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Protein

Protein CREG1

Gene

CREG1

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

Functioni

May contribute to the transcriptional control of cell growth and differentiation. Antagonizes transcriptional activation and cellular transformation by the adenovirus E1A protein. The transcriptional control activity of cell growth requires interaction with IGF2R.2 Publications

GO - Molecular functioni

  • FMN binding Source: InterPro
  • oxidoreductase activity Source: InterPro
  • transcription corepressor activity Source: ProtInc

GO - Biological processi

  • cell proliferation Source: ProtInc
  • multicellular organismal development Source: ProtInc
  • negative regulation of nucleic acid-templated transcription Source: GOC
  • regulation of growth Source: UniProtKB-KW
  • regulation of transcription from RNA polymerase II promoter Source: ProtInc
Complete GO annotation...

Keywords - Biological processi

Growth regulation

Names & Taxonomyi

Protein namesi
Recommended name:
Protein CREG1
Alternative name(s):
Cellular repressor of E1A-stimulated genes 1
Gene namesi
Name:CREG1
Synonyms:CREG
ORF Names:UNQ727/PRO1409
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:2351. CREG1.

Subcellular locationi

GO - Cellular componenti

  • extracellular exosome Source: UniProtKB
  • transcription factor complex Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA26869.

Polymorphism and mutation databases

BioMutaiCREG1.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 31311 PublicationAdd
BLAST
Chaini32 – 220189Protein CREG1PRO_0000006203Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi160 – 1601N-linked (GlcNAc...)1 Publication
Glycosylationi193 – 1931N-linked (GlcNAc...)1 Publication
Glycosylationi216 – 2161N-linked (GlcNAc...)1 Publication

Post-translational modificationi

N-glycosylated.2 Publications

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiO75629.
PaxDbiO75629.
PeptideAtlasiO75629.
PRIDEiO75629.

Expressioni

Gene expression databases

BgeeiO75629.
CleanExiHS_CREG1.
GenevisibleiO75629. HS.

Interactioni

Subunit structurei

Homodimer. Interacts with IGF2R; the interaction is dependent on glycosylation.2 Publications

Protein-protein interaction databases

BioGridi114332. 8 interactions.
IntActiO75629. 2 interactions.
STRINGi9606.ENSP00000359540.

Structurei

Secondary structure

1
220
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi55 – 6511Combined sources
Beta strandi67 – 748Combined sources
Helixi78 – 803Combined sources
Beta strandi84 – 907Combined sources
Beta strandi104 – 1074Combined sources
Helixi112 – 1198Combined sources
Beta strandi122 – 1287Combined sources
Helixi129 – 1313Combined sources
Helixi134 – 1385Combined sources
Beta strandi149 – 15810Combined sources
Helixi161 – 1633Combined sources
Helixi164 – 17411Combined sources
Helixi176 – 1805Combined sources
Helixi183 – 1853Combined sources
Beta strandi188 – 20013Combined sources
Beta strandi202 – 2054Combined sources
Helixi211 – 2166Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1XHNX-ray1.95A/B/C/D49-220[»]
ProteinModelPortaliO75629.
SMRiO75629. Positions 49-218.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO75629.

Family & Domainsi

Sequence similaritiesi

Belongs to the CREG family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG294476.
GeneTreeiENSGT00390000005914.
HOGENOMiHOG000239875.
HOVERGENiHBG051115.
InParanoidiO75629.
OMAiKVNETEM.
OrthoDBiEOG7ZWD33.
PhylomeDBiO75629.
TreeFamiTF324680.

Family and domain databases

Gene3Di2.30.110.10. 1 hit.
InterProiIPR014631. CREG.
IPR012349. Split_barrel_FMN-bd.
[Graphical view]
PIRSFiPIRSF036911. CREG. 1 hit.
SUPFAMiSSF50475. SSF50475. 1 hit.

Sequencei

Sequence statusi: Complete.

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

O75629-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAGLSRGSAR ALLAALLAST LLALLVSPAR GRGGRDHGDW DEASRLPPLP
60 70 80 90 100
PREDAARVAR FVTHVSDWGA LATISTLEAV RGRPFADVLS LSDGPPGAGS
110 120 130 140 150
GVPYFYLSPL QLSVSNLQEN PYATLTMTLA QTNFCKKHGF DPQSPLCVHI
160 170 180 190 200
MLSGTVTKVN ETEMDIAKHS LFIRHPEMKT WPSSHNWFFA KLNITNIWVL
210 220
DYFGGPKIVT PEEYYNVTVQ
Length:220
Mass (Da):24,075
Last modified:November 1, 1998 - v1
Checksum:i0DB95A1E4149CD7C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti52 – 598Missing in BAC04550 (PubMed:16710414).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF084523 mRNA. Translation: AAC34861.1.
AY359071 mRNA. Translation: AAQ89430.1.
AK095456 mRNA. Translation: BAC04550.1.
AK315497 mRNA. Translation: BAG37881.1.
AL031733 Genomic DNA. Translation: CAB42866.1.
CH471067 Genomic DNA. Translation: EAW90795.1.
BC006786 mRNA. Translation: AAH06786.1.
BC008628 mRNA. Translation: AAH08628.1.
CCDSiCCDS1262.1.
RefSeqiNP_003842.1. NM_003851.2.
UniGeneiHs.5710.

