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Protein

Digestive organ expansion factor homolog

Gene

DIEXF

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

Functioni

Regulates the p53 pathway to control the expansion growth of digestive organs.By similarity

GO - Molecular functioni

  • poly(A) RNA binding Source: UniProtKB
  • rRNA binding Source: GO_Central
  • U3 snoRNA binding Source: GO_Central

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Names & Taxonomyi

Protein namesi
Recommended name:
Digestive organ expansion factor homolog
Gene namesi
Name:DIEXF
Synonyms:C1orf107, DEF
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:28440. DIEXF.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA142672491.

Polymorphism and mutation databases

BioMutaiDIEXF.
DMDMi117949399.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 756756Digestive organ expansion factor homologPRO_0000254149Add
BLAST

Proteomic databases

EPDiQ68CQ4.
MaxQBiQ68CQ4.
PaxDbiQ68CQ4.
PeptideAtlasiQ68CQ4.
PRIDEiQ68CQ4.

PTM databases

iPTMnetiQ68CQ4.
PhosphoSiteiQ68CQ4.

Expressioni

Gene expression databases

BgeeiQ68CQ4.
CleanExiHS_C1orf107.
ExpressionAtlasiQ68CQ4. baseline and differential.
GenevisibleiQ68CQ4. HS.

Organism-specific databases

HPAiHPA026640.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
CEP70Q8NHQ13EBI-747711,EBI-739624
MAGEA11P43364-23EBI-747711,EBI-10178634
MID2Q9UJV3-23EBI-747711,EBI-10172526
MIPOL1Q8TD103EBI-747711,EBI-2548751
RUFY1Q96T513EBI-747711,EBI-3941207

Protein-protein interaction databases

BioGridi117972. 19 interactions.
IntActiQ68CQ4. 6 interactions.
MINTiMINT-3002142.
STRINGi9606.ENSP00000419005.

Structurei

3D structure databases

ProteinModelPortaliQ68CQ4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi84 – 17693Glu-richAdd
BLAST
Compositional biasi341 – 3444Poly-Asp

Sequence similaritiesi

Belongs to the def family.Curated

Phylogenomic databases

eggNOGiKOG2340. Eukaryota.
ENOG410XP00. LUCA.
GeneTreeiENSGT00390000000709.
HOVERGENiHBG079696.
InParanoidiQ68CQ4.
KOiK14774.
OMAiEVCNMLR.
OrthoDBiEOG7W1535.
PhylomeDBiQ68CQ4.
TreeFamiTF105930.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR010678. Digest_organ_expansion_fac-prd.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR12933. PTHR12933. 1 hit.
PfamiPF06862. UTP25. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 2 hits.

Sequencei

Sequence statusi: Complete.

Q68CQ4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGKRGSRSQS QLLNTLTKKQ KKHLRDFGEE HPFYDRVSRK EAKPQICQLS
60 70 80 90 100
ESSDSSDSES DSESEPQQVS GYHRLLATLK NVSEEEEEDE EEEEEEDSIV
110 120 130 140 150
DDAEMNDEDG GSDVSVEEEM AAESTESPEN VALSADPEGK EDGEEPPGTS
160 170 180 190 200
QTSPEEFTDA KHESLFSLET NFLEEESGDN SSLKASQDPF LQHVNKELKE
210 220 230 240 250
KAIQAVATNP KTTHELKWPI LGQLFFSSKF QKLETFKPPK DIDLKSLHLQ
260 270 280 290 300
KPLESTWTKT NSQFLSGPQK SSSPFTPLQK ELFLIMNSYR DLFYPERTAL
310 320 330 340 350
KNGEEIRHVY CLHVINHILK ANAQVLGNNS RRRSQKFGVG DDDDFRDQGL
360 370 380 390 400
TRPKVLIVVP FREAALRVVQ LFISLLEGDS KKKIIVSNKK RFQGEYGSDP
410 420 430 440 450
EERPPNLKRP EDYEAVFVGN IDDHFRIGVA ILQRSIRLYA PFYSSDILIA
460 470 480 490 500
SPLGLRTIIG GEGEKKRDFD FLSSIELLII DQADIYLMQN WEHVLHLMNH
510 520 530 540 550
MNLLPLDSHG VDFSRVRMWS LNNWSKYYRQ TLLFGALQDA QINSVFNKYC
560 570 580 590 600
VNMQGQVAVR NVPMTGSISH VLVQLPHVFQ RMEAENLASV IDARFNFFVN
610 620 630 640 650
KILPQYRDAV MSHTLIYIPS YFDFVRLRNY FKKEELNFTH ICEYTQKSGV
660 670 680 690 700
SRARHFFLQG EKQFLLFTER FHFYKRYTIK GIRNLIFYEL PTYPHFYSEI
710 720 730 740 750
CNMLRATNRG EEATWTCTVL YSKYDAQRLA AVVGVERAAQ MLQSNKNVHL

