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Protein

Dynein heavy chain, cytoplasmic

Gene

DYN1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Cytoplasmic dynein acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. Dynein has ATPase activity; the force-producing power stroke is thought to occur on release of ADP. Required to maintain uniform nuclear distribution in hyphae. May play an important role in the proper orientation of the mitotic spindle into the budding daughter cell yeast. Probably required for normal progression of the cell cycle.1 Publication

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi1796 – 1803ATPSequence analysis8
Nucleotide bindingi2074 – 2081ATPSequence analysis8
Nucleotide bindingi2418 – 2425ATPSequence analysis8
Nucleotide bindingi2760 – 2767ATPSequence analysis8

GO - Molecular functioni

  • ATP binding Source: SGD
  • ATP-dependent microtubule motor activity, minus-end-directed Source: SGD
  • microtubule motor activity Source: SGD
  • minus-end directed microfilament motor activity Source: SGD

GO - Biological processi

  • establishment of mitotic spindle localization Source: SGD
  • establishment of mitotic spindle orientation Source: SGD
  • karyogamy Source: UniProtKB-KW
  • mitotic sister chromatid segregation Source: SGD
  • nuclear migration along microtubule Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Motor protein

Keywords - Biological processi

Karyogamy

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-32023-MONOMER.
ReactomeiR-SCE-6798695. Neutrophil degranulation.

Names & Taxonomyi

Protein namesi
Recommended name:
Dynein heavy chain, cytoplasmic
Alternative name(s):
Dynein heavy chain, cytosolic
Short name:
DYHC
Gene namesi
Name:DYN1
Synonyms:DHC1
Ordered Locus Names:YKR054C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XI

Organism-specific databases

EuPathDBiFungiDB:YKR054C.
SGDiS000001762. DYN1.

Subcellular locationi

GO - Cellular componenti

  • astral microtubule Source: SGD
  • cell cortex Source: SGD
  • cytoplasmic dynein complex Source: SGD
  • cytoplasmic microtubule Source: SGD
  • spindle pole body Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Dynein, Microtubule

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001146431 – 4092Dynein heavy chain, cytoplasmicAdd BLAST4092

Proteomic databases

MaxQBiP36022.
PRIDEiP36022.

PTM databases

iPTMnetiP36022.

Interactioni

Subunit structurei

The dynein complex consists of at least two heavy chains and a number of intermediate and light chains. Interacts with DYN3.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
SMC1P329083EBI-6230,EBI-17402

Protein-protein interaction databases

BioGridi34185. 232 interactors.
DIPiDIP-2644N.
IntActiP36022. 9 interactors.
MINTiMINT-427451.

