Q9UJU6 (DBNL_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	DBNL
Synonyms:	CMAP, SH3P7
ORF Names:	PP5423

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	430 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Actin-binding adapter protein. May act as a common effector of antigen receptor-signaling pathways in leukocytes. Its association with dynamin suggests that it may also connect the actin cytoskeleton to endocytic function. 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. Binds to F-actin but is not involved in actin polymerization, capping or bundling. Does not bind G-actin. Ref.12
Subunit structure	Interacts with SHANK2 and SHANK3 By similarity. Interacts with FGD1, dynamin, MAP4K1 and PRAM1. Ref.1 Ref.13
Subcellular location	Cytoplasm › cytoskeleton. Cell projection › lamellipodium. Note: Cortical cytoskeleton. Associates with lamellipodial actin.
Domain	The SH3 domain mediates interaction with SHANK2, SHANK3 and PRAM1.
Post-translational modification	Degraded by caspases during apoptosis.
Sequence similarities	Belongs to the ABP1 family. Contains 1 ADF-H domain. Contains 1 SH3 domain.

Ontologies

Keywords
Biological process	Adaptive immunity Endocytosis Immunity
Cellular component	Cell projection Cytoplasm Cytoskeleton
Coding sequence diversity	Alternative splicing
Domain	Coiled coil SH3 domain
Ligand	Actin-binding
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	Rac protein signal transduction Inferred from sequence or structural similarity. Source: UniProtKB activation of JUN kinase activity Traceable author statement. Source: ProtInc cellular component disassembly involved in apoptosis Traceable author statement. Source: Reactome endocytosis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cell cortex Inferred from sequence or structural similarity. Source: UniProtKB cytoskeleton Inferred from electronic annotation. Source: UniProtKB-SubCell cytosol Traceable author statement. Source: Reactome lamellipodium Inferred from sequence or structural similarity. Source: UniProtKB
Molecular function	actin binding Inferred from sequence or structural similarity. Source: UniProtKB enzyme activator activity Traceable author statement. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
SH2D4A	Q9H788	3	EBI-751783,EBI-747035

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9UJU6-1)

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.

Isoform 2 (identifier: Q9UJU6-2)

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

Note: No experimental confirmation available.

Isoform 3 (identifier: Q9UJU6-3)

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.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 430

430

Drebrin-like protein

PRO_0000079793

Regions

Domain

4 – 133

130

ADF-H

Domain

371 – 430

60

SH3

Coiled coil

176 – 231

56

Potential

Sites

Site

361 – 362

2

Cleavage; by caspase-3

Amino acid modifications

Modified residue

162

1

Phosphotyrosine Ref.14 Ref.15 Ref.18

Modified residue

176

1

N6-acetyllysine Ref.25

Modified residue

178

1

Phosphoserine Ref.20

Modified residue

232

1

Phosphoserine Ref.17 Ref.21 Ref.22 Ref.23 Ref.24

Modified residue

269

1

Phosphoserine Ref.20 Ref.22 Ref.23 Ref.24

Modified residue

270

1

Phosphothreonine Ref.23

Modified residue

272

1

Phosphoserine Ref.20

Modified residue

275

1

Phosphoserine Ref.20 Ref.21 Ref.23 Ref.24

Modified residue

283

1

Phosphoserine Ref.16 Ref.19 Ref.20 Ref.22

Modified residue

288

1

N6-acetyllysine Ref.25

Modified residue

291

1

Phosphothreonine Ref.20

Modified residue

334

1

Phosphotyrosine By similarity

Modified residue

344

1

Phosphotyrosine By similarity

Natural variations

Alternative sequence

234

1

Q → QS in isoform 2 and isoform 3.

VSP_011398

Alternative sequence

251

1

Q → QGSTCASLQ in isoform 3.

VSP_011399

Experimental info

Mutagenesis

361

1

D → A: Abolishes cleavage by caspase-3. Ref.13

Sequence conflict

8

1

N → K in AAG17262. Ref.4

Sequence conflict

98

1

A → S in AAF81273. Ref.3

Sequence conflict

98

1

A → S in AAG13120. Ref.3

Sequence conflict

235

1

R → S in AAF81273. Ref.3

Sequence conflict

235

1

R → S in AAG13120. Ref.3

Sequence conflict

430

1

E → D in CAG33448. Ref.6

Secondary structure

1

.

.

.

.

.

.

.

.

.

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.

.

.

.

.

.

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430

Helix Strand Turn

Details...

Helix

9 – 20

12

Beta strand

22 – 25

4

Beta strand

27 – 38

12

Beta strand

40 – 48

9

Helix

50 – 56

7

Beta strand

61 – 70

10

Beta strand

72 – 74

3

Beta strand

76 – 85

10

Helix

91 – 107

17

Turn

108 – 110

3

Beta strand

111 – 115

5

Helix

120 – 123

4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 7E8C42ED047257AE	FASTA	430	48,207
	10 20 30 40 50 60 MAANLSRNGP ALQEAYVRVV TEKSPTDWAL FTYEGNSNDI RVAGTGEGGL EEMVEELNSG 70 80 90 100 110 120 KVMYAFCRVK DPNSGLPKFV LINWTGEGVN DVRKGACASH VSTMASFLKG AHVTINARAE 130 140 150 160 170 180 EDVEPECIME KVAKASGANY SFHKESGRFQ DVGPQAPVGS VYQKTNAVSE IKRVGKDSFW 190 200 210 220 230 240 AKAEKEEENR RLEEKRRAEE AQRQLEQERR ERELREAARR EQRYQEQGGE ASPQRTWEQQ 250 260 270 280 290 300 QEVVSRNRNE QESAVHPREI FKQKERAMST TSISSPQPGK LRSPFLQKQL TQPETHFGRE 310 320 330 340 350 360 PAAAISRPRA DLPAEEPAPS TPPCLVQAEE EAVYEEPPEQ ETFYEQPPLV QQQGAGSEHI 370 380 390 400 410 420 DHHIQGQGLS GQGLCARALY DYQAADDTEI SFDPENLITG IEVIDEGWWR GYGPDGHFGM 430 FPANYVELIE
	Isoform 2 [UniParc]. Checksum: D18F9D316FFD0B4E	FASTA	431	48,294
	10 20 30 40 50 60 MAANLSRNGP ALQEAYVRVV TEKSPTDWAL FTYEGNSNDI RVAGTGEGGL EEMVEELNSG 70 80 90 100 110 120 KVMYAFCRVK DPNSGLPKFV LINWTGEGVN DVRKGACASH VSTMASFLKG AHVTINARAE 130 140 150 160 170 180 EDVEPECIME KVAKASGANY SFHKESGRFQ DVGPQAPVGS VYQKTNAVSE IKRVGKDSFW 190 200 210 220 230 240 AKAEKEEENR RLEEKRRAEE AQRQLEQERR ERELREAARR EQRYQEQGGE ASPQSRTWEQ 250 260 270 280 290 300 QQEVVSRNRN EQESAVHPRE IFKQKERAMS TTSISSPQPG KLRSPFLQKQ LTQPETHFGR 310 320 330 340 350 360 EPAAAISRPR ADLPAEEPAP STPPCLVQAE EEAVYEEPPE QETFYEQPPL VQQQGAGSEH 370 380 390 400 410 420 IDHHIQGQGL SGQGLCARAL YDYQAADDTE ISFDPENLIT GIEVIDEGWW RGYGPDGHFG 430 MFPANYVELI E
	Isoform 3 [UniParc]. Checksum: 8C044FBD0E82C6D5	FASTA	439	49,042
	10 20 30 40 50 60 MAANLSRNGP ALQEAYVRVV TEKSPTDWAL FTYEGNSNDI RVAGTGEGGL EEMVEELNSG 70 80 90 100 110 120 KVMYAFCRVK DPNSGLPKFV LINWTGEGVN DVRKGACASH VSTMASFLKG AHVTINARAE 130 140 150 160 170 180 EDVEPECIME KVAKASGANY SFHKESGRFQ DVGPQAPVGS VYQKTNAVSE IKRVGKDSFW 190 200 210 220 230 240 AKAEKEEENR RLEEKRRAEE AQRQLEQERR ERELREAARR EQRYQEQGGE ASPQSRTWEQ 250 260 270 280 290 300 QQEVVSRNRN EQGSTCASLQ ESAVHPREIF KQKERAMSTT SISSPQPGKL RSPFLQKQLT 310 320 330 340 350 360 QPETHFGREP AAAISRPRAD LPAEEPAPST PPCLVQAEEE AVYEEPPEQE TFYEQPPLVQ 370 380 390 400 410 420 QQGAGSEHID HHIQGQGLSG QGLCARALYD YQAADDTEIS FDPENLITGI EVIDEGWWRG 430 YGPDGHFGMF PANYVELIE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 10567356] [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: 15498874] [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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). Tissue: 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: 12690205] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases 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: 15489334] [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: 9891087] [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: 11689006] [Abstract] Cited for: DEGRADATION BY CASPASES.
[12]	"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: 14729663] [Abstract] Cited for: FUNCTION.
[13]	"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: 15637062] [Abstract] Cited for: INTERACTION WITH PRAM1, CLEAVAGE BY CASPASES, MUTAGENESIS OF ASP-361.
[14]	"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: 15592455] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-162, MASS SPECTROMETRY.
[15]	"Quantitative phosphoproteome analysis using a dendrimer conjugation chemistry and tandem mass spectrometry." Tao W.A., Wollscheid B., O'Brien R., Eng J.K., Li X.-J., Bodenmiller B., Watts J.D., Hood L., Aebersold R. Nat. Methods 2:591-598(2005) [PubMed: 16094384] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-162, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[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: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-283, MASS SPECTROMETRY. 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: 16964243] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-232, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[18]	"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer." Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M. , Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J. Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-162, MASS SPECTROMETRY. Tissue: Lung carcinoma.
[19]	"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra." Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D. J. Proteome Res. 6:4150-4162(2007) [PubMed: 17924679] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-283, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[20]	"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry." Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A. Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007) [PubMed: 17287340] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-178; SER-269; SER-272; SER-275; SER-283 AND THR-291, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[21]	"Phosphoproteome of resting human platelets." Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A. J. Proteome Res. 7:526-534(2008) [PubMed: 18088087] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-232 AND SER-275, MASS SPECTROMETRY. Tissue: Platelet.
[22]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-232; SER-269 AND SER-283, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[23]	"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: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-232; SER-269; THR-270 AND SER-275, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[24]	"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: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-232; SER-269 AND SER-275, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[25]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-176 AND LYS-288, MASS SPECTROMETRY.
[26]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[27]	"NMR solution structures of actin depolymerizing factor homology domains." Goroncy A.K., Koshiba S., Tochio N., Tomizawa T., Sato M., Inoue M., Watanabe S., Hayashizaki Y., Tanaka A., Kigawa T., Yokoyama S. Protein Sci. 18:2384-2392(2009) [PubMed: 19768801] [Abstract] Cited for: STRUCTURE BY NMR OF 1-133.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.
CR457167 mRNA. Translation: CAG33448.1.
CH236960 Genomic DNA. Translation: EAL23770.1.
CH471128 Genomic DNA. Translation: EAW61132.1.
BC011677 mRNA. Translation: AAH11677.1.
BC031687 mRNA. Translation: AAH31687.1.

IPI

IPI00101968.
IPI00396437.
IPI00456925.

RefSeq

NP_001014436.1. NM_001014436.2.
NP_001116428.1. NM_001122956.1.
NP_054782.2. NM_014063.6.

UniGene

Hs.436500.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1X67	NMR	-	A	1-133	[»]

ProteinModelPortal

Q9UJU6.

SMR

Q9UJU6. Positions 1-133, 373-428.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9UJU6. 1 interaction.

MINT

MINT-1474845.

STRING

Q9UJU6.

PTM databases

PhosphoSite

Q9UJU6.

Polymorphism databases

DMDM

51316115.

2D gel databases

OGP

Q9UJU6.

Proteomic databases

PRIDE

Q9UJU6.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000448521; ENSP00000411701; ENSG00000136279.
ENST00000452461; ENSP00000412539; ENSG00000136279.

GeneID

28988.

KEGG

hsa:28988.

UCSC

uc003tjo.2. human.
uc003tjp.2. human.
uc003tjq.2. human.

Organism-specific databases

CTD

28988.

GeneCards

GC07P044084.

HGNC

HGNC:2696. DBNL.

HPA

HPA020265.
HPA027735.

MIM

610106. gene.

neXtProt

NX_Q9UJU6.

PharmGKB

PA27164.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG20095.

GeneTree

ENSGT00530000062953.

HOVERGEN

HBG051316.

OMA

QRYQEQG.

Enzyme and pathway databases

Pathway_Interaction_DB

tcrjnkpathway. JNK signaling in the CD4+ TCR pathway.
tcrpathway. TCR signaling in naive CD4+ T cells.

Reactome

REACT_578. Apoptosis.

Gene expression databases

ArrayExpress

Q9UJU6.

Bgee

Q9UJU6.

CleanEx

HS_DBNL.

Genevestigator

Q9UJU6.

GermOnline

ENSG00000136279. Homo sapiens.

Family and domain databases

InterPro

IPR002108. Actin-bd_cofilin/tropomyosin.
IPR001452. SH3_domain.
[Graphical view]

Pfam

PF00241. Cofilin_ADF. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]

SMART

SM00102. ADF. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view]

SUPFAM

SSF50044. SH3. 1 hit.

PROSITE

PS51263. ADF_H. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

51899.

PMAP-CutDB

Q9UJU6.

SOURCE

Search...

Entry information

Entry name

DBNL_HUMAN

Accession

Primary (citable) accession number: Q9UJU6
Secondary accession number(s): A4D2I9 , P84070, Q6IAI8, Q96F30, Q96K74, Q9HBN8, Q9NR72

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 16, 2004
Last sequence update:	May 1, 2000
Last modified:	January 25, 2012
This is version 104 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.