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A2AAY5

- SPD2B_MOUSE

UniProt

A2AAY5 - SPD2B_MOUSE

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Protein
SH3 and PX domain-containing protein 2B
Gene
Sh3pxd2b, Fad49, Tks4
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Adapter protein involved in invadopodia and podosome formation and extracellular matrix degradation. Binds matrix metalloproteinases (ADAMs), NADPH oxidases (NOXs) and phosphoinositides. Acts as an organizer protein that allows NOX1- or NOX3-dependent reactive oxygen species (ROS) generation and ROS localization. Plays a role in mitotic clonal expansion during the immediate early stage of adipocyte differentiation.3 Publications

GO - Molecular functioni

  1. SH2 domain binding Source: UniProtKB
  2. phosphatidylinositol-3,5-bisphosphate binding Source: UniProtKB
  3. phosphatidylinositol-3-phosphate binding Source: UniProtKB
  4. phosphatidylinositol-4-phosphate binding Source: UniProtKB
  5. phosphatidylinositol-5-phosphate binding Source: UniProtKB

GO - Biological processi

  1. adipose tissue development Source: UniProtKB
  2. bone development Source: UniProtKB
  3. cell differentiation Source: UniProtKB-KW
  4. extracellular matrix disassembly Source: Ensembl
  5. eye development Source: UniProtKB
  6. heart development Source: UniProtKB
  7. podosome assembly Source: UniProtKB
  8. positive regulation of fat cell differentiation Source: UniProtKB
  9. protein localization to membrane Source: UniProtKB
  10. skeletal system development Source: UniProtKB
  11. superoxide metabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Differentiation

Names & Taxonomyi

Protein namesi
Recommended name:
SH3 and PX domain-containing protein 2B
Alternative name(s):
Factor for adipocyte differentiation 49
Tyrosine kinase substrate with four SH3 domains
Gene namesi
Name:Sh3pxd2b
Synonyms:Fad49, Tks4
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 11

Organism-specific databases

MGIiMGI:2442062. Sh3pxd2b.

Subcellular locationi

Cytoplasm. Cell projectionpodosome
Note: Cytoplasmic in normal cells and localizes to podosomes in SRC-transformed cells.3 Publications

GO - Cellular componenti

  1. cell junction Source: UniProtKB-KW
  2. cell projection Source: UniProtKB-KW
  3. cytoplasm Source: UniProtKB
  4. podosome Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell projection, Cytoplasm

Pathology & Biotechi

Disruption phenotypei

Exhibit skeletal, cardiac and eye phenotypes. Mice have glaucoma and suffer growth retardation as well as craniofacial defects. Skeletons show marked kyphosis, poorly aligned teeth, anomalies in the iliac crest, and a prominent xiphisternum. Mice show loss of adipose tissue as well as cardiac deficiencies, such as dysmorphic ventricular chambers, thin mitral valves and immature and disarrayed trabeculae with frequent apical indentation. Mice show loss of ROS formation.2 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi25 – 251Y → F: Reduced phosphorylation. Almost complete loss of phosphorylation; when associated with F-373 and F-508. 1 Publication
Mutagenesisi373 – 3731Y → F: Reduced phosphorylation. Almost complete loss of phosphorylation; when associated with F-25 and F-508. 1 Publication
Mutagenesisi508 – 5081Y → F: Reduced phosphorylation. Almost complete loss of phosphorylation; when associated with F-25 and F-373. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 908908SH3 and PX domain-containing protein 2B
PRO_0000312202Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei25 – 251Phosphotyrosine Inferred
Modified residuei279 – 2791Phosphoserine By similarity
Modified residuei291 – 2911Phosphoserine By similarity
Modified residuei661 – 6611Phosphotyrosine1 Publication
Modified residuei840 – 8401Phosphoserine1 Publication

Post-translational modificationi

Phosphorylated in SRC-transformed cells.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiA2AAY5.
PRIDEiA2AAY5.

PTM databases

PhosphoSiteiA2AAY5.