Structurei

Secondary structure

14092
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi1366 – 1378Combined sources13
Beta strandi1384 – 1387Combined sources4
Beta strandi1389 – 1391Combined sources3
Beta strandi1393 – 1396Combined sources4
Helixi1399 – 1414Combined sources16
Turni1420 – 1424Combined sources5
Helixi1425 – 1458Combined sources34
Helixi1464 – 1468Combined sources5
Helixi1470 – 1491Combined sources22
Helixi1497 – 1501Combined sources5
Helixi1505 – 1533Combined sources29
Helixi1537 – 1540Combined sources4
Helixi1542 – 1550Combined sources9
Turni1551 – 1554Combined sources4
Helixi1556 – 1558Combined sources3
Helixi1559 – 1565Combined sources7
Beta strandi1567 – 1574Combined sources8
Beta strandi1576 – 1584Combined sources9
Beta strandi1589 – 1597Combined sources9
Helixi1604 – 1631Combined sources28
Helixi1636 – 1640Combined sources5
Helixi1645 – 1666Combined sources22
Helixi1669 – 1688Combined sources20
Helixi1692 – 1717Combined sources26
Helixi1721 – 1730Combined sources10
Beta strandi1733 – 1736Combined sources4
Helixi1743 – 1745Combined sources3
Beta strandi1747 – 1751Combined sources5
Beta strandi1754 – 1757Combined sources4
Helixi1773 – 1787Combined sources15
Beta strandi1791 – 1795Combined sources5
Helixi1802 – 1811Combined sources10
Turni1812 – 1814Combined sources3
Beta strandi1818 – 1821Combined sources4
Helixi1828 – 1841Combined sources14
Beta strandi1844 – 1849Combined sources6
Helixi1855 – 1874Combined sources20
Beta strandi1877 – 1880Combined sources4
Beta strandi1882 – 1887Combined sources6
Beta strandi1893 – 1898Combined sources6
Beta strandi1902 – 1905Combined sources4
Helixi1910 – 1913Combined sources4
Beta strandi1916 – 1920Combined sources5
Helixi1926 – 1938Combined sources13
Helixi1942 – 1959Combined sources18
Helixi1970 – 1986Combined sources17
Helixi1991 – 2001Combined sources11
Helixi2003 – 2005Combined sources3
Helixi2008 – 2021Combined sources14
Beta strandi2029 – 2032Combined sources4
Helixi2033 – 2045Combined sources13
Helixi2051 – 2066Combined sources16
Beta strandi2068 – 2073Combined sources6
Helixi2080 – 2094Combined sources15
Beta strandi2098 – 2104Combined sources7
Turni2106 – 2108Combined sources3
Helixi2111 – 2114Combined sources4
Turni2120 – 2122Combined sources3
Helixi2130 – 2138Combined sources9
Beta strandi2146 – 2154Combined sources9
Helixi2160 – 2164Combined sources5
Helixi2167 – 2170Combined sources4
Beta strandi2175 – 2177Combined sources3
Beta strandi2179 – 2181Combined sources3
Beta strandi2183 – 2185Combined sources3
Beta strandi2188 – 2197Combined sources10
Helixi2204 – 2209Combined sources6
Beta strandi2210 – 2214Combined sources5
Helixi2222 – 2238Combined sources17
Helixi2243 – 2256Combined sources14
Helixi2259 – 2270Combined sources12
Helixi2280 – 2297Combined sources18
Helixi2300 – 2302Combined sources3
Beta strandi2303 – 2305Combined sources3
Helixi2307 – 2327Combined sources21
Helixi2333 – 2345Combined sources13
Beta strandi2348 – 2350Combined sources3
Beta strandi2363 – 2365Combined sources3
Helixi2383 – 2385Combined sources3
Helixi2395 – 2410Combined sources16
Beta strandi2413 – 2417Combined sources5
Helixi2424 – 2433Combined sources10
Beta strandi2439 – 2444Combined sources6
Helixi2451 – 2461Combined sources11
Beta strandi2465 – 2467Combined sources3
Turni2468 – 2470Combined sources3
Beta strandi2471 – 2480Combined sources10
Beta strandi2482 – 2487Combined sources6
Turni2488 – 2490Combined sources3
Beta strandi2496 – 2498Combined sources3
Helixi2501 – 2511Combined sources11
Beta strandi2513 – 2516Combined sources4
Turni2518 – 2520Combined sources3
Beta strandi2523 – 2535Combined sources13
Helixi2548 – 2551Combined sources4
