CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-012288
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Cytoplasmic dynein 1 heavy chain 1 
Protein Synonyms/Alias
 Cytoplasmic dynein heavy chain 1; Dynein heavy chain, cytosolic 
Gene Name
 DYNC1H1 
Gene Synonyms/Alias
 DHC1; DNCH1; DNCL; DNECL; DYHC; KIAA0325 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
59LEAALEEKSALEQMRubiquitination[1]
67SALEQMRKFLSDPQVubiquitination[2, 3, 4]
85LVERSTLKEDVGDEGubiquitination[1, 5]
120SNSLAFIKRTPVIDAubiquitination[1, 2, 4]
129TPVIDADKPVSSQLRubiquitination[3]
235KVTDFGDKVEDPTFLacetylation[6]
371LRKIRNTKYPIQRALacetylation[7]
371LRKIRNTKYPIQRALubiquitination[5]
394DLSSQLLKVLGTRKLacetylation[7]
394DLSSQLLKVLGTRKLubiquitination[1, 2, 3, 4, 5]
400LKVLGTRKLMHVAYEubiquitination[3]
576RDQLGTAKNANEMFRubiquitination[3, 5, 8]
613TQLIQRVKDDIESLHubiquitination[5]
622DIESLHDKFKVQYPQubiquitination[3]
624ESLHDKFKVQYPQSQubiquitination[3]
634YPQSQACKMSHVRDLubiquitination[3, 8]
652SGSIIWAKQIDRQLTubiquitination[2, 3, 4, 8, 9]
671RVEDVLGKGWENHVEubiquitination[1, 3, 5]
681ENHVEGQKLKQDGDSubiquitination[3]
683HVEGQKLKQDGDSFRubiquitination[3, 5, 8]
692DGDSFRMKLNTQEIFubiquitination[1, 3]
736TGNVLKLKVNFLPEIubiquitination[3, 5, 8]
748PEIITLSKEVRNLKWubiquitination[1, 2, 3, 4, 5, 8, 10]
754SKEVRNLKWLGFRVPacetylation[7]
754SKEVRNLKWLGFRVPubiquitination[1, 2, 4, 5, 9]
809SLLVAGLKKEVQALIubiquitination[5]
956PGGEPKIKNVVHELRubiquitination[3]
981PIEECRYKLYQEMFAubiquitination[3]
1078RLGEDLNKWQALLVQubiquitination[1, 3]
1099TFDNAETKKEFGPVVubiquitination[3, 5]
1100FDNAETKKEFGPVVIubiquitination[3]
1125LKYDSWHKEVLSKFGacetylation[7]
1228FNDIMRRKDSAIQQQubiquitination[3]
1286ALTIYEGKFGRLKDDacetylation[7]
1330LEELQDLKGVWSELSubiquitination[1, 5, 11]
1347WEQIDQMKEQPWVSVubiquitination[1, 3, 5]
1371DALLNQLKSFPARLRubiquitination[2, 4]
1498DDLFNKVKEHINSVSubiquitination[5]
1526DALSWEDKLNRIMALubiquitination[5]
1584ALMKKVSKSPLVMDVubiquitination[5, 9]
1807QPPLRRRKLEHLITEubiquitination[3]
1834KSKIDNAKSFEWLSQubiquitination[3]
1878EYLGVQDKLVQTPLTubiquitination[1, 3]
1912FGPAGTGKTESVKALubiquitination[3, 5]
1917TGKTESVKALGHQLGubiquitination[3, 5]
1992HSNPNYDKTSAPITCubiquitination[3]
2004ITCELLNKQVKVSPDubiquitination[3]
2034NLPDNLKKLFRSLAMubiquitination[3]
2068TAEVLANKIVPFFKLubiquitination[1, 3, 5]
2104LVSAGNVKRERIQKIubiquitination[3]
2239MAWRVLLKALERLEGubiquitination[1, 3, 5]
2261IDPKAISKDHLYGTLubiquitination[1, 3, 5]
2349MFEVQDLKYATLATVubiquitination[3, 5]
2399DEAQRRRKGKEDEGEubiquitination[3]
2401AQRRRKGKEDEGEEAubiquitination[1, 3, 5]
2561QIEVETHKVAAPDVVubiquitination[3, 8]
2702TSDQTWVKLERIQFVubiquitination[1, 3, 5]
2721PPTDPGRKPLSHRFLubiquitination[3]
2856NIDTVALKHFPNIDRubiquitination[1, 2, 3, 4, 5, 12]
2865FPNIDREKAMSRPILubiquitination[3]
2879LYSNWLSKDYIPVDQubiquitination[1, 2, 3, 4]
2966YQIKVHRKYTGEDFDubiquitination[5]
2989RSGCKNEKIAFIMDEubiquitination[5]
3039QCKEGAQKEGLMLDSubiquitination[3]
