF-hand 1PROSITE-ProRule annotationAdd
BLAST
Domaini128 – 16336EF-hand 2PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 2 EF-hand domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG0041. Eukaryota.
ENOG4111JG9. LUCA.
GeneTreeiENSGT00390000012058.
HOGENOMiHOG000007978.
HOVERGENiHBG051446.
InParanoidiQ96C19.
OMAiKYDVGND.
OrthoDBiEOG7H1JNV.
PhylomeDBiQ96C19.
TreeFamiTF320736.

Family and domain databases

Gene3Di1.10.238.10. 1 hit.
InterProiIPR011992. EF-hand-dom_pair.
IPR002048. EF_hand_dom.
[Graphical view]
PfamiPF13499. EF-hand_7. 1 hit.
[Graphical view]
SMARTiSM00054. EFh. 2 hits.
[Graphical view]
SUPFAMiSSF47473. SSF47473. 1 hit.
PROSITEiPS50222. EF_HAND_2. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q96C19-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATDELATKL SRRLQMEGEG GGETPEQPGL NGAAAAAAGA PDEAAEALGS
60 70 80 90 100
ADCELSAKLL RRADLNQGIG EPQSPSRRVF NPYTEFKEFS RKQIKDMEKM
110 120 130 140 150
FKQYDAGRDG FIDLMELKLM MEKLGAPQTH LGLKNMIKEV DEDFDSKLSF
160 170 180 190 200
REFLLIFRKA AAGELQEDSG LCVLARLSEI DVSSEGVKGA KSFFEAKVQA
210 220 230 240
INVSSRFEEE IKAEQEERKK QAEEMKQRKA AFKELQSTFK
Length:240
Mass (Da):26,697
Last modified:December 1, 2001 - v1
Checksum:i9FE3FEC3007A8FC2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL031283 Genomic DNA. Translation: CAI21431.1.
CH471167 Genomic DNA. Translation: EAW51720.1.
BC007233 mRNA. Translation: AAH07233.1.
BC014923 mRNA. Translation: AAH14923.1.
BC023611 mRNA. Translation: AAH23611.1.
BC068473 mRNA. Translation: AAH68473.1.
CCDSiCCDS155.1.
RefSeqiNP_077305.2. NM_024329.5.
UniGeneiHs.465374.

Genome annotation databases

EnsembliENST00000375980; ENSP00000365147; ENSG00000142634.
GeneIDi79180.
KEGGihsa:79180.
UCSCiuc001awh.2. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL031283 Genomic DNA. Translation: CAI21431.1.
CH471167 Genomic DNA. Translation: EAW51720.1.
BC007233 mRNA. Translation: AAH07233.1.
BC014923 mRNA. Translation: AAH14923.1.
BC023611 mRNA. Translation: AAH23611.1.
BC068473 mRNA. Translation: AAH68473.1.
CCDSiCCDS155.1.
RefSeqiNP_077305.2. NM_024329.5.
UniGeneiHs.465374.

3D structure databases

ProteinModelPortaliQ96C19.
SMRiQ96C19. Positions 91-195.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi122597. 31 interactions.
IntActiQ96C19. 7 interactions.
MINTiMINT-2730606.
STRINGi9606.ENSP00000365147.

PTM databases

iPTMnetiQ96C19.
PhosphoSiteiQ96C19.
SwissPalmiQ96C19.

Polymorphism and mutation databases

BioMutaiEFHD2.
DMDMi20140139.

2D gel databases

REPRODUCTION-2DPAGEIPI00060181.
SWISS-2DPAGEQ96C19.

Proteomic databases

EPDiQ96C19.
MaxQBiQ96C19.
PaxDbiQ96C19.
PRIDEiQ96C19.
TopDownProteomicsiQ96C19.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000375980; ENSP00000365147; ENSG00000142634.
GeneIDi79180.
KEGGihsa:79180.
UCSCiuc001awh.2. human.

Organism-specific databases

CTDi79180.
GeneCardsiEFHD2.
HGNCiHGNC:28670. EFHD2.
HPAiHPA048961.
MIMi616450. gene.
neXtProtiNX_Q96C19.
PharmGKBiPA134942316.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0041. Eukaryota.
ENOG4111JG9. LUCA.
GeneTreeiENSGT00390000012058.
HOGENOMiHOG000007978.
HOVERGENiHBG051446.
InParanoidiQ96C19.
OMAiKYDVGND.
OrthoDBiEOG7H1JNV.
PhylomeDBiQ96C19.
TreeFamiTF320736.

Miscellaneous databases

ChiTaRSiEFHD2. human.
GenomeRNAii79180.
PROiQ96C19.
SOURCEiSearch...

Gene expression databases

BgeeiQ96C19.
CleanExiHS_EFHD2.
ExpressionAtlasiQ96C19. baseline and differential.
GenevisibleiQ96C19. HS.

Family and domain databases

Gene3Di1.10.238.10. 1 hit.
InterProiIPR011992. EF-hand-dom_pair.
IPR002048. EF_hand_dom.
[Graphical view]
PfamiPF13499. EF-hand_7. 1 hit.
[Graphical view]
SMARTiSM00054. EFh. 2 hits.
[Graphical view]
SUPFAMiSSF47473. SSF47473. 1 hit.
PROSITEiPS50222. EF_HAND_2. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "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].
    Tissue: Lung, Muscle, Testis and Uterus.
  4. Bienvenut W.V., Calvo F.
    Submitted (FEB-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-12; 62-78; 103-118; 124-134; 139-159; 177-188 AND 230-240, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Cervix carcinoma.
  5. Lubec G., Chen W.-Q., Sun Y.
    Submitted (DEC-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 63-77; 79-87; 160-176 AND 207-218, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Fetal brain cortex.
  6. "Identification of specific proteins in different lymphocyte populations by proteomic tools."
    Vuadens F., Gasparini D., Deon C., Sanchez J.-C., Hochstrasser D.F., Schneider P., Tissot J.-D.
    Proteomics 2:105-111(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION, TISSUE SPECIFICITY.
  7. Cited for: TISSUE SPECIFICITY, IDENTIFICATION BY MASS SPECTROMETRY.
  8. "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] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
    Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
    Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-74, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-74 AND SER-76, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. "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] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "Comparative proteomics analysis of caspase-9-protein complexes in untreated and cytochrome c/dATP stimulated lysates of NSCLC cells."
    Checinska A., Giaccone G., Rodriguez J.A., Kruyt F.A.E., Jimenez C.R.
    J. Proteomics 72:575-585(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CASP9, IDENTIFICATION BY MASS SPECTROMETRY.
  14. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-74, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  15. "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-233, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11; SER-74 AND SER-76, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. "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-74 AND SER-76, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  20. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiEFHD2_HUMAN
AccessioniPrimary (citable) accession number: Q96C19
Secondary accession number(s): Q5JYW9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 23, 2002
Last sequence update: December 1, 2001
Last modified: June 8, 2016
This is version 128 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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

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 one 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.