Expressioni

Tissue specificityi

Highly expressed in the stromal-vascular fraction of white adipose tissue with moderate expression in heart, skeletal muscle and the mature adipocyte fraction of white adipose tissue. Also expressed in brain, spleen, kidney and liver. Expressed in white and brown adipose tissues, eye, lung, heart, brain, spleen, stomach, liver and skeletal muscle (at protein level). Not expressed in kidney or bone marrow.3 Publications

Developmental stagei

Expression increases quickly after induction of adipocyte differentiation, reaches a maximum after 3 hours and decreases by 12 hours. Expressed from embryonic day E10.5 in heart and hindbrain, followed by an increased expression at E12.5 that also involves a subset of cells on the luminal side of the left ventricular wall in the case of the heart and neuroepithelium in the case of the brain. At E14.5, expression is present in developing bones (proximal ribs, lower jaw and clavicle), but the expression in the heart is no longer detectable. At stages E16.5 and E18.5, strong expression is seen in the long bones of the limbs, particularly in the growth plates, as well as in the facial and cranial bones and the primordial incisor. Expression in the ribs is seen in the proximal regions in those areas where the transition from cartilage to bone is expected to occur. Expression in the eye at E16.5 is highly specific for the ganglion cell layer.2 Publications

Gene expression databases

ArrayExpressiA2AAY5.
BgeeiA2AAY5.
CleanExiMM_SH3PXD2B.
GenevestigatoriA2AAY5.

Interactioni

Subunit structurei

Interacts with NOXO1 By similarity. Interacts (via SH3 domains) with NOXA1; the interaction is direct By similarity. Interacts with ADAM15. Interacts with FASLG By similarity.1 Publication

Protein-protein interaction databases

IntActiA2AAY5. 1 interaction.
MINTiMINT-4110712.

Structurei

3D structure databases

ProteinModelPortaliA2AAY5.
SMRiA2AAY5. Positions 7-132, 153-278, 370-432, 844-907.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini5 – 129125PX
Add
BLAST
Domaini152 – 21160SH3 1
Add
BLAST
Domaini221 – 28060SH3 2
Add
BLAST
Domaini368 – 42760SH3 3
Add
BLAST
Domaini846 – 90863SH3 4
Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi718 – 77760Pro-rich
Add
BLAST

Domaini

The PX domain is required for podosome localization because of its ability to bind phosphatidylinositol 3-phosphate (PtdIns3P) and phosphatidylinositol 3,4-bisphosphate (PtdIns(3,4)P2) and, to a lesser extent, phosphatidylinositol 4-phosphate (PtdIns4P), phosphatidylinositol 5-phosphate (PtdIns5P), and phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2). Binds to the third intramolecular SH3 domain By similarity.1 Publication

Sequence similaritiesi

Belongs to the SH3PXD2 family.
Contains 4 SH3 domains.

Keywords - Domaini

Repeat, SH3 domain

Phylogenomic databases

eggNOGiNOG148927.
GeneTreeiENSGT00530000063010.
HOGENOMiHOG000154376.
HOVERGENiHBG107128.
InParanoidiA2AAY5.
OMAiGHKVLAK.
OrthoDBiEOG7H4DSQ.
PhylomeDBiA2AAY5.
TreeFamiTF329347.

Family and domain databases

Gene3Di3.30.1520.10. 1 hit.
InterProiIPR001683. Phox.
IPR011511. SH3_2.
IPR001452. SH3_domain.
[Graphical view]
PfamiPF00787. PX. 1 hit.
PF00018. SH3_1. 3 hits.
PF07653. SH3_2. 1 hit.
[Graphical view]
SMARTiSM00312. PX. 1 hit.
SM00326. SH3. 4 hits.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 4 hits.
SSF64268. SSF64268. 1 hit.
PROSITEiPS50195. PX. 1 hit.
PS50002. SH3. 4 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