Genome annotation databases

EnsembliENST00000370509; ENSP00000359540; ENSG00000143162.
GeneIDi8804.
KEGGihsa:8804.
UCSCiuc001gel.3. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF084523 mRNA. Translation: AAC34861.1.
AY359071 mRNA. Translation: AAQ89430.1.
AK095456 mRNA. Translation: BAC04550.1.
AK315497 mRNA. Translation: BAG37881.1.
AL031733 Genomic DNA. Translation: CAB42866.1.
CH471067 Genomic DNA. Translation: EAW90795.1.
BC006786 mRNA. Translation: AAH06786.1.
BC008628 mRNA. Translation: AAH08628.1.
CCDSiCCDS1262.1.
RefSeqiNP_003842.1. NM_003851.2.
UniGeneiHs.5710.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1XHNX-ray1.95A/B/C/D49-220[»]
ProteinModelPortaliO75629.
SMRiO75629. Positions 49-218.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114332. 8 interactions.
IntActiO75629. 2 interactions.
STRINGi9606.ENSP00000359540.

Polymorphism and mutation databases

BioMutaiCREG1.

Proteomic databases

MaxQBiO75629.
PaxDbiO75629.
PeptideAtlasiO75629.
PRIDEiO75629.

Protocols and materials databases

DNASUi8804.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000370509; ENSP00000359540; ENSG00000143162.
GeneIDi8804.
KEGGihsa:8804.
UCSCiuc001gel.3. human.

Organism-specific databases

CTDi8804.
GeneCardsiGC01M167498.
HGNCiHGNC:2351. CREG1.
neXtProtiNX_O75629.
PharmGKBiPA26869.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG294476.
GeneTreeiENSGT00390000005914.
HOGENOMiHOG000239875.
HOVERGENiHBG051115.
InParanoidiO75629.
OMAiKVNETEM.
OrthoDBiEOG7ZWD33.
PhylomeDBiO75629.
TreeFamiTF324680.

Miscellaneous databases

EvolutionaryTraceiO75629.
GeneWikiiCREG1.
GenomeRNAii8804.
NextBioi33024.
PROiO75629.

Gene expression databases

BgeeiO75629.
CleanExiHS_CREG1.
GenevisibleiO75629. HS.

Family and domain databases

Gene3Di2.30.110.10. 1 hit.
InterProiIPR014631. CREG.
IPR012349. Split_barrel_FMN-bd.
[Graphical view]
PIRSFiPIRSF036911. CREG. 1 hit.
SUPFAMiSSF50475. SSF50475. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A cellular repressor of E1A-stimulated genes that inhibits activation by E2F."
    Veal E., Eisenstein M., Tseng Z.H., Gill G.
    Mol. Cell. Biol. 18:5032-5041(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Tongue.
  4. "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].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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: Lymph and Placenta.
  7. "Signal peptide prediction based on analysis of experimentally verified cleavage sites."
    Zhang Z., Henzel W.J.
    Protein Sci. 13:2819-2824(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 32-46.
  8. "The secreted glycoprotein CREG enhances differentiation of NTERA-2 human embryonal carcinoma cells."
    Veal E., Groisman R., Eisenstein M., Gill G.
    Oncogene 19:2120-2128(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, GLYCOSYLATION.
  9. "The secreted glycoprotein CREG inhibits cell growth dependent on the mannose-6-phosphate/insulin-like growth factor II receptor."
    Di Bacco A., Gill G.
    Oncogene 22:5436-5445(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH IGF2R, FUNCTION.
  10. "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
    Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
    J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-160; ASN-193 AND ASN-216.
    Tissue: Liver.
  11. "The crystal structure of CREG, a secreted glycoprotein involved in cellular growth and differentiation."
    Sacher M., Di Bacco A., Lunin V.V., Ye Z., Wagner J., Gill G., Cygler M.
    Proc. Natl. Acad. Sci. U.S.A. 102:18326-18331(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 49-220, SUBUNIT.

Entry informationi

Entry nameiCREG1_HUMAN
AccessioniPrimary (citable) accession number: O75629
Secondary accession number(s): B2RDD4, Q8N9A3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 15, 2005
Last sequence update: November 1, 1998
Last modified: June 24, 2015
This is version 118 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

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.