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Q9UJU6

- DBNL_HUMAN

UniProt

Q9UJU6 - DBNL_HUMAN

Protein

Drebrin-like protein

Gene

DBNL

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 132 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
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    Functioni

    Adapter protein that binds F-actin and DNM1, and thereby plays a role in receptor-mediated endocytosis. Plays a role in the reorganization of the actin cytoskeleton, formation of cell projections, such as neurites, in neuron morphogenesis and synapse formation via its interaction with WASL and COBL. Does not bind G-actin and promote actin polymerization by itself. Required for the formation of organized podosome rosettes By similarity. May act as a common effector of antigen receptor-signaling pathways in leukocytes. Acts as a key component of the immunological synapse that regulates T-cell activation by bridging TCRs and the actin cytoskeleton to gene activation and endocytic processes.By similarity1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei361 – 3622Cleavage; by caspase-3

    GO - Molecular functioni

    1. actin binding Source: UniProtKB
    2. actin filament binding Source: UniProtKB
    3. enzyme activator activity Source: ProtInc
    4. protein binding Source: IntAct

    GO - Biological processi

    1. activation of JUN kinase activity Source: ProtInc
    2. apoptotic process Source: Reactome
    3. cellular component disassembly involved in execution phase of apoptosis Source: Reactome
    4. endocytosis Source: UniProtKB-KW
    5. immune system process Source: UniProtKB-KW
    6. neuron projection morphogenesis Source: UniProtKB
    7. podosome assembly Source: UniProtKB
    8. Rac protein signal transduction Source: UniProtKB
    9. synapse assembly Source: UniProtKB

    Keywords - Biological processi

    Adaptive immunity, Endocytosis, Immunity, Transport

    Keywords - Ligandi

    Actin-binding

    Enzyme and pathway databases

    ReactomeiREACT_13541. Caspase-mediated cleavage of cytoskeletal proteins.
    SignaLinkiQ9UJU6.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Drebrin-like protein
    Alternative name(s):
    Cervical SH3P7
    Cervical mucin-associated protein
    Drebrin-F
    HPK1-interacting protein of 55 kDa
    Short name:
    HIP-55
    SH3 domain-containing protein 7
    Gene namesi
    Name:DBNL
    Synonyms:CMAP, SH3P7
    ORF Names:PP5423
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 7

    Organism-specific databases

    HGNCiHGNC:2696. DBNL.

    Subcellular locationi

    Cytoplasmcytoskeleton. Cell projectionlamellipodium. Cell projectionruffle By similarity. Cytoplasmcell cortex By similarity. Cytoplasmcytosol By similarity. Cell junctionsynapse By similarity. Cell projection By similarity. Cell membrane By similarity; Peripheral membrane protein By similarity; Cytoplasmic side By similarity. Cytoplasmic vesicleclathrin-coated vesicle membrane By similarity; Peripheral membrane protein By similarity; Cytoplasmic side By similarity. Golgi apparatus membrane By similarity; Peripheral membrane protein By similarity; Cytoplasmic side By similarity. Cell projectionpodosome By similarity
    Note: Detected in neuron cell body and cell projections, such as neurites. Colocalizes with cytosolic dynamin in hippocampus neurons By similarity. Cortical actin cytoskeleton. Associates with lamellipodial actin and membrane ruffles. Colocalizes with actin and cortactin at podosome dots and podosome rosettes By similarity.By similarity

    GO - Cellular componenti

    1. cell cortex Source: UniProtKB
    2. cell junction Source: UniProtKB-KW
    3. clathrin-coated vesicle membrane Source: UniProtKB-SubCell
    4. cytoplasm Source: UniProtKB
    5. cytosol Source: Reactome
    6. dendrite Source: Ensembl
    7. extracellular vesicular exosome Source: UniProt
    8. Golgi membrane Source: UniProtKB-SubCell
    9. lamellipodium Source: UniProtKB
    10. plasma membrane Source: UniProtKB-SubCell
    11. podosome Source: UniProtKB
    12. postsynaptic density Source: Ensembl
    13. ruffle Source: UniProtKB

    Keywords - Cellular componenti

    Cell junction, Cell membrane, Cell projection, Cytoplasm, Cytoplasmic vesicle, Cytoskeleton, Golgi apparatus, Membrane, Synapse

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi361 – 3611D → A: Abolishes cleavage by caspase-3. 1 Publication

    Organism-specific databases

    PharmGKBiPA27164.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 430430Drebrin-like proteinPRO_0000079793Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei176 – 1761N6-acetyllysine1 Publication
    Modified residuei232 – 2321Phosphoserine6 Publications
    Modified residuei269 – 2691Phosphoserine3 Publications
    Modified residuei283 – 2831Phosphoserine2 Publications
    Modified residuei288 – 2881N6-acetyllysine1 Publication
    Modified residuei334 – 3341PhosphotyrosineBy similarity
    Modified residuei344 – 3441PhosphotyrosineBy similarity

    Post-translational modificationi

    Degraded by caspases during apoptosis.