A2AAY5-1 [UniParc]FASTAAdd to Basket

« Hide

MPPRRSIVEV KVLDVQKRRV PNKHYVYIIR VTWSSGATEA IYRRYSKFFD    50
LQMQMLDKFP MEGGQKDPKQ RIIPFLPGKI LFRRSHIRDV AVKRLIPIDE 100
YCKALIQLPP YISQCDEVLQ FFETRPEDLN PPKEEHIGKK KSGNDPTSVD 150
PMVLEQYVVV ADYQKQESSE ISLSVGQVVD IIEKNESGWW FVSTAEEQGW 200
VPATCLEGQD GVQDEFSLQP EEEEKYTVIY PYTARDQDEM NLERGAVVEV 250
VQKNLEGWWK IRYQGKEGWA PASYLKKNSG EPLPPKLGPS SPAHSGALDL 300
DGVSRHQNAM GREKELLNNQ RDGRFEGRLV PDGDVKQRSP KMRQRPPPRR 350
DMTIPRGLNL PKPPIPPQVE EEYYTIAEFQ TTIPDGISFQ AGLKVEVIEK 400
SLSGWWYIQM EDKEGWAPAT FIDKYKKTSS ASRPNFLAPL PHEMTQLRLG 450
DAAATENNTG PEAVGPSRPL PEAPHGAVDS GMLWSKDWKG GKEAPRKASS 500
DLSASTGYEE ISDPTQEEKP SLPPRKESII KSEEELLERE RQKMEPLRGS 550
SPKPPGMILP MIPAKHAPLA RDSRKPEPKL DKSKFPLRND MGLECGHKVL 600
AKEVKKPNLR PISRSKAELS EEKVDPTSQN LFMKSRPQVR PKPTPSPKTE 650
PAQSEDHVDI YNLRSKLRPA KSQEKALLDG ESHHAAGSHD TALSRSFLPG 700
EGPGHGQDRS GRQDGLSPKE TPCRAPPRPA KTTDPGPKNV PVPVQEATLQ 750
QRPVVPPRRP PPPKKTSSSP LSCRPLPEVR GAQREESRVA PAAGRALLVP 800
PKAKPFLSNS SVGQDDMRGK GGLGPRVTGK VGETREKAAS FLNADGPKDS 850
LYVAVANFEG DEDTSSFQEG TVFEVREKNS SGWWFCQVLS GAPSWEGWIP 900
SNYLRKKP 908
Length:908
Mass (Da):101,517
Last modified:February 20, 2007 - v1
Checksum:i83341ABA6DF639AB
GO

Sequence cautioni

The sequence BAC40843.1 differs from that shown. Reason: Frameshift at several positions.

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti464 – 4641V → M in BAG81976. 1 Publication
Sequence conflicti464 – 4641V → M in AAI15765. 1 Publication
Sequence conflicti744 – 7441V → VSV in BAG81976. 1 Publication
Sequence conflicti744 – 7441V → VSV in BAE42425. 1 Publication
Sequence conflicti749 – 7491L → Q in BAG81976. 1 Publication
Sequence conflicti749 – 7491L → Q in BAE42425. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB430861 mRNA. Translation: BAG81976.1.
AK089330 mRNA. Translation: BAC40843.1. Frameshift.
AK171384 mRNA. Translation: BAE42425.1.
AL662780 Genomic DNA. Translation: CAM22517.1.
BC115711 mRNA. Translation: AAI15712.1.
BC115764 mRNA. Translation: AAI15765.1.
CCDSiCCDS24526.1.
RefSeqiNP_796338.2. NM_177364.3.
UniGeneiMm.227616.

Genome annotation databases

EnsembliENSMUST00000038753; ENSMUSP00000044276; ENSMUSG00000040711.
GeneIDi268396.
KEGGimmu:268396.
UCSCiuc007ijq.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB430861 mRNA. Translation: BAG81976.1 .
AK089330 mRNA. Translation: BAC40843.1 . Frameshift.
AK171384 mRNA. Translation: BAE42425.1 .
AL662780 Genomic DNA. Translation: CAM22517.1 .
BC115711 mRNA. Translation: AAI15712.1 .
BC115764 mRNA. Translation: AAI15765.1 .
CCDSi CCDS24526.1.
RefSeqi NP_796338.2. NM_177364.3.
UniGenei Mm.227616.