3076NPSSEGLKDRAATSPubiquitination[3]
3190YANLFHEKRSELEEQubiquitination[1]
3284SVKEDLDKVEPAVIEubiquitination[5]
3369AIREKMKKNYMSNPSubiquitination[2, 4, 9]
3407LNYADMLKRVEPLRNubiquitination[3]
3429DAKDNQQKANEVEQMubiquitination[5]
3480NRSTALLKSLSAEREacetylation[7, 13]
3480NRSTALLKSLSAEREubiquitination[3]
3581TENAIMLKRFNRYPLubiquitination[1, 3, 14]
3605EFIMNEYKDRKITRTubiquitination[1, 5]
3621FLDDAFRKNLESALRubiquitination[2, 3, 4]
3747LRLRQLEKSLLQALNubiquitination[1]
3757LQALNEVKGRILDDDubiquitination[1, 2, 3, 4, 5, 8, 9]
3774ITTLENLKREAAEVTubiquitination[1, 3, 5, 8, 11, 14]
3893LLARIKLKGTVGEPTubiquitination[1]
3945LSCLPAFKDLIAKVQubiquitination[3, 8]
4154FEPPPGVKANMLRTFubiquitination[1, 3, 5, 8]
4203YAPLGWSKKYEFGESubiquitination[3, 5]
4204APLGWSKKYEFGESDubiquitination[3, 8]
4228TWLDDTAKGRQNISPubiquitination[3, 8]
4237RQNISPDKIPWSALKubiquitination[2, 4]
4283RSFDSEFKLACKVDGacetylation[6, 7, 8, 13]
4283RSFDSEFKLACKVDGubiquitination[3]
4342QGVDMISKMLKMQMLubiquitination[1, 3]
4362LAYAETEKKTRTDSTubiquitination[1, 5]
4406KRTVENIKDPLFRFFubiquitination[1, 3, 5, 8]
4457TLINELVKGILPRSWacetylation[6]
4457TLINELVKGILPRSWubiquitination[1, 3, 5]
Reference
 [1] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [2] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [3] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [4] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [5] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [6] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [7] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [8] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [9] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [10] Mass spectrometric analysis of lysine ubiquitylation reveals promiscuity at site level.
 Danielsen JM, Sylvestersen KB, Bekker-Jensen S, Szklarczyk D, Poulsen JW, Horn H, Jensen LJ, Mailand N, Nielsen ML.
 Mol Cell Proteomics. 2011 Mar;10(3):M110.003590. [PMID: 21139048]
 [11] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572]
 [12] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [13] Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response.
 Beli P, Lukashchuk N, Wagner SA, Weinert BT, Olsen JV, Baskcomb L, Mann M, Jackson SP, Choudhary C.
 Mol Cell. 2012 Apr 27;46(2):212-25. [PMID: 22424773]
 [14] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724] 
Functional Description
 Cytoplasmic dynein 1 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. 
Sequence Annotation
 NP_BIND 1906 1913 ATP (Potential).
 NP_BIND 2224 2231 ATP (Potential).
 NP_BIND 2595 2602 ATP (Potential).
 NP_BIND 2937 2944 ATP (Potential).
 REGION 53 1867 Stem (By similarity).
 REGION 448 703 Interaction with DYNC1I2 (By similarity).
 REGION 651 802 Interaction with DYNC1LI2 (By
 REGION 1868 2099 AAA 1 (By similarity).
 REGION 2180 2452 AAA 2 (By similarity).
 REGION 2556 2805 AAA 3 (By similarity).
 REGION 2899 3168 AAA 4 (By similarity).