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ9UJU6.
    PaxDbiQ9UJU6.
    PRIDEiQ9UJU6.

    2D gel databases

    OGPiQ9UJU6.

    PTM databases

    PhosphoSiteiQ9UJU6.

    Miscellaneous databases

    PMAP-CutDBQ9UJU6.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9UJU6.
    BgeeiQ9UJU6.
    CleanExiHS_DBNL.
    GenevestigatoriQ9UJU6.

    Organism-specific databases

    HPAiHPA020265.
    HPA027735.

    Interactioni

    Subunit structurei

    Interacts with SHANK2, SHANK3 and SYN1. Interacts with FGD1 and DNM1. Interacts with ANKRD54. Interacts with COBL. Interacts with WASL and WIPF1 By similarity. Interacts with MAP4K1 and PRAM1.By similarity2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    SH2D4AQ9H7883EBI-751783,EBI-747035
    SH3BP2P783147EBI-751783,EBI-727062

    Protein-protein interaction databases

    BioGridi118809. 43 interactions.
    IntActiQ9UJU6. 4 interactions.
    MINTiMINT-1474845.
    STRINGi9606.ENSP00000407950.

    Structurei

    Secondary structure

    1
    430
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi9 – 2012
    Beta strandi22 – 254
    Beta strandi27 – 3812
    Beta strandi40 – 489
    Helixi50 – 567
    Beta strandi61 – 7010
    Beta strandi72 – 743
    Beta strandi76 – 8510
    Helixi91 – 10717
    Turni108 – 1103
    Beta strandi111 – 1155
    Helixi120 – 1234
    Helixi125 – 1339

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1X67NMR-A1-133[»]
    ProteinModelPortaliQ9UJU6.
    SMRiQ9UJU6. Positions 1-133, 373-428.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9UJU6.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini4 – 133130ADF-HPROSITE-ProRule annotationAdd
    BLAST
    Domaini371 – 43060SH3PROSITE-ProRule annotationAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili176 – 23156Sequence AnalysisAdd
    BLAST

    Domaini

    The SH3 domain mediates interaction with SHANK2, SHANK3 and PRAM1.

    Sequence similaritiesi

    Belongs to the ABP1 family.Curated
    Contains 1 ADF-H domain.PROSITE-ProRule annotation
    Contains 1 SH3 domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil, SH3 domain

    Phylogenomic databases

    eggNOGiNOG265859.
    HOGENOMiHOG000008567.
    HOVERGENiHBG051316.
    OMAiFQDTGPQ.
    OrthoDBiEOG7X3QR9.
    PhylomeDBiQ9UJU6.
    TreeFamiTF318935.

    Family and domain databases

    Gene3Di3.40.20.10. 1 hit.
    InterProiIPR002108. ADF-H.
    IPR029006. ADF-H/Gelsolin-like_dom.
    IPR001452. SH3_domain.
    [Graphical view]
    PfamiPF00241. Cofilin_ADF. 1 hit.
    PF14604. SH3_9. 1 hit.
    [Graphical view]
    SMARTiSM00102. ADF. 1 hit.
    SM00326. SH3. 1 hit.
    [Graphical view]
    SUPFAMiSSF50044. SSF50044. 1 hit.
    PROSITEiPS51263. ADF_H. 1 hit.
    PS50002. SH3. 1 hit.
    [Graphical view]

    Sequences (5)i

    Sequence statusi: Complete.