Beta strandi2554 – 2558Combined sources5
Turni2563 – 2565Combined sources3
Helixi2566 – 2578Combined sources13
Helixi2583 – 2588Combined sources6
Helixi2589 – 2606Combined sources18
Turni2609 – 2611Combined sources3
Helixi2619 – 2634Combined sources16
Helixi2641 – 2656Combined sources16
Turni2657 – 2659Combined sources3
Helixi2664 – 2680Combined sources17
Turni2691 – 2693Combined sources3
Beta strandi2696 – 2703Combined sources8
Helixi2709 – 2726Combined sources18
Helixi2736 – 2750Combined sources15
Beta strandi2751 – 2759Combined sources9
Turni2761 – 2763Combined sources3
Helixi2766 – 2776Combined sources11
Beta strandi2780 – 2782Combined sources3
Helixi2792 – 2808Combined sources17
Beta strandi2813 – 2818Combined sources6
Turni2819 – 2821Combined sources3
Helixi2825 – 2836Combined sources12
Beta strandi2837 – 2839Combined sources3
Turni2841 – 2843Combined sources3
Helixi2847 – 2863Combined sources17
Helixi2870 – 2884Combined sources15
Beta strandi2886 – 2892Combined sources7
Helixi2897 – 2904Combined sources8
Helixi2906 – 2911Combined sources6
Beta strandi2912 – 2916Combined sources5
Helixi2922 – 2932Combined sources11
Helixi2961 – 2979Combined sources19
Beta strandi2983 – 2985Combined sources3
Helixi2991 – 3027Combined sources37
Helixi3300 – 3304Combined sources5
Turni3305 – 3307Combined sources3
Helixi3308 – 3333Combined sources26
Turni3334 – 3336Combined sources3
Helixi3339 – 3355Combined sources17
Helixi3366 – 3370Combined sources5
Helixi3373 – 3382Combined sources10
Helixi3388 – 3399Combined sources12
Beta strandi3402 – 3408Combined sources7
Helixi3414 – 3422Combined sources9
Helixi3423 – 3425Combined sources3
Beta strandi3426 – 3429Combined sources4
Helixi3436 – 3445Combined sources10
Beta strandi3449 – 3453Combined sources5
Beta strandi3455 – 3457Combined sources3
Helixi3463 – 3466Combined sources4
Beta strandi3477 – 3480Combined sources4
Beta strandi3482 – 3487Combined sources6
Beta strandi3493 – 3498Combined sources6
Helixi3507 – 3512Combined sources6
Beta strandi3513 – 3517Combined sources5
Helixi3523 – 3537Combined sources15
Helixi3539 – 3572Combined sources34
Beta strandi3573 – 3576Combined sources4
Helixi3580 – 3638Combined sources59
Helixi3646 – 3655Combined sources10
Helixi3670 – 3686Combined sources17
Helixi3692 – 3710Combined sources19
Helixi3713 – 3726Combined sources14
Beta strandi3727 – 3729Combined sources3
Turni3738 – 3740Combined sources3
Helixi3743 – 3752Combined sources10
Helixi3756 – 3765Combined sources10
Helixi3774 – 3780Combined sources7
Beta strandi3784 – 3790Combined sources7
Helixi3797 – 3805Combined sources9
Turni3806 – 3808Combined sources3
Beta strandi3813 – 3815Combined sources3
Helixi3819 – 3835Combined sources17
Beta strandi3839 – 3842Combined sources4
Helixi3844 – 3847Combined sources4
Helixi3848 – 3853Combined sources6
Helixi3855 – 3861Combined sources7
Turni3865 – 3867Combined sources3
Beta strandi3868 – 3870Combined sources3
Beta strandi3873 – 3876Combined sources4
Beta strandi3879 – 3881Combined sources3
Helixi3886 – 3891Combined sources6
Beta strandi3892 – 3897Combined sources6
Helixi3903 – 3913Combined sources11
Helixi3914 – 3917Combined sources4
Helixi3923 – 3944Combined sources22
Turni3946 – 3949Combined sources4
Beta strandi3950 – 3952Combined sources3
Helixi3958 – 3974Combined sources17
Helixi3980 – 3982Combined sources3
Helixi3983 – 3991Combined sources9
Turni3995 – 3997Combined sources3
Helixi4001 – 4014Combined sources14
Beta strandi4018 – 4020Combined sources3
Beta strandi4023 – 4026Combined sources4
Helixi4038 – 4051Combined sources14
Helixi4058 – 4061Combined sources4
Beta strandi4063 – 4065Combined sources3
Helixi4067 – 4090Combined sources24