3D structure databases

ProteinModelPortali A2AAY5.
SMRi A2AAY5. Positions 7-132, 153-278, 370-432, 844-907.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi A2AAY5. 1 interaction.
MINTi MINT-4110712.

PTM databases

PhosphoSitei A2AAY5.

Proteomic databases

PaxDbi A2AAY5.
PRIDEi A2AAY5.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000038753 ; ENSMUSP00000044276 ; ENSMUSG00000040711 .
GeneIDi 268396.
KEGGi mmu:268396.
UCSCi uc007ijq.1. mouse.

Organism-specific databases

CTDi 285590.
MGIi MGI:2442062. Sh3pxd2b.

Phylogenomic databases

eggNOGi NOG148927.
GeneTreei ENSGT00530000063010.
HOGENOMi HOG000154376.
HOVERGENi HBG107128.
InParanoidi A2AAY5.
OMAi GHKVLAK.
OrthoDBi EOG7H4DSQ.
PhylomeDBi A2AAY5.
TreeFami TF329347.

Miscellaneous databases

NextBioi 392275.
PROi A2AAY5.
SOURCEi Search...

Gene expression databases

ArrayExpressi A2AAY5.
Bgeei A2AAY5.
CleanExi MM_SH3PXD2B.
Genevestigatori A2AAY5.

Family and domain databases

Gene3Di 3.30.1520.10. 1 hit.
InterProi IPR001683. Phox.
IPR011511. SH3_2.
IPR001452. SH3_domain.
[Graphical view ]
Pfami PF00787. PX. 1 hit.
PF00018. SH3_1. 3 hits.
PF07653. SH3_2. 1 hit.
[Graphical view ]
SMARTi SM00312. PX. 1 hit.
SM00326. SH3. 4 hits.
[Graphical view ]
SUPFAMi SSF50044. SSF50044. 4 hits.
SSF64268. SSF64268. 1 hit.
PROSITEi PS50195. PX. 1 hit.
PS50002. SH3. 4 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "A novel gene, fad49, plays a crucial role in the immediate early stage of adipocyte differentiation via involvement in mitotic clonal expansion."
    Hishida T., Eguchi T., Osada S., Nishizuka M., Imagawa M.
    FEBS J. 275:5576-5588(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, DOMAIN.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Dendritic cell.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  4. "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] OF 1-647.
  5. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
    Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
    Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-661, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  6. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-840, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. "The podosomal-adaptor protein SH3PXD2B is essential for normal postnatal development."
    Mao M., Thedens D.R., Chang B., Harris B.S., Zheng Q.Y., Johnson K.R., Donahue L.R., Anderson M.G.
    Mamm. Genome 20:462-475(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH ADAM15.
  8. "The novel adaptor protein Tks4 (SH3PXD2B) is required for functional podosome formation."
    Buschman M.D., Bromann P.A., Cejudo-Martin P., Wen F., Pass I., Courtneidge S.A.
    Mol. Biol. Cell 20:1302-1311(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY, PHOSPHORYLATION, MUTAGENESIS OF TYR-25; TYR-373 AND TYR-508, SUBCELLULAR LOCATION.
  9. "Novel p47(phox)-related organizers regulate localized NADPH oxidase 1 (Nox1) activity."
    Gianni D., Diaz B., Taulet N., Fowler B., Courtneidge S.A., Bokoch G.M.
    Sci. Signal. 2:RA54-RA54(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  10. Cited for: DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE.

Entry informationi

Entry nameiSPD2B_MOUSE
AccessioniPrimary (citable) accession number: A2AAY5
Secondary accession number(s): B6F0V1
, Q1LZL8, Q1LZM5, Q3TB89, Q8BIC6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 4, 2007
Last sequence update: February 20, 2007
Last modified: July 9, 2014
This is version 67 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi