Q05193 (DYN1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Dynamin-1
EC=3.6.5.5

Gene names

Name:	DNM1
Synonyms:	DNM

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	864 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Microtubule-associated force-producing protein involved in producing microtubule bundles and able to bind and hydrolyze GTP. Most probably involved in vesicular trafficking processes. Involved in receptor-mediated endocytosis.
Catalytic activity	GTP + H2O = GDP + phosphate.
Subunit structure	Interacts with CAV1 and SH3GLB1. Binds SH3GL1, SH3GL2 and SH3GL3 By similarity. Interacts with PHOCN By similarity. Interacts with SNX9. Interacts with MYO1E (via SH3 domain). Ref.4 Ref.6
Subcellular location	Cytoplasm. Cytoplasm › cytoskeleton. Note: Microtubule-associated. Ref.4
Sequence similarities	Belongs to the dynamin family. Contains 1 GED domain. Contains 1 PH domain.

Ontologies

Keywords
Biological process	Endocytosis
Cellular component	Cytoplasm Cytoskeleton Microtubule
Coding sequence diversity	Alternative splicing Polymorphism
Ligand	GTP-binding Nucleotide-binding
Molecular function	Hydrolase Motor protein
PTM	Nitration Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	endosome organization Inferred from mutant phenotype PubMed 19706678. Source: BHF-UCL receptor internalization Inferred from electronic annotation. Source: Compara receptor-mediated endocytosis Inferred from mutant phenotype PubMed 10521508. Source: UniProtKB
Cellular_component	membrane coat Inferred from electronic annotation. Source: Compara microtubule Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	GTP binding Inferred from electronic annotation. Source: UniProtKB-KW GTPase activity Traceable author statement PubMed 10944110. Source: ProtInc phospholipid binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		5	EBI-713135,EBI-713135
FNBP1	Q96RU3	5	EBI-713135,EBI-1111248
GRB2	P62993	3	EBI-713135,EBI-401755
NCK1	P16333	2	EBI-713135,EBI-389883

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q05193-1)

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: Q05193-2)

The sequence of this isoform differs from the canonical sequence as follows:
     407-444: MAFETIVKKQ...LISTVRQCTK → LAFEATVKKQ...LTATIRKCSE

Isoform 3 (identifier: Q05193-3)

The sequence of this isoform differs from the canonical sequence as follows:
     845-864: SRSGQASPSRPESPRPPFDL → RITISDP

Isoform 4 (identifier: Q05193-4)

The sequence of this isoform differs from the canonical sequence as follows:
     846-864: RSGQASPSRPESPRPPFDL → QPIGSGKSIPS

Isoform 5 (identifier: Q05193-5)

The sequence of this isoform differs from the canonical sequence as follows:
     407-444: MAFETIVKKQ...LISTVRQCTK → LAFEATVKKQ...LTATIRKCSE
     845-864: SRSGQASPSRPESPRPPFDL → RITISDP

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 864

864

Dynamin-1

PRO_0000206563

Regions

Domain

519 – 625

107

PH

Domain

659 – 750

92

GED

Nucleotide binding

38 – 45

8

GTP By similarity

Nucleotide binding

136 – 140

5

GTP By similarity

Nucleotide binding

205 – 208

4

GTP By similarity

Amino acid modifications

Modified residue

80

1

Phosphotyrosine By similarity

Modified residue

125

1

Nitrated tyrosine By similarity

Modified residue

125

1

Phosphotyrosine By similarity

Modified residue

347

1

Phosphoserine By similarity

Modified residue

354

1

Phosphotyrosine By similarity

Modified residue

512

1

Phosphoserine By similarity

Modified residue

778

1

Phosphoserine By similarity

Modified residue

822

1

Phosphoserine By similarity

Modified residue

851

1

Phosphoserine By similarity

Modified residue

857

1

Phosphoserine By similarity

Natural variations

Alternative sequence

407 – 444

38

MAFET…RQCTK → LAFEATVKKQVQKLKEPSIK CVDMVVSELTATIRKCSE in isoform 2 and isoform 5.

VSP_031518

Alternative sequence

845 – 864

20

SRSGQ…PPFDL → RITISDP in isoform 3 and isoform 5.

VSP_031519

Alternative sequence

846 – 864

19

RSGQA…PPFDL → QPIGSGKSIPS in isoform 4.

VSP_031520

Natural variant

744

1

D → N. Ref.1
Corresponds to variant rs1042007 [ dbSNP | Ensembl ].

VAR_048904

Experimental info

Mutagenesis

44

1

K → A: Inhibits receptor-mediated endocytosis. Ref.1

Sequence conflict

188

1

K → E in AAH50279. Ref.3

Sequence conflict

287

1

N → D in AAH50279. Ref.3

Sequence conflict

809

1

L → M in AAH50279. Ref.3

Secondary structure

1

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864

Helix Strand Turn

Details...

Helix

10 – 21

12

Turn

22 – 24

3

Helix

26 – 28

3

Beta strand

33 – 37

5

Helix

44 – 49

6

Turn

50 – 52

3

Beta strand

61 – 63

3

Beta strand

69 – 75

7

Beta strand

80 – 83

4

Helix

84 – 86

3

Helix

94 – 109

16

Turn

110 – 113

4

Beta strand

120 – 126

7

Beta strand

131 – 136

6

Helix

152 – 164

13

Beta strand

169 – 176

8

Helix

181 – 183

3

Helix

185 – 193

9

Beta strand

200 – 205

6

Helix

207 – 209

3

Helix

217 – 220

4

Beta strand

231 – 233

3

Helix

239 – 243

5

Helix

248 – 261

14

Turn

263 – 265

3

Helix

266 – 271

6

Helix

274 – 317

44

Beta strand

520 – 529

10

Helix

533 – 535

3

Beta strand

537 – 555

19

Beta strand

561 – 566

6

Beta strand

570 – 574

5

Beta strand

579 – 582

4

Beta strand

584 – 590

7

Beta strand

601 – 609

9

Helix

610 – 622

13

Helix

726 – 741

16

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified March 18, 2008. Version 2. Checksum: 7FCD8CB572FFEAEF	FASTA	864	97,408
	10 20 30 40 50 60 MGNRGMEDLI PLVNRLQDAF SAIGQNADLD LPQIAVVGGQ SAGKSSVLEN FVGRDFLPRG 70 80 90 100 110 120 SGIVTRRPLV LQLVNATTEY AEFLHCKGKK FTDFEEVRLE IEAETDRVTG TNKGISPVPI 130 140 150 160 170 180 NLRVYSPHVL NLTLVDLPGM TKVPVGDQPP DIEFQIRDML MQFVTKENCL ILAVSPANSD 190 200 210 220 230 240 LANSDALKVA KEVDPQGQRT IGVITKLDLM DEGTDARDVL ENKLLPLRRG YIGVVNRSQK 250 260 270 280 290 300 DIDGKKDITA ALAAERKFFL SHPSYRHLAD RMGTPYLQKV LNQQLTNHIR DTLPGLRNKL 310 320 330 340 350 360 QSQLLSIEKE VEEYKNFRPD DPARKTKALL QMVQQFAVDF EKRIEGSGDQ IDTYELSGGA 370 380 390 400 410 420 RINRIFHERF PFELVKMEFD EKELRREISY AIKNIHGIRT GLFTPDMAFE TIVKKQVKKI 430 440 450 460 470 480 REPCLKCVDM VISELISTVR QCTKKLQQYP RLREEMERIV TTHIREREGR TKEQVMLLID 490 500 510 520 530 540 IELAYMNTNH EDFIGFANAQ QRSNQMNKKK TSGNQDEILV IRKGWLTINN IGIMKGGSKE 550 560 570 580 590 600 YWFVLTAENL SWYKDDEEKE KKYMLSVDNL KLRDVEKGFM SSKHIFALFN TEQRNVYKDY 610 620 630 640 650 660 RQLELACETQ EEVDSWKASF LRAGVYPERV GDKEKASETE ENGSDSFMHS MDPQLERQVE 670 680 690 700 710 720 TIRNLVDSYM AIVNKTVRDL MPKTIMHLMI NNTKEFIFSE LLANLYSCGD QNTLMEESAE 730 740 750 760 770 780 QAQRRDEMLR MYHALKEALS IIGDINTTTV STPMPPPVDD SWLQVQSVPA GRRSPTSSPT 790 800 810 820 830 840 PQRRAPAVPP ARPGSRGPAP GPPPAGSALG GAPPVPSRPG ASPDPFGPPP QVPSRPNRAP 850 860 PGVPSRSGQA SPSRPESPRP PFDL