    This entry describes 5 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9UJU6-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MAANLSRNGP ALQEAYVRVV TEKSPTDWAL FTYEGNSNDI RVAGTGEGGL    50
    EEMVEELNSG KVMYAFCRVK DPNSGLPKFV LINWTGEGVN DVRKGACASH 100
    VSTMASFLKG AHVTINARAE EDVEPECIME KVAKASGANY SFHKESGRFQ 150
    DVGPQAPVGS VYQKTNAVSE IKRVGKDSFW AKAEKEEENR RLEEKRRAEE 200
    AQRQLEQERR ERELREAARR EQRYQEQGGE ASPQRTWEQQ QEVVSRNRNE 250
    QESAVHPREI FKQKERAMST TSISSPQPGK LRSPFLQKQL TQPETHFGRE 300
    PAAAISRPRA DLPAEEPAPS TPPCLVQAEE EAVYEEPPEQ ETFYEQPPLV 350
    QQQGAGSEHI DHHIQGQGLS GQGLCARALY DYQAADDTEI SFDPENLITG 400
    IEVIDEGWWR GYGPDGHFGM FPANYVELIE 430
    Length:430
    Mass (Da):48,207
    Last modified:May 1, 2000 - v1
    Checksum:i7E8C42ED047257AE
    GO
    Isoform 2 (identifier: Q9UJU6-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         234-234: Q → QS

    Note: No experimental confirmation available.

    Show »
    Length:431
    Mass (Da):48,294
    Checksum:iD18F9D316FFD0B4E
    GO
    Isoform 3 (identifier: Q9UJU6-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         234-234: Q → QS
         251-251: Q → QGSTCASLQ

    Note: No experimental confirmation available.

    Show »
    Length:439
    Mass (Da):49,042
    Checksum:i8C044FBD0E82C6D5
    GO
    Isoform 4 (identifier: Q9UJU6-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-109: MAANLSRNGP...HVSTMASFLK → MKATAMTSAWLAQG
         234-234: Q → QS

    Show »
    Length:336
    Mass (Da):37,959
    Checksum:iCDDA7B4BDFAADB32
    GO
    Isoform 5 (identifier: Q9UJU6-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-103: Missing.

    Show »
    Length:327
    Mass (Da):37,101
    Checksum:iBE4C189EDD962834
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti8 – 81N → K in AAG17262. (PubMed:15498874)Curated
    Sequence conflicti98 – 981A → S in AAF81273. 1 PublicationCurated
    Sequence conflicti98 – 981A → S in AAG13120. 1 PublicationCurated
    Sequence conflicti235 – 2351R → S in AAF81273. 1 PublicationCurated
    Sequence conflicti235 – 2351R → S in AAG13120. 1 PublicationCurated
    Sequence conflicti430 – 4301E → D in CAG33448. 1 PublicationCurated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 109109MAANL…ASFLK → MKATAMTSAWLAQG in isoform 4. CuratedVSP_054779Add
    BLAST
    Alternative sequencei1 – 103103Missing in isoform 5. 1 PublicationVSP_054780Add
    BLAST
    Alternative sequencei234 – 2341Q → QS in isoform 2, isoform 3 and isoform 4. 2 PublicationsVSP_011398
    Alternative sequencei251 – 2511Q → QGSTCASLQ in isoform 3. 1 PublicationVSP_011399

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF197060 mRNA. Translation: AAF13701.1.
    AF077353 mRNA. Translation: AAF80228.1.
    AF250287 mRNA. Translation: AAF81273.1.
    AF151364 mRNA. Translation: AAG13120.1.
    AF218020 mRNA. Translation: AAG17262.2.
    AK027367 mRNA. Translation: BAB55065.1.
    AK293698 mRNA. Translation: BAG57133.1.
    CR457167 mRNA. Translation: CAG33448.1.
    AC017116 Genomic DNA. No translation available.
    CH236960 Genomic DNA. Translation: EAL23770.1.
    CH471128 Genomic DNA. Translation: EAW61132.1.
    BC011677 mRNA. Translation: AAH11677.1.
    BC031687 mRNA. Translation: AAH31687.1.
    CCDSiCCDS34622.1. [Q9UJU6-2]
    CCDS34623.1. [Q9UJU6-1]
    CCDS47579.1. [Q9UJU6-3]
    CCDS64633.1. [Q9UJU6-4]
    CCDS64634.1. [Q9UJU6-5]
    RefSeqiNP_001014436.1. NM_001014436.2. [Q9UJU6-1]
    NP_001116428.1. NM_001122956.1. [Q9UJU6-3]
    NP_001271242.1. NM_001284313.1. [Q9UJU6-5]
    NP_001271244.1. NM_001284315.1. [Q9UJU6-4]
    NP_054782.2. NM_014063.6. [Q9UJU6-2]
    UniGeneiHs.436500.

