Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q9UJU6

- DBNL_HUMAN

UniProt

Q9UJU6 - DBNL_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Drebrin-like protein

Gene

DBNL

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

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

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
Complete GO annotation...

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. cytoplasm Source: UniProtKB
  4. cytoplasmic vesicle Source: UniProtKB-KW
  5. cytosol Source: Reactome
  6. dendrite Source: Ensembl
  7. extracellular vesicular exosome Source: UniProt
  8. Golgi apparatus Source: UniProtKB-KW
  9. lamellipodium Source: UniProtKB
  10. plasma membrane Source: UniProtKB-KW
  11. podosome Source: UniProtKB
  12. postsynaptic density Source: Ensembl
  13. ruffle Source: UniProtKB
Complete GO annotation...

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

BgeeiQ9UJU6.
CleanExiHS_DBNL.
ExpressionAtlasiQ9UJU6. baseline and differential.
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. 49 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 – 2012Combined sources
Beta strandi22 – 254Combined sources
Beta strandi27 – 3812Combined sources
Beta strandi40 – 489Combined sources
Helixi50 – 567Combined sources
Beta strandi61 – 7010Combined sources
Beta strandi72 – 743Combined sources
Beta strandi76 – 8510Combined sources
Helixi91 – 10717Combined sources
Turni108 – 1103Combined sources
Beta strandi111 – 1155Combined sources
Helixi120 – 1234Combined sources
Helixi125 – 1339Combined sources

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.
GeneTreeiENSGT00530000062953.
HOGENOMiHOG000008567.
HOVERGENiHBG051316.
InParanoidiQ9UJU6.
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

        10         20         30         40         50
MAANLSRNGP ALQEAYVRVV TEKSPTDWAL FTYEGNSNDI RVAGTGEGGL
60 70 80 90 100
EEMVEELNSG KVMYAFCRVK DPNSGLPKFV LINWTGEGVN DVRKGACASH
110 120 130 140 150
VSTMASFLKG AHVTINARAE EDVEPECIME KVAKASGANY SFHKESGRFQ
160 170 180 190 200
DVGPQAPVGS VYQKTNAVSE IKRVGKDSFW AKAEKEEENR RLEEKRRAEE
210 220 230 240 250
AQRQLEQERR ERELREAARR EQRYQEQGGE ASPQRTWEQQ QEVVSRNRNE
260 270 280 290 300
QESAVHPREI FKQKERAMST TSISSPQPGK LRSPFLQKQL TQPETHFGRE
310 320 330 340 350
PAAAISRPRA DLPAEEPAPS TPPCLVQAEE EAVYEEPPEQ ETFYEQPPLV
360 370 380 390 400
QQQGAGSEHI DHHIQGQGLS GQGLCARALY DYQAADDTEI SFDPENLITG
410 420 430
IEVIDEGWWR GYGPDGHFGM FPANYVELIE
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. 49 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.
GeneTreei ENSGT00530000062953.
HOGENOMi HOG000008567.
HOVERGENi HBG051316.
InParanoidi Q9UJU6.
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

Bgeei Q9UJU6.
CleanExi HS_DBNL.
ExpressionAtlasi Q9UJU6. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 133 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