 REGION 3189 3500 Stalk (By similarity).
 REGION 3553 3782 AAA 5 (By similarity).
 REGION 4005 4221 AAA 6 (By similarity).
 MOD_RES 1125 1125 N6-acetyllysine.
 MOD_RES 3379 3379 Phosphotyrosine (By similarity).
 MOD_RES 3480 3480 N6-acetyllysine.
 MOD_RES 4218 4218 Phosphothreonine (By similarity).
 MOD_RES 4221 4221 Phosphothreonine (By similarity).
 MOD_RES 4283 4283 N6-acetyllysine.
 MOD_RES 4368 4368 Phosphoserine.  
Keyword
 3D-structure; Acetylation; ATP-binding; Charcot-Marie-Tooth disease; Coiled coil; Complete proteome; Cytoplasm; Cytoskeleton; Disease mutation; Dynein; Mental retardation; Microtubule; Motor protein; Neurodegeneration; Neuropathy; Nucleotide-binding; Phosphoprotein; Polymorphism; Reference proteome; Repeat; Transport. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 4646 AA 
Protein Sequence
MSEPGGGGGE DGSAGLEVSA VQNVADVSVL QKHLRKLVPL LLEDGGEAPA ALEAALEEKS 60
ALEQMRKFLS DPQVHTVLVE RSTLKEDVGD EGEEEKEFIS YNINIDIHYG VKSNSLAFIK 120
RTPVIDADKP VSSQLRVLTL SEDSPYETLH SFISNAVAPF FKSYIRESGK ADRDGDKMAP 180
SVEKKIAELE MGLLHLQQNI EIPEISLPIH PMITNVAKQC YERGEKPKVT DFGDKVEDPT 240
FLNQLQSGVN RWIREIQKVT KLDRDPASGT ALQEISFWLN LERALYRIQE KRESPEVLLT 300
LDILKHGKRF HATVSFDTDT GLKQALETVN DYNPLMKDFP LNDLLSATEL DKIRQALVAI 360
FTHLRKIRNT KYPIQRALRL VEAISRDLSS QLLKVLGTRK LMHVAYEEFE KVMVACFEVF 420
QTWDDEYEKL QVLLRDIVKR KREENLKMVW RINPAHRKLQ ARLDQMRKFR RQHEQLRAVI 480
VRVLRPQVTA VAQQNQGEVP EPQDMKVAEV LFDAADANAI EEVNLAYENV KEVDGLDVSK 540
EGTEAWEAAM KRYDERIDRV ETRITARLRD QLGTAKNANE MFRIFSRFNA LFVRPHIRGA 600
IREYQTQLIQ RVKDDIESLH DKFKVQYPQS QACKMSHVRD LPPVSGSIIW AKQIDRQLTA 660
YMKRVEDVLG KGWENHVEGQ KLKQDGDSFR MKLNTQEIFD DWARKVQQRN LGVSGRIFTI 720
ESTRVRGRTG NVLKLKVNFL PEIITLSKEV RNLKWLGFRV PLAIVNKAHQ ANQLYPFAIS 780
LIESVRTYER TCEKVEERNT ISLLVAGLKK EVQALIAEGI ALVWESYKLD PYVQRLAETV 840
FNFQEKVDDL LIIEEKIDLE VRSLETCMYD HKTFSEILNR VQKAVDDLNL HSYSNLPIWV 900
NKLDMEIERI LGVRLQAGLR AWTQVLLGQA EDKAEVDMDT DAPQVSHKPG GEPKIKNVVH 960
ELRITNQVIY LNPPIEECRY KLYQEMFAWK MVVLSLPRIQ SQRYQVGVHY ELTEEEKFYR 1020