	Isoform 2 [UniParc]. Checksum: DC9E3D5259D891DF	FASTA	864	97,263
	10 20 30 40 50 60 MGNRGMEDLI PLVNRLQDAF SAIGQNADLD LPQIAVVGGQ SAGKSSVLEN FVGRDFLPRG 70 80 90 100 110 120 SGIVTRRPLV LQLVNATTEY AEFLHCKGKK FTDFEEVRLE IEAETDRVTG TNKGISPVPI 130 140 150 160 170 180 NLRVYSPHVL NLTLVDLPGM TKVPVGDQPP DIEFQIRDML MQFVTKENCL ILAVSPANSD 190 200 210 220 230 240 LANSDALKVA KEVDPQGQRT IGVITKLDLM DEGTDARDVL ENKLLPLRRG YIGVVNRSQK 250 260 270 280 290 300 DIDGKKDITA ALAAERKFFL SHPSYRHLAD RMGTPYLQKV LNQQLTNHIR DTLPGLRNKL 310 320 330 340 350 360 QSQLLSIEKE VEEYKNFRPD DPARKTKALL QMVQQFAVDF EKRIEGSGDQ IDTYELSGGA 370 380 390 400 410 420 RINRIFHERF PFELVKMEFD EKELRREISY AIKNIHGIRT GLFTPDLAFE ATVKKQVQKL 430 440 450 460 470 480 KEPSIKCVDM VVSELTATIR KCSEKLQQYP RLREEMERIV TTHIREREGR TKEQVMLLID 490 500 510 520 530 540 IELAYMNTNH EDFIGFANAQ QRSNQMNKKK TSGNQDEILV IRKGWLTINN IGIMKGGSKE 550 560 570 580 590 600 YWFVLTAENL SWYKDDEEKE KKYMLSVDNL KLRDVEKGFM SSKHIFALFN TEQRNVYKDY 610 620 630 640 650 660 RQLELACETQ EEVDSWKASF LRAGVYPERV GDKEKASETE ENGSDSFMHS MDPQLERQVE 670 680 690 700 710 720 TIRNLVDSYM AIVNKTVRDL MPKTIMHLMI NNTKEFIFSE LLANLYSCGD QNTLMEESAE 730 740 750 760 770 780 QAQRRDEMLR MYHALKEALS IIGDINTTTV STPMPPPVDD SWLQVQSVPA GRRSPTSSPT 790 800 810 820 830 840 PQRRAPAVPP ARPGSRGPAP GPPPAGSALG GAPPVPSRPG ASPDPFGPPP QVPSRPNRAP 850 860 PGVPSRSGQA SPSRPESPRP PFDL
	Isoform 3 [UniParc]. Checksum: 89040FCDDAC2870C	FASTA	851	96,041
	10 20 30 40 50 60 MGNRGMEDLI PLVNRLQDAF SAIGQNADLD LPQIAVVGGQ SAGKSSVLEN FVGRDFLPRG 70 80 90 100 110 120 SGIVTRRPLV LQLVNATTEY AEFLHCKGKK FTDFEEVRLE IEAETDRVTG TNKGISPVPI 130 140 150 160 170 180 NLRVYSPHVL NLTLVDLPGM TKVPVGDQPP DIEFQIRDML MQFVTKENCL ILAVSPANSD 190 200 210 220 230 240 LANSDALKVA KEVDPQGQRT IGVITKLDLM DEGTDARDVL ENKLLPLRRG YIGVVNRSQK 250 260 270 280 290 300 DIDGKKDITA ALAAERKFFL SHPSYRHLAD RMGTPYLQKV LNQQLTNHIR DTLPGLRNKL 310 320 330 340 350 360 QSQLLSIEKE VEEYKNFRPD DPARKTKALL QMVQQFAVDF EKRIEGSGDQ IDTYELSGGA 370 380 390 400 410 420 RINRIFHERF PFELVKMEFD EKELRREISY AIKNIHGIRT GLFTPDMAFE TIVKKQVKKI 430 440 450 460 470 480 REPCLKCVDM VISELISTVR QCTKKLQQYP RLREEMERIV TTHIREREGR TKEQVMLLID 490 500 510 520 530 540 IELAYMNTNH EDFIGFANAQ QRSNQMNKKK TSGNQDEILV IRKGWLTINN IGIMKGGSKE 550 560 570 580 590 600 YWFVLTAENL SWYKDDEEKE KKYMLSVDNL KLRDVEKGFM SSKHIFALFN TEQRNVYKDY 610 620 630 640 650 660 RQLELACETQ EEVDSWKASF LRAGVYPERV GDKEKASETE ENGSDSFMHS MDPQLERQVE 670 680 690 700 710 720 TIRNLVDSYM AIVNKTVRDL MPKTIMHLMI NNTKEFIFSE LLANLYSCGD QNTLMEESAE 730 740 750 760 770 780 QAQRRDEMLR MYHALKEALS IIGDINTTTV STPMPPPVDD SWLQVQSVPA GRRSPTSSPT 790 800 810 820 830 840 PQRRAPAVPP ARPGSRGPAP GPPPAGSALG GAPPVPSRPG ASPDPFGPPP QVPSRPNRAP 850 PGVPRITISD P
	Isoform 4 [UniParc]. Checksum: 7FF33D80ED860B02	FASTA	856	96,397
	10 20 30 40 50 60 MGNRGMEDLI PLVNRLQDAF SAIGQNADLD LPQIAVVGGQ SAGKSSVLEN FVGRDFLPRG 70 80 90 100 110 120 SGIVTRRPLV LQLVNATTEY AEFLHCKGKK FTDFEEVRLE IEAETDRVTG TNKGISPVPI 130 140 150 160 170 180 NLRVYSPHVL NLTLVDLPGM TKVPVGDQPP DIEFQIRDML MQFVTKENCL ILAVSPANSD 190 200 210 220 230 240 LANSDALKVA KEVDPQGQRT IGVITKLDLM DEGTDARDVL ENKLLPLRRG YIGVVNRSQK 250 260 270 280 290 300 DIDGKKDITA ALAAERKFFL SHPSYRHLAD RMGTPYLQKV LNQQLTNHIR DTLPGLRNKL 310 320 330 340 350 360 QSQLLSIEKE VEEYKNFRPD DPARKTKALL QMVQQFAVDF EKRIEGSGDQ IDTYELSGGA 370 380 390 400 410 420 RINRIFHERF PFELVKMEFD EKELRREISY AIKNIHGIRT GLFTPDMAFE TIVKKQVKKI 430 440 450 460 470 480 REPCLKCVDM VISELISTVR QCTKKLQQYP RLREEMERIV TTHIREREGR TKEQVMLLID 490 500 510 520 530 540 IELAYMNTNH EDFIGFANAQ QRSNQMNKKK TSGNQDEILV IRKGWLTINN IGIMKGGSKE 550 560 570 580 590 600 YWFVLTAENL SWYKDDEEKE KKYMLSVDNL KLRDVEKGFM SSKHIFALFN TEQRNVYKDY 610 620 630 640 650 660 RQLELACETQ EEVDSWKASF LRAGVYPERV GDKEKASETE ENGSDSFMHS MDPQLERQVE 670 680 690 700 710 720 TIRNLVDSYM AIVNKTVRDL MPKTIMHLMI NNTKEFIFSE LLANLYSCGD QNTLMEESAE 730 740 750 760 770 780 QAQRRDEMLR MYHALKEALS IIGDINTTTV STPMPPPVDD SWLQVQSVPA GRRSPTSSPT 790 800 810 820 830 840 PQRRAPAVPP ARPGSRGPAP GPPPAGSALG GAPPVPSRPG ASPDPFGPPP QVPSRPNRAP 850 PGVPSQPIGS GKSIPS
	Isoform 5 [UniParc]. Checksum: 4230B9970D097B20	FASTA	851	95,895
	10 20 30 40 50 60 MGNRGMEDLI PLVNRLQDAF SAIGQNADLD LPQIAVVGGQ SAGKSSVLEN FVGRDFLPRG 70 80 90 100 110 120 SGIVTRRPLV LQLVNATTEY AEFLHCKGKK FTDFEEVRLE IEAETDRVTG TNKGISPVPI 130 140 150 160 170 180 NLRVYSPHVL NLTLVDLPGM TKVPVGDQPP DIEFQIRDML MQFVTKENCL ILAVSPANSD 190 200 210 220 230 240 LANSDALKVA KEVDPQGQRT IGVITKLDLM DEGTDARDVL ENKLLPLRRG YIGVVNRSQK 250 260 270 280 290 300 DIDGKKDITA ALAAERKFFL SHPSYRHLAD RMGTPYLQKV LNQQLTNHIR DTLPGLRNKL 310 320 330 340 350 360 QSQLLSIEKE VEEYKNFRPD DPARKTKALL QMVQQFAVDF EKRIEGSGDQ IDTYELSGGA 370 380 390 400 410 420 RINRIFHERF PFELVKMEFD EKELRREISY AIKNIHGIRT GLFTPDLAFE ATVKKQVQKL 430 440 450 460 470 480 KEPSIKCVDM VVSELTATIR KCSEKLQQYP RLREEMERIV TTHIREREGR TKEQVMLLID 490 500 510 520 530 540 IELAYMNTNH EDFIGFANAQ QRSNQMNKKK TSGNQDEILV IRKGWLTINN IGIMKGGSKE 550 560 570 580 590 600 YWFVLTAENL SWYKDDEEKE KKYMLSVDNL KLRDVEKGFM SSKHIFALFN TEQRNVYKDY 610 620 630 640 650 660 RQLELACETQ EEVDSWKASF LRAGVYPERV GDKEKASETE ENGSDSFMHS MDPQLERQVE 670 680 690 700 710 720 TIRNLVDSYM AIVNKTVRDL MPKTIMHLMI NNTKEFIFSE LLANLYSCGD QNTLMEESAE 730 740 750 760 770 780 QAQRRDEMLR MYHALKEALS IIGDINTTTV STPMPPPVDD SWLQVQSVPA GRRSPTSSPT 790 800 810 820 830 840 PQRRAPAVPP ARPGSRGPAP GPPPAGSALG GAPPVPSRPG ASPDPFGPPP QVPSRPNRAP 850 PGVPRITISD P

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Mutations in human dynamin block an intermediate stage in coated vesicle formation." van der Bliek A.M., Redelmeier T.E., Tisdale E.J., Meyerowitz E.M., Schmid S.L. J. Cell Biol. 122:553-563(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE [MRNA] OF 387-466 (ISOFORM 2), NUCLEOTIDE SEQUENCE [MRNA] OF 726-856 (ISOFORMS 3 AND 4), MUTAGENESIS OF LYS-44, VARIANT ASN-744.
[2]	"DNA sequence and analysis of human chromosome 9." Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L. , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I. Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	"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] (ISOFORM 3). Tissue: Brain and PNS.
[4]	"SNX9 regulates dynamin assembly and is required for efficient clathrin-mediated endocytosis." Soulet F., Yarar D., Leonard M., Schmid S.L. Mol. Biol. Cell 16:2058-2067(2005) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, INTERACTION WITH SNX9.
[5]	"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[6]	"Myosin 1E interacts with synaptojanin-1 and dynamin and is involved in endocytosis." Krendel M., Osterweil E.K., Mooseker M.S. FEBS Lett. 581:644-650(2007) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH MYO1E.
[7]	"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] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Platelet.
[8]	"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] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[9]	"Three-dimensional solution structure of the pleckstrin homology domain from dynamin." Downing A.K., Driscoll P.C., Gout I., Salim K., Zvelebil M.J., Waterfield M.D. Curr. Biol. 4:884-891(1994) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 511-630.
[10]	"Crystal structure at 2.2-A resolution of the pleckstrin homology domain from human dynamin." Ferguson K.M., Lemmon M.A., Schlessinger J., Sigler P.B. Cell 79:199-209(1994) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 509-633.
[11]	"Crystal structure of the pleckstrin homology domain from dynamin." Timm D., Salim K., Gout I., Guruprasad L., Waterfield M., Blundell T. Nat. Struct. Biol. 1:782-788(1994) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 509-630.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

L07807 mRNA. Translation: AAA02803.1.
L07808 mRNA. Translation: AAA02804.1.
L07809 mRNA. Translation: AAA02805.1.
L07810 mRNA. Translation: AAA02806.1.
AL590708 Genomic DNA. Translation: CAI13837.1.
AL590708 Genomic DNA. Translation: CAI13839.2.
BC050279 mRNA. Translation: AAH50279.2.
BC063850 mRNA. Translation: AAH63850.1.

IPI

IPI00413140.
IPI00657691.
IPI00816287.
IPI00887273.
IPI00888758.

PIR

A40671.

RefSeq

NP_001005336.1. NM_001005336.1.
NP_004399.2. NM_004408.2.

UniGene

Hs.522413.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1DYN	X-ray	2.20	A/B	510-633	[»]
2DYN	X-ray	2.30	A/B	509-630	[»]
2X2E	X-ray	2.00	A/D	6-750	[»]
2X2F	X-ray	2.00	A/D	6-750	[»]
3SNH	X-ray	3.70	A	6-746	[»]
3ZYC	X-ray	2.20	A/D	6-750	[»]
3ZYS	electron microscopy	12.20	A/D	6-750	[»]
			C/F	518-630	[»]

ProteinModelPortal

Q05193.

ModBase

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Protein-protein interaction databases

DIP

DIP-36242N.

IntAct

Q05193. 15 interactions.

MINT

MINT-233135.

STRING

9606.ENSP00000362014.

PTM databases

PhosphoSite

Q05193.

Polymorphism databases

DMDM

172046078.

Proteomic databases

PaxDb

Q05193.

PRIDE

Q05193.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000341179; ENSP00000345680; ENSG00000106976.
ENST00000372923; ENSP00000362014; ENSG00000106976.
ENST00000393594; ENSP00000377219; ENSG00000106976.
ENST00000475805; ENSP00000419225; ENSG00000106976.
ENST00000486160; ENSP00000420045; ENSG00000106976.

GeneID

1759.

KEGG

hsa:1759.

UCSC

uc022bnx.1. human.
uc022bny.1. human.
uc022boa.1. human.

Organism-specific databases

CTD

1759.

GeneCards

GC09P130965.

H-InvDB

HIX0026786.
HIX0211497.

HGNC

HGNC:2972. DNM1.

HPA

CAB005920.
HPA049910.

MIM

602377. gene.

neXtProt

NX_Q05193.

PharmGKB

PA27440.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0699.

HOGENOM

HOG000161069.

HOVERGEN

HBG107833.

KO

K01528.

OMA

QYPHLRE.

PhylomeDB

Q05193.

Enzyme and pathway databases

Pathway_Interaction_DB

ephbfwdpathway. EPHB forward signaling.
ephrinbrevpathway. Ephrin B reverse signaling.
trkrpathway. Neurotrophic factor-mediated Trk receptor signaling.
txa2pathway. Thromboxane A2 receptor signaling.

Reactome

REACT_111045. Developmental Biology.
REACT_111102. Signal Transduction.
REACT_11123. Membrane Trafficking.
REACT_6900. Immune System.

Gene expression databases

ArrayExpress

Q05193.

Bgee

Q05193.

CleanEx

HS_DNM1.

Genevestigator

Q05193.

GermOnline

ENSG00000106976. Homo sapiens.

Family and domain databases

Gene3D

2.30.29.30. 1 hit.

InterPro

IPR022812. Dynamin.
IPR000375. Dynamin_central.
IPR001401. Dynamin_GTPase.
IPR019762. Dynamin_GTPase_CS.
IPR003130. GED.
IPR020850. GTPase_effector_domain_GED.
IPR011993. PH_like_dom.
IPR001849. Pleckstrin_homology.
[Graphical view]

PANTHER

PTHR11566. PTHR11566. 1 hit.

Pfam

PF01031. Dynamin_M. 1 hit.
PF00350. Dynamin_N. 1 hit.
PF02212. GED. 1 hit.
PF00169. PH. 1 hit.
[Graphical view]

PRINTS

PR00195. DYNAMIN.

SMART

SM00053. DYNc. 1 hit.
SM00302. GED. 1 hit.
SM00233. PH. 1 hit.
[Graphical view]

PROSITE

PS00410. DYNAMIN. 1 hit.
PS51388. GED. 1 hit.
PS50003. PH_DOMAIN. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

Q05193.

ChEMBL

CHEMBL4958.

ChiTaRS

DNM1. human.

EvolutionaryTrace

Q05193.

GenomeRNAi

1759.

NextBio

7163.

SOURCE

Search...

Entry information

Entry name

DYN1_HUMAN

Accession

Primary (citable) accession number: Q05193
Secondary accession number(s): A6NLM6 , Q5SYX0, Q5SYX2, Q6P3T6, Q86VD2

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1994
Last sequence update:	March 18, 2008
Last modified:	May 1, 2013
This is version 127 of the entry and version 2 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.