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Protein

Protein sprouty homolog 3

Gene

SPRY3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 3 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.

GO - Biological processi

  1. multicellular organismal development Source: UniProtKB
  2. regulation of signal transduction Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Names & Taxonomyi

Protein namesi
Recommended name:
Protein sprouty homolog 3
Short name:
Spry-3
Gene namesi
Name:SPRY3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome X

Organism-specific databases

HGNCiHGNC:11271. SPRY3.

Subcellular locationi

Cytoplasm. Membrane; Peripheral membrane protein
Note: Found in the cytoplasm in unstimulated cells but is translocated to the membrane ruffles in cells stimulated with EGF (epidermal growth factor).

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
  2. membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA36100.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 288288Protein sprouty homolog 3PRO_0000076904Add
BLAST

Proteomic databases

MaxQBiO43610.
PaxDbiO43610.
PRIDEiO43610.

PTM databases

PhosphoSiteiO43610.

Expressioni

Tissue specificityi

Widely expressed; particularly in the fetal tissues.

Inductioni

By FGF signaling.

Gene expression databases

BgeeiO43610.
CleanExiHS_SPRY3.
GenevestigatoriO43610.

Organism-specific databases

HPAiCAB013505.

Interactioni

Protein-protein interaction databases

BioGridi115545. 1 interaction.
STRINGi9606.ENSP00000302978.

Structurei

3D structure databases

ProteinModelPortaliO43610.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini154 – 260107SPRPROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi147 – 270124Cys-richAdd
BLAST

Domaini

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

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiNOG128987.
GeneTreeiENSGT00390000003535.
HOGENOMiHOG000233079.
HOVERGENiHBG003544.
InParanoidiO43610.
KOiK17384.
OMAiGRCKCVL.
OrthoDBiEOG7G4QDV.
PhylomeDBiO43610.
TreeFamiTF325070.

Family and domain databases

InterProiIPR007875. Sprouty.
[Graphical view]
PfamiPF05210. Sprouty. 1 hit.
[Graphical view]
PROSITEiPS51227. SPR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O43610-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDAAVTDDFQ QILPIEQLRS THASNDYVER PPAPCKQALS SPSLIVQTHK
60 70 80 90 100
SDWSLATMPT SLPRSLSQCH QLQPLPQHLS QSSIASSMSH STTASDQRLL
110 120 130 140 150
ASITPSPSGQ SIIRTQPGAG VHPKADGALK GEAEQSAGHP SEHLFICEEC
160 170 180 190 200
GRCKCVPCTA ARPLPSCWLC NQRCLCSAES LLDYGTCLCC VKGLFYHCST
210 220 230 240 250
DDEDNCADEP CSCGPSSCFV RWAAMSLISL FLPCLCCYLP TRGCLHLCQQ
260 270 280
GYDSLRRPGC RCKRHTNTVC RKISSGSAPF PKAQEKSV
Length:288
Mass (Da):31,222
Last modified:February 21, 2001 - v2
Checksum:i62C59F5E897D99B8
GO

Sequence cautioni

The sequence AAC39567.1 differs from that shown. Reason: Frameshift at position 96. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti93 – 931T → P in AAC39567 (PubMed:9458049).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti161 – 1611A → T.
Corresponds to variant rs35474915 [ dbSNP | Ensembl ].
VAR_034519

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ271735 Genomic DNA. Translation: CAB96768.1.
AK289543 mRNA. Translation: BAF82232.1.
CH471247 Genomic DNA. Translation: EAW55876.1.
BC069609 mRNA. Translation: AAH69609.1.
BC074972 mRNA. Translation: AAH74972.1.
BC074973 mRNA. Translation: AAH74973.1.
AF041038 mRNA. Translation: AAC39567.1. Frameshift.
CCDSiCCDS14769.4.
RefSeqiNP_005831.1. NM_005840.1.
XP_005274699.1. XM_005274642.2.
XP_005274700.1. XM_005274643.2.
XP_005274857.1. XM_005274800.2.
UniGeneiHs.381912.

Genome annotation databases

EnsembliENST00000302805; ENSP00000302978; ENSG00000168939.
GeneIDi10251.
KEGGihsa:10251.
UCSCiuc004fnq.1. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ271735 Genomic DNA. Translation: CAB96768.1.
AK289543 mRNA. Translation: BAF82232.1.
CH471247 Genomic DNA. Translation: EAW55876.1.
BC069609 mRNA. Translation: AAH69609.1.
BC074972 mRNA. Translation: AAH74972.1.
BC074973 mRNA. Translation: AAH74973.1.
AF041038 mRNA. Translation: AAC39567.1. Frameshift.
CCDSiCCDS14769.4.
RefSeqiNP_005831.1. NM_005840.1.
XP_005274699.1. XM_005274642.2.
XP_005274700.1. XM_005274643.2.
XP_005274857.1. XM_005274800.2.
UniGeneiHs.381912.

3D structure databases

ProteinModelPortaliO43610.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115545. 1 interaction.
STRINGi9606.ENSP00000302978.

PTM databases

PhosphoSiteiO43610.

Proteomic databases

MaxQBiO43610.
PaxDbiO43610.
PRIDEiO43610.

Protocols and materials databases

DNASUi10251.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000302805; ENSP00000302978; ENSG00000168939.
GeneIDi10251.
KEGGihsa:10251.
UCSCiuc004fnq.1. human.

Organism-specific databases

CTDi10251.
GeneCardsiGC0XP154997.
HGNCiHGNC:11271. SPRY3.
HPAiCAB013505.
MIMi300531. gene.
neXtProtiNX_O43610.
PharmGKBiPA36100.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG128987.
GeneTreeiENSGT00390000003535.
HOGENOMiHOG000233079.
HOVERGENiHBG003544.
InParanoidiO43610.
KOiK17384.
OMAiGRCKCVL.
OrthoDBiEOG7G4QDV.
PhylomeDBiO43610.
TreeFamiTF325070.

Miscellaneous databases

GeneWikiiSPRY3.
GenomeRNAii10251.
NextBioi38842.
PROiO43610.
SOURCEiSearch...

Gene expression databases

BgeeiO43610.
CleanExiHS_SPRY3.
GenevestigatoriO43610.

Family and domain databases

InterProiIPR007875. Sprouty.
[Graphical view]
PfamiPF05210. Sprouty. 1 hit.
[Graphical view]
PROSITEiPS51227. SPR. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  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: Cerebellum.
  3. "The DNA sequence of the human X chromosome."
    Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
    , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
    Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. 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].
  6. "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] OF 93-191.

Entry informationi

Entry nameiSPY3_HUMAN
AccessioniPrimary (citable) accession number: O43610
Secondary accession number(s): A8K0H8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: February 21, 2001
Last modified: January 7, 2015
This is version 107 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

Miscellaneous

The gene coding for this protein is located in the pseudoautosomal region 2 (PAR2) of X and Y chromosomes.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome X
    Human chromosome X: 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

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.