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3J67electron microscopy34.00A1554-4092[»]
3J68electron microscopy30.00A1554-4092[»]
3QMZX-ray6.00A/B1364-4092[»]
4AI6X-ray3.40A/B1364-4092[»]
4AKGX-ray3.30A/B1364-4092[»]
4AKHX-ray3.60A/B1364-4092[»]
4AKIX-ray3.70A/B1364-4092[»]
4W8FX-ray3.54A/B1364-3038[»]
A/B3292-4092[»]
5AFRX-ray5.00A/B1-557[»]
ProteinModelPortaliP36022.
SMRiP36022.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 1757StemBy similarityAdd BLAST1757
Regioni1758 – 1979AAA 1By similarityAdd BLAST222
Regioni2036 – 2273AAA 2By similarityAdd BLAST238
Regioni2379 – 2628AAA 3By similarityAdd BLAST250
Regioni2722 – 2984AAA 4By similarityAdd BLAST263
Regioni2993 – 3300StalkBy similarityAdd BLAST308
Regioni3370 – 3599AAA 5By similarityAdd BLAST230
Regioni3760 – 3970AAA 6By similarityAdd BLAST211

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili154 – 175Sequence analysisAdd BLAST22
Coiled coili486 – 508Sequence analysisAdd BLAST23
Coiled coili542 – 566Sequence analysisAdd BLAST25
Coiled coili932 – 959Sequence analysisAdd BLAST28
Coiled coili1042 – 1063Sequence analysisAdd BLAST22
Coiled coili1681 – 1705Sequence analysisAdd BLAST25
Coiled coili2993 – 3092Sequence analysisAdd BLAST100
Coiled coili3242 – 3300Sequence analysisAdd BLAST59
Coiled coili3532 – 3608Sequence analysisAdd BLAST77

Domaini

Dynein heavy chains probably consist of an N-terminal stem (which binds cargo and interacts with other dynein components), and the head or motor domain. The motor contains six tandemly-linked AAA domains in the head, which form a ring. A stalk-like structure (formed by two of the coiled coil domains) protrudes between AAA 4 and AAA 5 and terminates in a microtubule-binding site. A seventh domain may also contribute to this ring; it is not clear whether the N-terminus or the C-terminus forms this extra domain. There are four well-conserved and two non-conserved ATPase sites, one per AAA domain. Probably only one of these (within AAA 1) actually hydrolyzes ATP, the others may serve a regulatory function.

Sequence similaritiesi

Belongs to the dynein heavy chain family.Curated

Keywords - Domaini

Coiled coil, Repeat

Phylogenomic databases

GeneTreeiENSGT00860000133709.
HOGENOMiHOG000176055.
InParanoidiP36022.
KOiK10413.
OMAiTRKKCEH.
OrthoDBiEOG092C00NZ.

Family and domain databases

Gene3Di3.40.50.300. 5 hits.
InterProiIPR003593. AAA+_ATPase.
IPR011704. ATPase_dyneun-rel_AAA.
IPR026983. DHC_fam.
IPR024743. Dynein_HC_stalk.
IPR024317. Dynein_heavy_chain_D4_dom.
IPR004273. Dynein_heavy_dom.
IPR013594. Dynein_heavy_dom-1.
IPR013602. Dynein_heavy_dom-2.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR10676. PTHR10676. 1 hit.
PfamiPF07728. AAA_5. 1 hit.
PF12780. AAA_8. 1 hit.
PF08385. DHC_N1. 1 hit.
PF08393. DHC_N2. 1 hit.
PF03028. Dynein_heavy. 1 hit.
PF12777. MT. 1 hit.
[Graphical view]
SMARTiSM00382. AAA. 3 hits.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 5 hits.

Sequencei

Sequence statusi: Complete.

P36022-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MCKNEARLAN ELIEFVAATV TGIKNSPKEN EQAFIDYLHC QYLERFQFFL
60 70 80 90 100
GLLDGREFDT LFVFLFEELD RTIVTIDIGE EAIYDANLAN KKYSTLLIIK
110 120 130 140 150
SRSVIVDAEP IATQISAIYL PGPVNAGNLA SIITHGVSSV FGQLIKSDTK
160 170 180 190 200
TYSVETIDKT RRKLDDISKQ FQQLHTSIET PDLLAMVPSI IKLAVSKGAT
210 220 230 240 250
SHDYANYLPS NDLESMRFLN ILQSIANKWF LVLKQTLAID RDIKNGSFLD
260 270 280 290 300
EVEFWSNFYE VLKSLIEQTQ SQEFQVCLSV LTNAKRFHNL TNLLNEGSLS
310 320 330 340 350
DKFKLADKYN QFLSSIPIDE VRQASNLEDL QELFPVLASS LKKFRYSGYP
360 370 380 390 400
VQRFVVLMDK ISQEVMDAIL SNLSDLFQLE YGSFLGLYEK SAGMIEEWDD
410 420 430 440 450
IVQDVNLLIR EDLRKRAPQE LLIQKLTFTS ASVKATLDEI LSTRKRFFSL
460 470 480 490 500
AETIKSISPS TYHEEIQRLY HPFEQIHDIS VNFRLKLEQA ESEFSKNMLD
510 520 530 540 550
LEKKLQNTLA SFMDSDHCPT EKLSYLVKFK PLMELCPRIK VKVLENQQIL
560 570 580 590 600
LLEIKKDIRQ LETGLELLPK ILHVEALNNI PPISARISYF LNVQSRIDNI
610 620 630 640 650
VQYLEALFGS NWNDTLEGRS ISTSIVQLRK ETNPHDVFLH WLGNFPEKAT
660 670 680 690 700
ANLLTTPILK LIRNNEDDYE LKVNFDFALA AAYSELRSLT YMAFQVPSHI
710 720 730 740 750
VRIARTYMYL YPRAINLVEL IQTFFSLSKS LSYTFYTNIF LKRNVQTVWL
760 770 780 790 800
LLQQILITPW ESLQEESSEM SCSVHSLARL EKSIDGILSD YQILKNSEPQ
810 820 830 840 850
FAKEFSGLKS FDGTADDLHE VEEIISNIQA IFENLFTKGL TNVSDHISTF
860 870 880 890 900
NNLIISIILE KVRLNLKKMH FPKHVLKLSF NEGRITSSPS LAAMKRSLLK
910 920 930 940 950
DIEALLNKVV LINFLHDPDH PLSTTLTFNS LVIKLKDDIQ NCIEQVQNLH
960 970 980 990 1000
CKINSYVKEW QKMEFLWQIT EEAFLEVVDN STQRCFGILK GLLDSQSKFD
1010 1020 1030 1040 1050
LIISRNNFSK NLVLHTEDAQ RHIRSKMDSW ILYVSKHLLT IYERDARKLH
1060 1070 1080 1090 1100
EDMNRDREAV EDMDINFTSL KNITVIIEAV NVNKRHLTER DIQIKLLGSV
1110 1120 1130 1140 1150
MRALTKLKVR FPSHFVYIDQ LDNDFSSLRQ SLSYVEQELQ KHRVVIAKSL
1160 1170 1180 1190 1200
EEGVENINNL SQSLNESWSV RKPISPTLTP PEALKILEFF NESITKLKKK
1210 1220 1230 1240 1250
MHSVAAAAKM LLIPVVLNDQ LTHVVEEVKT YDLVWRSIKN LWEDVQRTFE
1260 1270 1280 1290 1300
TPWCRVDVLL LQSDLANFLR RADELPRAVK QFEMYKSLFS QVNMLTSVNK
1310 1320 1330 1340 1350
ILVELKDGAL KPRHWNMIFR DIGKRQIQKN LLDKLEFSLK DVMVLNLTLN
1360 1370 1380 1390 1400
EILLTKIIER AQKEFVIEKS LNRIKKFWKE AQYEVIEHSS GLKLVREWDV
1410 1420 1430 1440 1450
LEQACKEDLE ELVSMKASNY YKIFEQDCLD LESKLTKLSE IQVNWVEVQF
1460 1470 1480 1490 1500
YWLDLYGILG ENLDIQNFLP LETSKFKSLT SEYKMITTRA FQLDTTIEVI
1510 1520 1530 1540 1550
HIPNFDTTLK LTIDSLKMIK SSLSTFLERQ RRQFPRFYFL GNDDLLKIIG
1560 1570 1580 1590 1600
SGKHHDQVSK FMKKMFGSIE SIIFLEDFIT GVRSVEGEVL NLNEKIELKD
1610 1620 1630 1640 1650
SIQAQEWLNI LDTEIKLSVF TQFRDCLGQL KDGTDIEVVV SKYIFQAILL
1660 1670 1680 1690 1700
SAQVMWTELV EKCLQTNQFS KYWKEVDMKI KGLLDKLNKS SDNVKKKIEA
1710 1720 1730 1740 1750
LLVEYLHFNN VIGQLKNCST KEEARLLWAK VQKFYQKNDT LDDLNSVFIS
1760 1770 1780 1790 1800
QSGYLLQYKF EYIGIPERLI YTPLLLIGFA TLTDSLHQKY GGCFFGPAGT
1810 1820 1830 1840 1850
GKTETVKAFG QNLGRVVVVF NCDDSFDYQV LSRLLVGITQ IGAWGCFDEF
1860 1870 1880 1890 1900
NRLDEKVLSA VSANIQQIQN GLQVGKSHIT LLEEETPLSP HTAVFITLNP
1910 1920 1930 1940 1950
GYNGRSELPE NLKKSFREFS MKSPQSGTIA EMILQIMGFE DSKSLASKIV
1960 1970 1980 1990 2000
HFLELLSSKC SSMNHYHFGL RTLKGVLRNC SPLISEFGEG EKTVVESLKR
2010 2020 2030 2040 2050
VILPSLGDTD ELVFKDELSK IFDSAGTPLN SKAIVQCLKD AGQRSGFSMS
2060 2070 2080 2090 2100
EEFLKKCMQF YYMQKTQQAL ILVGKAGCGK TATWKTVIDA MAIFDGHANV
2110 2120 2130 2140 2150
VYVIDTKVLT KESLYGSMLK ATLEWRDGLF TSILRRVNDD ITGTFKNSRI
2160 2170 2180 2190 2200
WVVFDSDLDP EYVEAMNSVL DDNKILTLPN GERLPIPPNF RILFETDNLD
2210 2220 2230 2240 2250
HTTPATITRC GLLWFSTDVC SISSKIDHLL NKSYEALDNK LSMFELDKLK
2260 2270 2280 2290 2300
DLISDSFDMA SLTNIFTCSN DLVHILGVRT FNKLETAVQL AVHLISSYRQ
2310 2320 2330 2340 2350
WFQNLDDKSL KDVITLLIKR SLLYALAGDS TGESQRAFIQ TINTYFGHDS
2360 2370 2380 2390 2400
QELSDYSTIV IANDKLSFSS FCSEIPSVSL EAHEVMRPDI VIPTIDTIKH
2410 2420 2430 2440 2450
EKIFYDLLNS KRGIILCGPP GSGKTMIMNN ALRNSSLYDV VGINFSKDTT
2460 2470 2480 2490 2500
TEHILSALHR HTNYVTTSKG LTLLPKSDIK NLVLFCDEIN LPKLDKYGSQ
2510 2520 2530 2540 2550
NVVLFLRQLM EKQGFWKTPE NKWVTIERIH IVGACNPPTD PGRIPMSERF
2560 2570 2580 2590 2600
TRHAAILYLG YPSGKSLSQI YEIYYKAIFK LVPEFRSYTE PFARASVHLY
2610 2620 2630 2640 2650
NECKARYSTG LQSHYLFSPR ELTRLVRGVY TAINTGPRQT LRSLIRLWAY
2660 2670 2680 2690 2700
EAWRIFADRL VGVKEKNSFE QLLYETVDKY LPNQDLGNIS STSLLFSGLL
2710 2720 2730 2740 2750
SLDFKEVNKT DLVNFIEERF KTFCDEELEV PMVIHESMVD HILRIDRALK
2760 2770 2780 2790 2800
QVQGHMMLIG ASRTGKTILT RFVAWLNGLK IVQPKIHRHS NLSDFDMILK
2810 2820 2830 2840 2850
KAISDCSLKE SRTCLIIDES NILETAFLER MNTLLANADI PDLFQGEEYD
2860 2870 2880 2890 2900
KLLNNLRNKT RSLGLLLDTE QELYDWFVGE IAKNLHVVFT ICDPTNNKSS
2910 2920 2930 2940 2950
AMISSPALFN RCIINWMGDW DTKTMSQVAN NMVDVIPMEF TDFIVPEVNK
2960 2970 2980 2990 3000
ELVFTEPIQT IRDAVVNILI HFDRNFYQKM KVGVNPRSPG YFIDGLRALV
3010 3020 3030 3040 3050
KLVTAKYQDL QENQRFVNVG LEKLNESVLK VNELNKTLSK KSTELTEKEK
3060 3070 3080 3090 3100
EARSTLDKML MEQNESERKQ EATEEIKKIL KVQEEDIRKR KEVVMKSIQD
3110 3120 3130 3140 3150
IEPTILEAQR GVKNIKKQQL TEIRSMVNPP SGVKIVMEAV CAILGYQFSN
3160 3170 3180 3190 3200
WRDIQQFIRK DDFIHNIVHY DTTLHMKPQI RKYMEEEFLS DPNFTYETIN
3210 3220 3230 3240 3250
RASKACGPLY QWVNAQINFS KVLENVDPLR QEMKRIEFES LKTKANLLAA
3260 3270 3280 3290 3300
EEMTQDLEAS IEVSKRKYSL LIRDVEAIKT EMSNVQANLD RSISLVKSLT
3310 3320 3330 3340 3350
FEKERWLNTT KQFSKTSQEL IGNCIISSIY ETYFGHLNER ERADMLVILK
3360 3370 3380 3390 3400
RLLGKFAVKY DVNYRFIDYL VTLDEKMKWL ECGLDKNDYF LENMSIVMNS
3410 3420 3430 3440 3450
QDAVPFLLDP SSHMITVISN YYGNKTVLLS FLEEGFVKRL ENAIRFGSVV
3460 3470 3480 3490 3500
IIQDGEFFDP IISRLISREF NHAGNRVTVE IGDHEVDVSG DFKLFIHSCD
3510 3520 3530 3540 3550
PSGDIPIFLR SRVRLVHFVT NKESIETRIF DITLTEENAE MQRKREDLIK
3560 3570 3580 3590 3600
LNTEYKLKLK NLEKRLLEEL NNSQGNMLEN DELMVTLNNL KKEAMNIEKK
3610 3620 3630 3640 3650
LSESEEFFPQ FDNLVEEYSI IGKHSVKIFS MLEKFGQFHW FYGISIGQFL
3660 3670 3680 3690 3700
SCFKRVFIKK SRETRAARTR VDEILWLLYQ EVYCQFSTAL DKKFKMIMAM
3710 3720 3730 3740 3750
TMFCLYKFDI ESEQYKEAVL TMIGVLSESS DGVPKLTVDT NNDLRYLWDY
3760 3770 3780 3790 3800
VTTKSYISAL NWFKNEFFVD EWNIADVVAN SENNYFTMAS ERDVDGTFKL
3810 3820 3830 3840 3850
IELAKASKES LKIIPLGSIE NLNYAQEEIS KSKIEGGWIL LQNIQMSLSW
3860 3870 3880 3890 3900
VKTYLHKHVE ETKAAEEHEK FKMFMTCHLT GDKLPAPLLQ RTDRFVYEDI
3910 3920 3930 3940 3950
PGILDTVKDL WGSQFFTGKI SGVWSVYCTF LLSWFHALIT ARTRLVPHGF
3960 3970 3980 3990 4000
SKKYYFNDCD FQFASVYLEN VLATNSTNNI PWAQVRDHIA TIVYGGKIDE
4010 4020 4030 4040 4050
EKDLEVVAKL CAHVFCGSDN LQIVPGVRIP QPLLQQSEEE ERARLTAILS
4060 4070 4080 4090
NTIEPADSLS SWLQLPRESI LNYERLQAKE VASSTEQLLQ EM
Length:4,092
Mass (Da):471,348
Last modified:June 1, 1994 - v1
Checksum:i3D9DF447E8E2D6BB
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti589Y → C in AAA16055 (PubMed:8234262).Curated1
Sequence conflicti601V → A in AAA16055 (PubMed:8234262).Curated1
Sequence conflicti1364E → A in AAA16055 (PubMed:8234262).Curated1
Sequence conflicti2118 – 2119ML → IV in CAA79923 (PubMed:8248224).Curated2

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z21877 Genomic DNA. Translation: CAA79923.1.
L15626 Unassigned DNA. Translation: AAA16055.1.
Z28279 Genomic DNA. Translation: CAA82132.1.
BK006944 Genomic DNA. Translation: DAA09205.1.
PIRiS38128.
RefSeqiNP_012980.1. NM_001179844.1.

Genome annotation databases

EnsemblFungiiYKR054C; YKR054C; YKR054C.
GeneIDi853928.
KEGGisce:YKR054C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z21877 Genomic DNA. Translation: CAA79923.1.
L15626 Unassigned DNA. Translation: AAA16055.1.
Z28279 Genomic DNA. Translation: CAA82132.1.
BK006944 Genomic DNA. Translation: DAA09205.1.
PIRiS38128.
RefSeqiNP_012980.1. NM_001179844.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3J67electron microscopy34.00A1554-4092[»]
3J68electron microscopy30.00A1554-4092[»]
3QMZX-ray6.00A/B1364-4092[»]
4AI6X-ray3.40A/B1364-4092[»]
4AKGX-ray3.30A/B1364-4092[»]
4AKHX-ray3.60A/B1364-4092[»]
4AKIX-ray3.70A/B1364-4092[»]
4W8FX-ray3.54A/B1364-3038[»]
A/B3292-4092[»]
5AFRX-ray5.00A/B1-557[»]
ProteinModelPortaliP36022.
SMRiP36022.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34185. 232 interactors.
DIPiDIP-2644N.
IntActiP36022. 9 interactors.
MINTiMINT-427451.

PTM databases

iPTMnetiP36022.

Proteomic databases

MaxQBiP36022.
PRIDEiP36022.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYKR054C; YKR054C; YKR054C.
GeneIDi853928.
KEGGisce:YKR054C.

Organism-specific databases

EuPathDBiFungiDB:YKR054C.
SGDiS000001762. DYN1.

Phylogenomic databases

GeneTreeiENSGT00860000133709.
HOGENOMiHOG000176055.
InParanoidiP36022.
KOiK10413.
OMAiTRKKCEH.
OrthoDBiEOG092C00NZ.

Enzyme and pathway databases

BioCyciYEAST:G3O-32023-MONOMER.
ReactomeiR-SCE-6798695. Neutrophil degranulation.

Miscellaneous databases

PROiP36022.

Family and domain databases

Gene3Di3.40.50.300. 5 hits.
InterProiIPR003593. AAA+_ATPase.
IPR011704. ATPase_dyneun-rel_AAA.
IPR026983. DHC_fam.
IPR024743. Dynein_HC_stalk.
IPR024317. Dynein_heavy_chain_D4_dom.
IPR004273. Dynein_heavy_dom.
IPR013594. Dynein_heavy_dom-1.
IPR013602. Dynein_heavy_dom-2.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR10676. PTHR10676. 1 hit.
PfamiPF07728. AAA_5. 1 hit.
PF12780. AAA_8. 1 hit.
PF08385. DHC_N1. 1 hit.
PF08393. DHC_N2. 1 hit.
PF03028. Dynein_heavy. 1 hit.
PF12777. MT. 1 hit.
[Graphical view]
SMARTiSM00382. AAA. 3 hits.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 5 hits.
ProtoNetiSearch...

Entry informationi

Entry nameiDYHC_YEAST
AccessioniPrimary (citable) accession number: P36022
Secondary accession number(s): D6VXB5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: November 30, 2016
This is version 147 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 195 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome XI
    Yeast (Saccharomyces cerevisiae) chromosome XI: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.