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A1X283

- SPD2B_HUMAN

UniProt

A1X283 - SPD2B_HUMAN

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Protein

SH3 and PX domain-containing protein 2B

Gene

SH3PXD2B

Organism
Homo sapiens (Human)
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 (By similarity).By similarity

GO - Molecular functioni

  1. phosphatidylinositol-3,5-bisphosphate binding Source: UniProtKB
  2. phosphatidylinositol-3-phosphate binding Source: UniProtKB
  3. phosphatidylinositol-4-phosphate binding Source: Ensembl
  4. phosphatidylinositol-5-phosphate binding Source: UniProtKB
  5. SH2 domain 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: UniProtKB
  5. eye development Source: UniProtKB
  6. heart development Source: UniProtKB
  7. podosome assembly Source: UniProtKB
  8. positive regulation of fat cell differentiation Source: Ensembl
  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):
Adapter protein HOFI
Factor for adipocyte differentiation 49
Tyrosine kinase substrate with four SH3 domains
Gene namesi
Name:SH3PXD2B
Synonyms:FAD49, KIAA1295, TKS4
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 5

Organism-specific databases

HGNCiHGNC:29242. SH3PXD2B.

Subcellular locationi

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

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

Involvement in diseasei

Frank-Ter Haar syndrome (FTHS) [MIM:249420]: A syndrome characterized by brachycephaly, wide fontanels, prominent forehead, hypertelorism, prominent eyes, macrocornea with or without glaucoma, full cheeks, small chin, bowing of the long bones and flexion deformity of the fingers.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti43 – 431R → W in FTHS. 1 Publication
VAR_063764

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi249420. phenotype.
Orphaneti1266. Dermato-cardio-skeletal syndrome, Borrone type.
137834. Frank-Ter Haar syndrome.
PharmGKBiPA134864119.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 911911SH3 and PX domain-containing protein 2BPRO_0000312201Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei279 – 2791Phosphoserine1 Publication
Modified residuei291 – 2911Phosphoserine2 Publications
Modified residuei843 – 8431PhosphoserineBy similarity

Post-translational modificationi

Phosphorylated in SRC-transformed cells.By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiA1X283.
PaxDbiA1X283.
PRIDEiA1X283.

PTM databases

PhosphoSiteiA1X283.

Expressioni

Tissue specificityi

Expressed in fibroblasts.1 Publication

Gene expression databases

BgeeiA1X283.
CleanExiHS_SH3PXD2B.
ExpressionAtlasiA1X283. baseline and differential.
GenevestigatoriA1X283.

Organism-specific databases

HPAiHPA036471.

Interactioni

Subunit structurei

Interacts with ADAM15 (By similarity). Interacts with NOXO1. Interacts (via SH3 domains) with NOXA1; the interaction is direct. Interacts with FASLG.By similarity4 Publications

Protein-protein interaction databases

BioGridi130149. 7 interactions.
IntActiA1X283. 2 interactions.
STRINGi9606.ENSP00000309714.

Structurei

3D structure databases

ProteinModelPortaliA1X283.
SMRiA1X283. Positions 7-132, 153-278, 370-550, 842-910.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini5 – 129125PXPROSITE-ProRule annotationAdd
BLAST
Domaini152 – 21160SH3 1PROSITE-ProRule annotationAdd
BLAST
Domaini221 – 28060SH3 2PROSITE-ProRule annotationAdd
BLAST
Domaini368 – 42760SH3 3PROSITE-ProRule annotationAdd
BLAST
Domaini849 – 91163SH3 4PROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi729 – 80678Pro-richAdd
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).By similarity

Sequence similaritiesi

Belongs to the SH3PXD2 family.Curated
Contains 1 PX (phox homology) domain.PROSITE-ProRule annotation
Contains 4 SH3 domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, SH3 domain

Phylogenomic databases

eggNOGiNOG148927.
GeneTreeiENSGT00530000063010.
HOGENOMiHOG000154376.
HOVERGENiHBG107128.
InParanoidiA1X283.
OMAiGHKVLAK.
OrthoDBiEOG7H4DSQ.
PhylomeDBiA1X283.
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.