NALTRMPDGP VALEESYSAV MGIVSEVEQY VKVWLQYQCL WDMQAENIYN RLGEDLNKWQ 1080
ALLVQIRKAR GTFDNAETKK EFGPVVIDYG KVQSKVNLKY DSWHKEVLSK FGQMLGSNMT 1140
EFHSQISKSR QELEQHSVDT ASTSDAVTFI TYVQSLKRKI KQFEKQVELY RNGQRLLEKQ 1200
RFQFPPSWLY IDNIEGEWGA FNDIMRRKDS AIQQQVANLQ MKIVQEDRAV ESRTTDLLTD 1260
WEKTKPVTGN LRPEEALQAL TIYEGKFGRL KDDREKCAKA KEALELTDTG LLSGSEERVQ 1320
VALEELQDLK GVWSELSKVW EQIDQMKEQP WVSVQPRKLR QNLDALLNQL KSFPARLRQY 1380
ASYEFVQRLL KGYMKINMLV IELKSEALKD RHWKQLMKRL HVNWVVSELT LGQIWDVDLQ 1440
KNEAIVKDVL LVAQGEMALE EFLKQIREVW NTYELDLVNY QNKCRLIRGW DDLFNKVKEH 1500
INSVSAMKLS PYYKVFEEDA LSWEDKLNRI MALFDVWIDV QRRWVYLEGI FTGSADIKHL 1560
LPVETQRFQS ISTEFLALMK KVSKSPLVMD VLNIQGVQRS LERLADLLGK IQKALGEYLE 1620
RERSSFPRFY FVGDEDLLEI IGNSKNVAKL QKHFKKMFAG VSSIILNEDN SVVLGISSRE 1680
GEEVMFKTPV SITEHPKINE WLTLVEKEMR VTLAKLLAES VTEVEIFGKA TSIDPNTYIT 1740
WIDKYQAQLV VLSAQIAWSE NVETALSSMG GGGDAAPLHS VLSNVEVTLN VLADSVLMEQ 1800
PPLRRRKLEH LITELVHQRD VTRSLIKSKI DNAKSFEWLS QMRFYFDPKQ TDVLQQLSIQ 1860
MANAKFNYGF EYLGVQDKLV QTPLTDRCYL TMTQALEARL GGSPFGPAGT GKTESVKALG 1920
HQLGRFVLVF NCDETFDFQA MGRIFVGLCQ VGAWGCFDEF NRLEERMLSA VSQQVQCIQE 1980
ALREHSNPNY DKTSAPITCE LLNKQVKVSP DMAIFITMNP GYAGRSNLPD NLKKLFRSLA 2040
MTKPDRQLIA QVMLYSQGFR TAEVLANKIV PFFKLCDEQL SSQSHYDFGL RALKSVLVSA 2100
GNVKRERIQK IKREKEERGE AVDEGEIAEN LPEQEILIQS VCETMVPKLV AEDIPLLFSL 2160
LSDVFPGVQY HRGEMTALRE ELKKVCQEMY LTYGDGEEVG GMWVEKVLQL YQITQINHGL 2220
MMVGPSGSGK SMAWRVLLKA LERLEGVEGV AHIIDPKAIS KDHLYGTLDP NTREWTDGLF 2280
THVLRKIIDS VRGELQKRQW IVFDGDVDPE WVENLNSVLD DNKLLTLPNG ERLSLPPNVR 2340
IMFEVQDLKY ATLATVSRCG MVWFSEDVLS TDMIFNNFLA RLRSIPLDEG EDEAQRRRKG 2400
KEDEGEEAAS PMLQIQRDAA TIMQPYFTSN GLVTKALEHA FQLEHIMDLT RLRCLGSLFS 2460
MLHQACRNVA QYNANHPDFP MQIEQLERYI QRYLVYAILW SLSGDSRLKM RAELGEYIRR 2520
ITTVPLPTAP NIPIIDYEVS ISGEWSPWQA KVPQIEVETH KVAAPDVVVP TLDTVRHEAL 2580
LYTWLAEHKP LVLCGPPGSG KTMTLFSALR ALPDMEVVGL NFSSATTPEL LLKTFDHYCE 2640
YRRTPNGVVL APVQLGKWLV LFCDEINLPD MDKYGTQRVI SFIRQMVEHG GFYRTSDQTW 2700
VKLERIQFVG ACNPPTDPGR KPLSHRFLRH VPVVYVDYPG PASLTQIYGT FNRAMLRLIP 2760
