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Q9H772

- GREM2_HUMAN

UniProt

Q9H772 - GREM2_HUMAN

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Protein

Gremlin-2

Gene

GREM2

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

Functioni

Cytokine that inhibits the activity of BMP2 and BMP4 in a dose-dependent manner, and thereby modulates signaling by BMP family members. Contributes to the regulation of embryonic morphogenesis via BMP family members. Antagonizes BMP4-induced suppression of progesterone production in granulosa cells (By similarity).By similarity

GO - Molecular functioni

  1. heparin binding Source: UniProtKB

GO - Biological processi

  1. BMP signaling pathway Source: Reactome
  2. cytokine-mediated signaling pathway Source: UniProtKB
  3. determination of dorsal identity Source: Ensembl
  4. embryonic body morphogenesis Source: UniProtKB
  5. regulation of cytokine activity Source: UniProtKB
  6. sequestering of BMP from receptor via BMP binding Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Cytokine, Developmental protein

Keywords - Ligandi

Heparin-binding

Enzyme and pathway databases

ReactomeiREACT_12034. Signaling by BMP.
SignaLinkiQ9H772.

Names & Taxonomyi

Protein namesi
Recommended name:
Gremlin-2
Alternative name(s):
Cysteine knot superfamily 1, BMP antagonist 2
DAN domain family member 3
Protein related to DAN and cerberus
Gene namesi
Name:GREM2
Synonyms:CKTSF1B2, DAND3, PRDC
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:17655. GREM2.

Subcellular locationi

Secreted Curated

GO - Cellular componenti

  1. extracellular region Source: Reactome
  2. extracellular space Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134968998.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2121Sequence AnalysisAdd
BLAST
Chaini22 – 168147Gremlin-2PRO_0000006720Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi40 – 401N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi73 ↔ 123PROSITE-ProRule annotation
Disulfide bondi87 ↔ 137PROSITE-ProRule annotation
Disulfide bondi97 ↔ 155PROSITE-ProRule annotation
Disulfide bondi101 ↔ 157PROSITE-ProRule annotation
Glycosylationi161 – 1611N-linked (GlcNAc...)Sequence Analysis

Post-translational modificationi

N-glycosylated.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ9H772.
PRIDEiQ9H772.

PTM databases

PhosphoSiteiQ9H772.

Expressioni

Gene expression databases

BgeeiQ9H772.
CleanExiHS_GREM2.
GenevestigatoriQ9H772.

Organism-specific databases

HPAiCAB009920.

Interactioni

Subunit structurei

Homodimer. Interacts with BMP2, BMP4 and BMP7, but has lower affinity for BMP7 than for BMP2 and BMP4. Binds heparin; this impairs the interaction with BMP2 (By similarity).By similarity

Protein-protein interaction databases

BioGridi122150. 1 interaction.
STRINGi9606.ENSP00000318650.

Structurei

3D structure databases

ProteinModelPortaliQ9H772.
SMRiQ9H772. Positions 50-160.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini73 – 16391CTCKPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the DAN family.Curated
Contains 1 CTCK (C-terminal cystine knot-like) domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG41424.
GeneTreeiENSGT00510000046909.
HOGENOMiHOG000237358.
HOVERGENiHBG051837.
InParanoidiQ9H772.
OMAiCAFCKPH.
OrthoDBiEOG7Q2N7B.
PhylomeDBiQ9H772.
TreeFamiTF106445.

Family and domain databases

InterProiIPR006207. Cys_knot_C.
IPR004133. DAN.
IPR017159. Gremlin_precursor.
[Graphical view]
PfamiPF03045. DAN. 1 hit.
[Graphical view]
PIRSFiPIRSF037254. Gremlin_precursor. 1 hit.
SMARTiSM00041. CT. 1 hit.
[Graphical view]
PROSITEiPS01225. CTCK_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q9H772-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MFWKLSLSLF LVAVLVKVAE ARKNRPAGAI PSPYKDGSSN NSERWQHQIK
60 70 80 90 100
EVLASSQEAL VVTERKYLKS DWCKTQPLRQ TVSEEGCRSR TILNRFCYGQ
110 120 130 140 150
CNSFYIPRHV KKEEESFQSC AFCKPQRVTS VLVELECPGL DPPFRLKKIQ
160
KVKQCRCMSV NLSDSDKQ
Length:168
Mass (Da):19,320
Last modified:March 1, 2001 - v1
Checksum:iD5A4E4E818BF8C0E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti11 – 111L → M in AAH46632. (PubMed:15489334)Curated
Sequence conflicti31 – 311P → H in AAH46632. (PubMed:15489334)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti131 – 1311V → I.
Corresponds to variant rs34188522 [ dbSNP | Ensembl ].
VAR_048876

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK024848 mRNA. Translation: BAB15026.1.
AL358176 Genomic DNA. Translation: CAH74074.1.
BC046632 mRNA. Translation: AAH46632.1.
CCDSiCCDS31070.1.
RefSeqiNP_071914.3. NM_022469.3.
UniGeneiHs.98206.

Genome annotation databases

EnsembliENST00000318160; ENSP00000318650; ENSG00000180875.
GeneIDi64388.
KEGGihsa:64388.
UCSCiuc001hys.3. human.

Polymorphism databases

DMDMi62510699.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK024848 mRNA. Translation: BAB15026.1 .
AL358176 Genomic DNA. Translation: CAH74074.1 .
BC046632 mRNA. Translation: AAH46632.1 .
CCDSi CCDS31070.1.
RefSeqi NP_071914.3. NM_022469.3.
UniGenei Hs.98206.

3D structure databases

ProteinModelPortali Q9H772.
SMRi Q9H772. Positions 50-160.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 122150. 1 interaction.
STRINGi 9606.ENSP00000318650.

PTM databases

PhosphoSitei Q9H772.

Polymorphism databases

DMDMi 62510699.

Proteomic databases

PaxDbi Q9H772.
PRIDEi Q9H772.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000318160 ; ENSP00000318650 ; ENSG00000180875 .
GeneIDi 64388.
KEGGi hsa:64388.
UCSCi uc001hys.3. human.

Organism-specific databases

CTDi 64388.
GeneCardsi GC01M240652.
HGNCi HGNC:17655. GREM2.
HPAi CAB009920.
MIMi 608832. gene.
neXtProti NX_Q9H772.
PharmGKBi PA134968998.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG41424.
GeneTreei ENSGT00510000046909.
HOGENOMi HOG000237358.
HOVERGENi HBG051837.
InParanoidi Q9H772.
OMAi CAFCKPH.
OrthoDBi EOG7Q2N7B.
PhylomeDBi Q9H772.
TreeFami TF106445.

Enzyme and pathway databases

Reactomei REACT_12034. Signaling by BMP.
SignaLinki Q9H772.

Miscellaneous databases

GenomeRNAii 64388.
NextBioi 66317.
PROi Q9H772.
SOURCEi Search...

Gene expression databases

Bgeei Q9H772.
CleanExi HS_GREM2.
Genevestigatori Q9H772.

Family and domain databases

InterProi IPR006207. Cys_knot_C.
IPR004133. DAN.
IPR017159. Gremlin_precursor.
[Graphical view ]
Pfami PF03045. DAN. 1 hit.
[Graphical view ]
PIRSFi PIRSF037254. Gremlin_precursor. 1 hit.
SMARTi SM00041. CT. 1 hit.
[Graphical view ]
PROSITEi PS01225. CTCK_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "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: Colon.
  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: Brain.
  4. "Identification and characterization of human CKTSF1B2 and CKTSF1B3 genes in silico."
    Katoh M., Katoh M.
    Oncol. Rep. 12:423-427(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION.

Entry informationi

Entry nameiGREM2_HUMAN
AccessioniPrimary (citable) accession number: Q9H772
Secondary accession number(s): Q86UD9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 12, 2005
Last sequence update: March 1, 2001
Last modified: October 29, 2014
This is version 92 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, 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. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3