A1X283-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MPPRRSIVEV KVLDVQKRRV PNKHYVYIIR VTWSSGSTEA IYRRYSKFFD
60 70 80 90 100
LQMQMLDKFP MEGGQKDPKQ RIIPFLPGKI LFRRSHIRDV AVKRLIPIDE
110 120 130 140 150
YCKALIQLPP YISQCDEVLQ FFETRPEDLN PPKEEHIGKK KSGGDQTSVD
160 170 180 190 200
PMVLEQYVVV ANYQKQESSE ISLSVGQVVD IIEKNESGWW FVSTAEEQGW
210 220 230 240 250
VPATCLEGQD GVQDEFSLQP EEEEKYTVIY PYTARDQDEM NLERGAVVEV
260 270 280 290 300
IQKNLEGWWK IRYQGKEGWA PASYLKKNSG EPLPPKPGPG SPSHPGALDL
310 320 330 340 350
DGVSRQQNAV GREKELLSSQ RDGRFEGRPV PDGDAKQRSP KMRQRPPPRR
360 370 380 390 400
DMTIPRGLNL PKPPIPPQVE EEYYTIAEFQ TTIPDGISFQ AGLKVEVIEK
410 420 430 440 450
NLSGWWYIQI EDKEGWAPAT FIDKYKKTSN ASRPNFLAPL PHEVTQLRLG
460 470 480 490 500
EAAALENNTG SEATGPSRPL PDAPHGVMDS GLPWSKDWKG SKDVLRKASS
510 520 530 540 550
DMSASAGYEE ISDPDMEEKP SLPPRKESII KSEGELLERE RERQRTEQLR
560 570 580 590 600
GPTPKPPGVI LPMMPAKHIP PARDSRRPEP KPDKSRLFQL KNDMGLECGH
610 620 630 640 650
KVLAKEVKKP NLRPISKSKT DLPEEKPDAT PQNPFLKSRP QVRPKPAPSP
660 670 680 690 700
KTEPPQGEDQ VDICNLRSKL RPAKSQDKSL LDGEGPQAVG GQDVAFSRSF
710 720 730 740 750
LPGEGPGRAQ DRTGKQDGLS PKEISCRAPP RPAKTTDPVS KSVPVPLQEA
760 770 780 790 800
PQQRPVVPPR RPPPPKKTSS SSRPLPEVRG PQCEGHESRA APTPGRALLV
810 820 830 840 850
PPKAKPFLSN SLGGQDDTRG KGSLGPWGTG KIGENREKAA AASVPNADGL
860 870 880 890 900
KDSLYVAVAD FEGDKDTSSF QEGTVFEVRE KNSSGWWFCQ VLSGAPSWEG
910
WIPSNYLRKK P
Length:911
Mass (Da):101,579
Last modified:May 5, 2009 - v3
Checksum:iA5AA524F9AA21318
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti28 – 281I → V in AAZ99795. 1 PublicationCurated
Sequence conflicti72 – 721I → T in AAZ99795. 1 PublicationCurated
Sequence conflicti712 – 7121R → G in AAZ99795. 1 PublicationCurated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti43 – 431R → W in FTHS. 1 Publication
VAR_063764
Natural varianti101 – 1011Y → F.
Corresponds to variant rs6880739 [ dbSNP | Ensembl ].
VAR_046226

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB430862 mRNA. Translation: BAG81977.1.
DQ109556 mRNA. Translation: AAZ99795.1.
AC008671 Genomic DNA. No translation available.
AC011407 Genomic DNA. No translation available.
AC090064 Genomic DNA. No translation available.
AB037716 mRNA. Translation: BAA92533.1.
CCDSiCCDS34291.1.
RefSeqiNP_001017995.1. NM_001017995.2.
UniGeneiHs.285666.