    Genome annotation databases

    EnsembliENST00000440166; ENSP00000415173; ENSG00000136279. [Q9UJU6-5]
    ENST00000448521; ENSP00000411701; ENSG00000136279. [Q9UJU6-1]
    ENST00000468694; ENSP00000417653; ENSG00000136279. [Q9UJU6-3]
    ENST00000490734; ENSP00000417749; ENSG00000136279. [Q9UJU6-4]
    ENST00000494774; ENSP00000419992; ENSG00000136279. [Q9UJU6-2]
    GeneIDi28988.
    KEGGihsa:28988.
    UCSCiuc003tjo.4. human. [Q9UJU6-2]
    uc003tjp.4. human. [Q9UJU6-1]
    uc003tjq.4. human. [Q9UJU6-3]

    Polymorphism databases

    DMDMi51316115.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF197060 mRNA. Translation: AAF13701.1 .
    AF077353 mRNA. Translation: AAF80228.1 .
    AF250287 mRNA. Translation: AAF81273.1 .
    AF151364 mRNA. Translation: AAG13120.1 .
    AF218020 mRNA. Translation: AAG17262.2 .
    AK027367 mRNA. Translation: BAB55065.1 .
    AK293698 mRNA. Translation: BAG57133.1 .
    CR457167 mRNA. Translation: CAG33448.1 .
    AC017116 Genomic DNA. No translation available.
    CH236960 Genomic DNA. Translation: EAL23770.1 .
    CH471128 Genomic DNA. Translation: EAW61132.1 .
    BC011677 mRNA. Translation: AAH11677.1 .
    BC031687 mRNA. Translation: AAH31687.1 .
    CCDSi CCDS34622.1. [Q9UJU6-2 ]
    CCDS34623.1. [Q9UJU6-1 ]
    CCDS47579.1. [Q9UJU6-3 ]
    CCDS64633.1. [Q9UJU6-4 ]
    CCDS64634.1. [Q9UJU6-5 ]
    RefSeqi NP_001014436.1. NM_001014436.2. [Q9UJU6-1 ]
    NP_001116428.1. NM_001122956.1. [Q9UJU6-3 ]
    NP_001271242.1. NM_001284313.1. [Q9UJU6-5 ]
    NP_001271244.1. NM_001284315.1. [Q9UJU6-4 ]
    NP_054782.2. NM_014063.6. [Q9UJU6-2 ]
    UniGenei Hs.436500.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1X67 NMR - A 1-133 [» ]
    ProteinModelPortali Q9UJU6.
    SMRi Q9UJU6. Positions 1-133, 373-428.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 118809. 43 interactions.
    IntActi Q9UJU6. 4 interactions.
    MINTi MINT-1474845.
    STRINGi 9606.ENSP00000407950.

    PTM databases

    PhosphoSitei Q9UJU6.

    Polymorphism databases

    DMDMi 51316115.

    2D gel databases

    OGPi Q9UJU6.

    Proteomic databases

    MaxQBi Q9UJU6.
    PaxDbi Q9UJU6.
    PRIDEi Q9UJU6.

    Protocols and materials databases

    DNASUi 28988.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000440166 ; ENSP00000415173 ; ENSG00000136279 . [Q9UJU6-5 ]
    ENST00000448521 ; ENSP00000411701 ; ENSG00000136279 . [Q9UJU6-1 ]
    ENST00000468694 ; ENSP00000417653 ; ENSG00000136279 . [Q9UJU6-3 ]
    ENST00000490734 ; ENSP00000417749 ; ENSG00000136279 . [Q9UJU6-4 ]
    ENST00000494774 ; ENSP00000419992 ; ENSG00000136279 . [Q9UJU6-2 ]
    GeneIDi 28988.
    KEGGi hsa:28988.
    UCSCi uc003tjo.4. human. [Q9UJU6-2 ]
    uc003tjp.4. human. [Q9UJU6-1 ]
    uc003tjq.4. human. [Q9UJU6-3 ]

    Organism-specific databases

    CTDi 28988.
    GeneCardsi GC07P044084.
    HGNCi HGNC:2696. DBNL.
    HPAi HPA020265.
    HPA027735.
    MIMi 610106. gene.
    neXtProti NX_Q9UJU6.
    PharmGKBi PA27164.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG265859.
    HOGENOMi HOG000008567.
    HOVERGENi HBG051316.
    OMAi FQDTGPQ.
    OrthoDBi EOG7X3QR9.
    PhylomeDBi Q9UJU6.
    TreeFami TF318935.

    Enzyme and pathway databases

    Reactomei REACT_13541. Caspase-mediated cleavage of cytoskeletal proteins.
    SignaLinki Q9UJU6.