FITGEK
Length:756
Mass (Da):87,055
Last modified:October 31, 2006 - v2
Checksum:iA8821B0AC4BF4067
GO

Sequence cautioni

The sequence CAI95693.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti111 – 1111G → D in CAH18684 (PubMed:17974005).Curated
Sequence conflicti111 – 1111G → D in CAH56170 (PubMed:17974005).Curated
Sequence conflicti258 – 2581T → A in CAH56170 (PubMed:17974005).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti67 – 671Q → E.1 Publication
Corresponds to variant rs585627 [ dbSNP | Ensembl ].
VAR_028827

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR749825 mRNA. Translation: CAH18684.1.
BX648514 mRNA. Translation: CAH56170.1.
AL022398 Genomic DNA. Translation: CAA18546.1.
AL022398 Genomic DNA. Translation: CAI95693.1. Sequence problems.
BC022964 mRNA. Translation: AAH22964.1.
CCDSiCCDS1493.1.
RefSeqiNP_055203.4. NM_014388.6.
UniGeneiHs.194754.

Genome annotation databases

EnsembliENST00000491415; ENSP00000419005; ENSG00000117597.
GeneIDi27042.
KEGGihsa:27042.
UCSCiuc001hhr.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR749825 mRNA. Translation: CAH18684.1.
BX648514 mRNA. Translation: CAH56170.1.
AL022398 Genomic DNA. Translation: CAA18546.1.
AL022398 Genomic DNA. Translation: CAI95693.1. Sequence problems.
BC022964 mRNA. Translation: AAH22964.1.
CCDSiCCDS1493.1.
RefSeqiNP_055203.4. NM_014388.6.
UniGeneiHs.194754.

3D structure databases

ProteinModelPortaliQ68CQ4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi117972. 19 interactions.
IntActiQ68CQ4. 6 interactions.
MINTiMINT-3002142.
STRINGi9606.ENSP00000419005.

PTM databases

iPTMnetiQ68CQ4.
PhosphoSiteiQ68CQ4.

Polymorphism and mutation databases

BioMutaiDIEXF.
DMDMi117949399.

Proteomic databases

EPDiQ68CQ4.
MaxQBiQ68CQ4.
PaxDbiQ68CQ4.
PeptideAtlasiQ68CQ4.
PRIDEiQ68CQ4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000491415; ENSP00000419005; ENSG00000117597.
GeneIDi27042.
KEGGihsa:27042.
UCSCiuc001hhr.3. human.

Organism-specific databases

CTDi27042.
GeneCardsiDIEXF.
HGNCiHGNC:28440. DIEXF.
HPAiHPA026640.
neXtProtiNX_Q68CQ4.
PharmGKBiPA142672491.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2340. Eukaryota.
ENOG410XP00. LUCA.
GeneTreeiENSGT00390000000709.
HOVERGENiHBG079696.
InParanoidiQ68CQ4.
KOiK14774.
OMAiEVCNMLR.
OrthoDBiEOG7W1535.
PhylomeDBiQ68CQ4.
TreeFamiTF105930.

Miscellaneous databases

GenomeRNAii27042.
NextBioi49618.
PROiQ68CQ4.

Gene expression databases

BgeeiQ68CQ4.
CleanExiHS_C1orf107.
ExpressionAtlasiQ68CQ4. baseline and differential.
GenevisibleiQ68CQ4. HS.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR010678. Digest_organ_expansion_fac-prd.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR12933. PTHR12933. 1 hit.
PfamiPF06862. UTP25. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 2 hits.
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT GLU-67.
    Tissue: Endometrial adenocarcinoma and Fetal kidney.
  2. "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].
  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: Cervix.
  4. "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].
  5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  6. "Systematic analysis of protein pools, isoforms, and modifications affecting turnover and subcellular localization."
    Ahmad Y., Boisvert F.M., Lundberg E., Uhlen M., Lamond A.I.
    Mol. Cell. Proteomics 11:M111.013680.01-M111.013680.15(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiDIEXF_HUMAN
AccessioniPrimary (citable) accession number: Q68CQ4
Secondary accession number(s): O75992, Q4VY00, Q63HL9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: October 31, 2006
Last modified: May 11, 2016
This is version 95 of the entry and version 2 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, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. 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.