Genome annotation databases

EnsembliENST00000311601; ENSP00000309714; ENSG00000174705.
GeneIDi285590.
KEGGihsa:285590.
UCSCiuc003mbr.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB430862 mRNA. Translation: BAG81977.1 .
DQ109556 mRNA. Translation: AAZ99795.1 .
AC008671 Genomic DNA. No translation available.
AC011407 Genomic DNA. No translation available.
AC090064 Genomic DNA. No translation available.
AB037716 mRNA. Translation: BAA92533.1 .
CCDSi CCDS34291.1.
RefSeqi NP_001017995.1. NM_001017995.2.
UniGenei Hs.285666.

3D structure databases

ProteinModelPortali A1X283.
SMRi A1X283. Positions 7-132, 153-278, 370-550, 842-910.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 130149. 7 interactions.
IntActi A1X283. 2 interactions.
STRINGi 9606.ENSP00000309714.

PTM databases

PhosphoSitei A1X283.

Proteomic databases

MaxQBi A1X283.
PaxDbi A1X283.
PRIDEi A1X283.

Protocols and materials databases

DNASUi 285590.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000311601 ; ENSP00000309714 ; ENSG00000174705 .
GeneIDi 285590.
KEGGi hsa:285590.
UCSCi uc003mbr.3. human.

Organism-specific databases

CTDi 285590.
GeneCardsi GC05M171693.
H-InvDB HIX0005417.
HGNCi HGNC:29242. SH3PXD2B.
HPAi HPA036471.
MIMi 249420. phenotype.
613293. gene.
neXtProti NX_A1X283.
Orphaneti 1266. Dermato-cardio-skeletal syndrome, Borrone type.
137834. Frank-Ter Haar syndrome.
PharmGKBi PA134864119.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG148927.
GeneTreei ENSGT00530000063010.
HOGENOMi HOG000154376.
HOVERGENi HBG107128.
InParanoidi A1X283.
OMAi GHKVLAK.
OrthoDBi EOG7H4DSQ.
PhylomeDBi A1X283.
TreeFami TF329347.

Miscellaneous databases

ChiTaRSi SH3PXD2B. human.
GenomeRNAii 285590.
NextBioi 95625.
PROi A1X283.
SOURCEi Search...

Gene expression databases

Bgeei A1X283.
CleanExi HS_SH3PXD2B.
ExpressionAtlasi A1X283. baseline and differential.
Genevestigatori A1X283.

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].
  2. "Identification and characterization of HOFI, a novel homolog of FISH."
    Lanyi A., Geiszt M.
    Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "The DNA sequence and comparative analysis of human chromosome 5."
    Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.
    , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
    Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "Prediction of the coding sequences of unidentified human genes. XVI. The complete sequences of 150 new cDNA clones from brain which code for large proteins in vitro."
    Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.
    DNA Res. 7:65-73(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 362-911.
    Tissue: Brain.
  5. "The adaptor protein fish associates with members of the ADAMs family and localizes to podosomes of Src-transformed cells."
    Abram C.L., Seals D.F., Pass I., Salinsky D., Maurer L., Roth T.M., Courtneidge S.A.
    J. Biol. Chem. 278:16844-16851(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, DOMAIN PX, INTERACTION WITH ADAM12; ADAM15 AND ADAM19.
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-291, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. "Identification of SH3 domain interaction partners of human FasL (CD178) by phage display screening."
    Voss M., Lettau M., Janssen O.
    BMC Immunol. 10:53-53(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FASLG.
  8. "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, INTERACTION WITH NOXA1.
  9. Cited for: TISSUE SPECIFICITY, VARIANT FTHS TRP-43.
  10. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-279 AND SER-291, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "Direct interaction between Tks proteins and the N-terminal proline-rich region (PRR) of NoxA1 mediates Nox1-dependent ROS generation."
    Gianni D., Dermardirossian C., Bokoch G.M.
    Eur. J. Cell Biol. 90:164-171(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH NOXA1 AND NOXO1.
  12. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiSPD2B_HUMAN
AccessioniPrimary (citable) accession number: A1X283
Secondary accession number(s): B6F0V2, Q9P2Q1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 4, 2007
Last sequence update: May 5, 2009
Last modified: October 29, 2014
This is version 72 of the entry and version 3 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 5
    Human chromosome 5: 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