    Miscellaneous databases

    ChiTaRSi DBNL. human.
    EvolutionaryTracei Q9UJU6.
    GeneWikii Drebrin-like.
    GenomeRNAii 28988.
    NextBioi 35471259.
    PMAP-CutDB Q9UJU6.
    PROi Q9UJU6.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9UJU6.
    Bgeei Q9UJU6.
    CleanExi HS_DBNL.
    Genevestigatori Q9UJU6.

    Family and domain databases

    Gene3Di 3.40.20.10. 1 hit.
    InterProi IPR002108. ADF-H.
    IPR029006. ADF-H/Gelsolin-like_dom.
    IPR001452. SH3_domain.
    [Graphical view ]
    Pfami PF00241. Cofilin_ADF. 1 hit.
    PF14604. SH3_9. 1 hit.
    [Graphical view ]
    SMARTi SM00102. ADF. 1 hit.
    SM00326. SH3. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50044. SSF50044. 1 hit.
    PROSITEi PS51263. ADF_H. 1 hit.
    PS50002. SH3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A novel src homology 3 domain-containing adaptor protein, HIP-55, that interacts with hematopoietic progenitor kinase 1."
      Ensenat D., Yao Z., Wang X.-S., Kori R., Zhou G., Lee S.C., Tan T.-H.
      J. Biol. Chem. 274:33945-33950(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH MAP4K1.
    2. "Molecular cloning of cDNA encoding drebrin F."
      Zhang W., Yuan Z., Wan T., He L., Cao X.
      Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    3. "Expression cloning of a novel cervical mucin-associated protein (CMAP)."
      Toribara N.W., Ho S.B., Wang R., Arthur M., Shekels L.L., Spurr-Michaud S., Keutmann H.T., Hill J.A., Gipson I.K.
      Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Cervix.
    4. "Large-scale cDNA transfection screening for genes related to cancer development and progression."
      Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X., Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X.
      , Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.
      Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    5. "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] (ISOFORMS 3 AND 5).
      Tissue: Cerebellum and Mammary gland.
    6. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    7. "Human chromosome 7: DNA sequence and biology."
      Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., Kanematsu E., Gentles S.
      , Christopoulos C.C., Choufani S., Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., Adams M.D., Tsui L.-C.
      Science 300:767-772(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    9. "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] (ISOFORMS 1 AND 2).
      Tissue: Brain and Eye.
    10. "SH3P7 is a cytoskeleton adapter protein and is coupled to signal transduction from lymphocyte antigen receptors."
      Larbolette O., Wollscheid B., Schweikert J., Nielsen P.J., Wienands J.
      Mol. Cell. Biol. 19:1539-1546(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION.
    11. "Caspase-mediated cleavage of actin-binding and SH3-domain-containing proteins cortactin, HS1, and HIP-55 during apoptosis."
      Chen Y.-R., Kori R., John B., Tan T.-H.
      Biochem. Biophys. Res. Commun. 288:981-989(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: DEGRADATION BY CASPASES.
    12. "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry."
      Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M., Peters E.C.
      Anal. Chem. 76:2763-2772(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-283, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    13. "Recruitment of the actin-binding protein HIP-55 to the immunological synapse regulates T cell receptor signaling and endocytosis."
      Le Bras S., Foucault I., Foussat A., Brignone C., Acuto O., Deckert M.
      J. Biol. Chem. 279:15550-15560(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    14. "PRAM-1 potentiates arsenic trioxide-induced JNK activation."
      Denis F.M., Benecke A., Di Gioia Y., Touw I.P., Cayre Y.E., Lutz P.G.
      J. Biol. Chem. 280:9043-9048(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PRAM1, CLEAVAGE BY CASPASES, MUTAGENESIS OF ASP-361.
    15. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-283, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    17. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
      Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
      Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-232, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    18. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-232, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Platelet.
    19. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-232 AND SER-269, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    20. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    21. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-232 AND SER-269, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    22. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-176 AND LYS-288, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    23. "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-232 AND SER-269, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    24. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    25. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-232, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    26. Cited for: STRUCTURE BY NMR OF 1-133.

    Entry informationi

    Entry nameiDBNL_HUMAN
    AccessioniPrimary (citable) accession number: Q9UJU6
    Secondary accession number(s): A4D2I9
    , B4DEM2, C9J7P1, P84070, Q6IAI8, Q96F30, Q96K74, Q9HBN8, Q9NR72
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 16, 2004
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 132 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 7
      Human chromosome 7: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3