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Protein

Protein sprouty homolog 2

Gene

SPRY2

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

Functioni

May function as an antagonist of fibroblast growth factor (FGF) pathways and may negatively modulate respiratory organogenesis.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei144 – 1452Cleavage; by FAP1 Publication

GO - Molecular functioni

  • protein kinase binding Source: BHF-UCL
  • protein serine/threonine kinase activator activity Source: UniProtKB
  • protein serine/threonine kinase inhibitor activity Source: BHF-UCL

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Enzyme and pathway databases

ReactomeiREACT_111080. Spry regulation of FGF signaling.
REACT_12484. EGFR downregulation.
SignaLinkiO43597.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein sprouty homolog 2
Short name:
Spry-2
Gene namesi
Name:SPRY2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 13

Organism-specific databases

HGNCiHGNC:11270. SPRY2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Cytoplasm, Cytoskeleton, Membrane, Microtubule

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi144 – 1441P → L: Inhibits cleavage by the prolyl endopeptidase FAP. 1 Publication

Organism-specific databases

PharmGKBiPA36099.

Polymorphism and mutation databases

BioMutaiSPRY2.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 315315Protein sprouty homolog 2PRO_0000076901Add
BLAST

Post-translational modificationi

Cleaved at Pro-144 by the prolyl endopeptidase FAP (seprase) activity (in vitro).1 Publication

Proteomic databases

PaxDbiO43597.
PRIDEiO43597.

PTM databases

PhosphoSiteiO43597.

Expressioni

Inductioni

By FGF signaling.

Gene expression databases

BgeeiO43597.
CleanExiHS_SPRY2.
ExpressionAtlasiO43597. baseline and differential.
GenevestigatoriO43597.

Organism-specific databases

HPAiCAB037205.
HPA042198.

Interactioni

Subunit structurei

Interacts with RAF1.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
Q5JPT63EBI-742487,EBI-10244213
AQP1P299723EBI-742487,EBI-745213
ATRIPQ8WXE13EBI-742487,EBI-747353
C19orf66Q9NUL53EBI-742487,EBI-10313866
CATSPER1Q8NEC53EBI-742487,EBI-744545
CBLP2268117EBI-742487,EBI-518228
CHRDQ9H2X03EBI-742487,EBI-947551
CREB5Q02930-33EBI-742487,EBI-10192698
EIF4E2O605733EBI-742487,EBI-398610
FAIMQ9NVQ43EBI-742487,EBI-10314711
FRS3O435593EBI-742487,EBI-725515
GNEQ9Y2233EBI-742487,EBI-4291090
GP9P147703EBI-742487,EBI-1754109
GRAP2O757913EBI-742487,EBI-740418
GRB2P629933EBI-742487,EBI-401755
HEXIM2Q96MH23EBI-742487,EBI-5460660
HSD3B7Q9H2F33EBI-742487,EBI-3918847
KRTAP10-11P604123EBI-742487,EBI-10217483
KRTAP10-5P603703EBI-742487,EBI-10172150
KRTAP10-8P604103EBI-742487,EBI-10171774
KRTAP10-9P604113EBI-742487,EBI-10172052
KRTAP4-11Q9BYQ63EBI-742487,EBI-10302392
KRTAP4-12Q9BQ664EBI-742487,EBI-739863
KRTAP4-7Q9BYR03EBI-742487,EBI-10302547
KRTAP5-6Q6L8G93EBI-742487,EBI-10250562
KRTAP5-9P263713EBI-742487,EBI-3958099
KRTAP9-2Q9BYQ43EBI-742487,EBI-1044640
KRTAP9-4Q9BYQ23EBI-742487,EBI-10185730
LASP1Q148473EBI-742487,EBI-742828
LCE1BQ5T7P33EBI-742487,EBI-10245913
LCE2DQ5TA823EBI-742487,EBI-10246750
LCE3CQ5T5A83EBI-742487,EBI-10245291
LCE3EQ5T5B03EBI-742487,EBI-10245456
LCE4AQ5TA783EBI-742487,EBI-10246358
LONRF1Q17RB83EBI-742487,EBI-2341787
MAPKBP1O603363EBI-742487,EBI-947402
MDFIQ997503EBI-742487,EBI-724076
MEOX2A4D1273EBI-742487,EBI-10172134
MID2Q9UJV3-23EBI-742487,EBI-10172526
MLLT6Q6P2C63EBI-742487,EBI-5773143
NCK2O436393EBI-742487,EBI-713635
OTX1P322424EBI-742487,EBI-740446
PACSIN3Q9UKS63EBI-742487,EBI-77926
PRKAB2O437413EBI-742487,EBI-1053424
PTGER3Q147X83EBI-742487,EBI-10234038
RUNX1T1Q06455-43EBI-742487,EBI-10224192
SH3KBP1Q96B972EBI-742487,EBI-346595
SPRY1O436093EBI-742487,EBI-3866665
STK16O757163EBI-742487,EBI-749295
TCAF1Q9Y4C23EBI-742487,EBI-750484
TXNDC5Q86UY03EBI-742487,EBI-2825190
UBASH3AP570754EBI-742487,EBI-2105393
UBASH3BQ8TF423EBI-742487,EBI-1380492
USP20Q9Y2K63EBI-742487,EBI-2511991
ZDHHC17Q8IUH53EBI-742487,EBI-524753
ZNF417Q8TAU33EBI-742487,EBI-740727
ZNF587Q96SQ53EBI-742487,EBI-6427977

Protein-protein interaction databases

BioGridi115547. 115 interactions.
IntActiO43597. 80 interactions.
MINTiMINT-2999467.
STRINGi9606.ENSP00000366306.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3BUMX-ray2.00A49-61[»]
3OB1X-ray2.20A49-60[»]
ProteinModelPortaliO43597.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO43597.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini177 – 291115SPRPROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi125 – 1317Poly-Ser
Compositional biasi178 – 301124Cys-richAdd
BLAST

Domaini

The Cys-rich domain is responsible for the localization of the protein to the membrane ruffles.1 Publication

Sequence similaritiesi

Belongs to the sprouty family.Curated
Contains 1 SPR (sprouty) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG83905.
GeneTreeiENSGT00390000003535.
HOVERGENiHBG003544.
InParanoidiO43597.
KOiK17383.
OMAiETRAQNG.
OrthoDBiEOG7G4QDV.
PhylomeDBiO43597.
TreeFamiTF325070.

Family and domain databases

InterProiIPR007875. Sprouty.
IPR030780. SPRY2.
[Graphical view]
PANTHERiPTHR12365:SF8. PTHR12365:SF8. 1 hit.
PfamiPF05210. Sprouty. 1 hit.
[Graphical view]
PROSITEiPS51227. SPR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O43597-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEARAQSGNG SQPLLQTPRD GGRQRGEPDP RDALTQQVHV LSLDQIRAIR
60 70 80 90 100
NTNEYTEGPT VVPRPGLKPA PRPSTQHKHE RLHGLPEHRQ PPRLQHSQVH
110 120 130 140 150
SSARAPLSRS ISTVSSGSRS STRTSTSSSS SEQRLLGSSF SSGPVADGII
160 170 180 190 200
RVQPKSELKP GELKPLSKED LGLHAYRCED CGKCKCKECT YPRPLPSDWI
210 220 230 240 250
CDKQCLCSAQ NVIDYGTCVC CVKGLFYHCS NDDEDNCADN PCSCSQSHCC
260 270 280 290 300
TRWSAMGVMS LFLPCLWCYL PAKGCLKLCQ GCYDRVNRPG CRCKNSNTVC
310
CKVPTVPPRN FEKPT
Length:315
Mass (Da):34,688
Last modified:June 1, 1998 - v1
Checksum:i8CC6256929D91A7E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti48 – 481A → V in BAG36546 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti106 – 1061P → S.
Corresponds to variant rs504122 [ dbSNP | Ensembl ].
VAR_024647

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF039843 mRNA. Translation: AAC04258.1.
AL713749 mRNA. Translation: CAD28524.1.
AK313810 mRNA. Translation: BAG36546.1.
AL354668 Genomic DNA. Translation: CAI14911.1.
BC015745 mRNA. Translation: AAH15745.1.
CCDSiCCDS9463.1.
RefSeqiNP_005833.1. NM_005842.2.
XP_005266274.1. XM_005266217.1.
XP_006719816.1. XM_006719753.1.
UniGeneiHs.18676.

Genome annotation databases

EnsembliENST00000377102; ENSP00000366306; ENSG00000136158.
ENST00000377104; ENSP00000366308; ENSG00000136158.
GeneIDi10253.
KEGGihsa:10253.
UCSCiuc001vli.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF039843 mRNA. Translation: AAC04258.1.
AL713749 mRNA. Translation: CAD28524.1.
AK313810 mRNA. Translation: BAG36546.1.
AL354668 Genomic DNA. Translation: CAI14911.1.
BC015745 mRNA. Translation: AAH15745.1.
CCDSiCCDS9463.1.
RefSeqiNP_005833.1. NM_005842.2.
XP_005266274.1. XM_005266217.1.
XP_006719816.1. XM_006719753.1.
UniGeneiHs.18676.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3BUMX-ray2.00A49-61[»]
3OB1X-ray2.20A49-60[»]
ProteinModelPortaliO43597.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115547. 115 interactions.
IntActiO43597. 80 interactions.
MINTiMINT-2999467.
STRINGi9606.ENSP00000366306.

PTM databases

PhosphoSiteiO43597.

Polymorphism and mutation databases

BioMutaiSPRY2.

Proteomic databases

PaxDbiO43597.
PRIDEiO43597.

Protocols and materials databases

DNASUi10253.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000377102; ENSP00000366306; ENSG00000136158.
ENST00000377104; ENSP00000366308; ENSG00000136158.
GeneIDi10253.
KEGGihsa:10253.
UCSCiuc001vli.3. human.

Organism-specific databases

CTDi10253.
GeneCardsiGC13M080910.
HGNCiHGNC:11270. SPRY2.
HPAiCAB037205.
HPA042198.
MIMi602466. gene.
neXtProtiNX_O43597.
PharmGKBiPA36099.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG83905.
GeneTreeiENSGT00390000003535.
HOVERGENiHBG003544.
InParanoidiO43597.
KOiK17383.
OMAiETRAQNG.
OrthoDBiEOG7G4QDV.
PhylomeDBiO43597.
TreeFamiTF325070.

Enzyme and pathway databases

ReactomeiREACT_111080. Spry regulation of FGF signaling.
REACT_12484. EGFR downregulation.
SignaLinkiO43597.

Miscellaneous databases

ChiTaRSiSPRY2. human.
EvolutionaryTraceiO43597.
GeneWikiiSPRY2.
GenomeRNAii10253.
NextBioi35467891.
PROiO43597.
SOURCEiSearch...

Gene expression databases

BgeeiO43597.
CleanExiHS_SPRY2.
ExpressionAtlasiO43597. baseline and differential.
GenevestigatoriO43597.

Family and domain databases

InterProiIPR007875. Sprouty.
IPR030780. SPRY2.
[Graphical view]
PANTHERiPTHR12365:SF8. PTHR12365:SF8. 1 hit.
PfamiPF05210. Sprouty. 1 hit.
[Graphical view]
PROSITEiPS51227. SPR. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sprouty encodes a novel antagonist of FGF signaling that patterns apical branching of the Drosophila airways."
    Hacohen N., Kramer S., Sutherland D., Hiromi Y., Krasnow M.A.
    Cell 92:253-263(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "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: Substantia nigra.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  4. "The DNA sequence and analysis of human chromosome 13."
    Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L., Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.
    Nature 428:522-528(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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: Skin.
  6. "Sprouty proteins are targeted to membrane ruffles upon growth factor receptor tyrosine kinase activation. Identification of a novel translocation domain."
    Lim J., Wong E.S.M., Ong S.H., Yusoff P., Low B.C., Guy G.R.
    J. Biol. Chem. 275:32837-32845(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, DOMAIN.
  7. "Mammalian Sprouty4 suppresses Ras-independent ERK activation by binding to Raf1."
    Sasaki A., Taketomi T., Kato R., Saeki K., Nonami A., Sasaki M., Kuriyama M., Saito N., Shibuya M., Yoshimura A.
    Nat. Cell Biol. 5:427-432(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RAF1.
  8. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  9. "Cleavage-site specificity of prolyl endopeptidase FAP investigated with a full-length protein substrate."
    Huang C.H., Suen C.S., Lin C.T., Chien C.H., Lee H.Y., Chung K.M., Tsai T.Y., Jiaang W.T., Hwang M.J., Chen X.
    J. Biochem. 149:685-692(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: CLEAVAGE BY FAP, CLEAVAGE SITE, MUTAGENESIS OF PRO-144.

Entry informationi

Entry nameiSPY2_HUMAN
AccessioniPrimary (citable) accession number: O43597
Secondary accession number(s): B2R9J9, Q5T6Z7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: June 1, 1998
Last modified: May 27, 2015
This is version 131 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, Reference proteome

Documents

  1. Human chromosome 13
    Human chromosome 13: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. 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.