SLRTYAEPLT AAMVEFYTMS QERFTQDTQP HYIYSPREMT RWVRGIFEAL RPLETLPVEG 2820
LIRIWAHEAL RLFQDRLVED EERRWTDENI DTVALKHFPN IDREKAMSRP ILYSNWLSKD 2880
YIPVDQEELR DYVKARLKVF YEEELDVPLV LFNEVLDHVL RIDRIFRQPQ GHLLLIGVSG 2940
AGKTTLSRFV AWMNGLSVYQ IKVHRKYTGE DFDEDLRTVL RRSGCKNEKI AFIMDESNVL 3000
DSGFLERMNT LLANGEVPGL FEGDEYATLM TQCKEGAQKE GLMLDSHEEL YKWFTSQVIR 3060
NLHVVFTMNP SSEGLKDRAA TSPALFNRCV LNWFGDWSTE ALYQVGKEFT SKMDLEKPNY 3120
IVPDYMPVVY DKLPQPPSHR EAIVNSCVFV HQTLHQANAR LAKRGGRTMA ITPRHYLDFI 3180
NHYANLFHEK RSELEEQQMH LNVGLRKIKE TVDQVEELRR DLRIKSQELE VKNAAANDKL 3240
KKMVKDQQEA EKKKVMSQEI QEQLHKQQEV IADKQMSVKE DLDKVEPAVI EAQNAVKSIK 3300
KQHLVEVRSM ANPPAAVKLA LESICLLLGE STTDWKQIRS IIMRENFIPT IVNFSAEEIS 3360
DAIREKMKKN YMSNPSYNYE IVNRASLACG PMVKWAIAQL NYADMLKRVE PLRNELQKLE 3420
DDAKDNQQKA NEVEQMIRDL EASIARYKEE YAVLISEAQA IKADLAAVEA KVNRSTALLK 3480
SLSAERERWE KTSETFKNQM STIAGDCLLS AAFIAYAGYF DQQMRQNLFT TWSHHLQQAN 3540
IQFRTDIART EYLSNADERL RWQASSLPAD DLCTENAIML KRFNRYPLII DPSGQATEFI 3600
MNEYKDRKIT RTSFLDDAFR KNLESALRFG NPLLVQDVES YDPVLNPVLN REVRRTGGRV 3660
LITLGDQDID LSPSFVIFLS TRDPTVEFPP DLCSRVTFVN FTVTRSSLQS QCLNEVLKAE 3720
RPDVDEKRSD LLKLQGEFQL RLRQLEKSLL QALNEVKGRI LDDDTIITTL ENLKREAAEV 3780
TRKVEETDIV MQEVETVSQQ YLPLSTACSS IYFTMESLKQ IHFLYQYSLQ FFLDIYHNVL 3840
YENPNLKGVT DHTQRLSIIT KDLFQVAFNR VARGMLHQDH ITFAMLLARI KLKGTVGEPT 3900
YDAEFQHFLR GNEIVLSAGS TPRIQGLTVE QAEAVVRLSC LPAFKDLIAK VQADEQFGIW 3960
LDSSSPEQTV PYLWSEETPA TPIGQAIHRL LLIQAFRPDR LLAMAHMFVS TNLGESFMSI 4020
MEQPLDLTHI VGTEVKPNTP VLMCSVPGYD ASGHVEDLAA EQNTQITSIA IGSAEGFNQA 4080
DKAINTAVKS GRWVMLKNVH LAPGWLMQLE KKLHSLQPHA CFRLFLTMEI NPKVPVNLLR 4140
AGRIFVFEPP PGVKANMLRT FSSIPVSRIC KSPNERARLY FLLAWFHAII QERLRYAPLG 4200
WSKKYEFGES DLRSACDTVD TWLDDTAKGR QNISPDKIPW SALKTLMAQS IYGGRVDNEF 4260
DQRLLNTFLE RLFTTRSFDS EFKLACKVDG HKDIQMPDGI RREEFVQWVE LLPDTQTPSW 4320
LGLPNNAERV LLTTQGVDMI SKMLKMQMLE DEDDLAYAET EKKTRTDSTS DGRPAWMRTL 4380
HTTASNWLHL IPQTLSHLKR TVENIKDPLF RFFEREVKMG AKLLQDVRQD LADVVQVCEG 4440
KKKQTNYLRT LINELVKGIL PRSWSHYTVP AGMTVIQWVS DFSERIKQLQ NISLAAASGG 4500
AKELKNIHVC LGGLFVPEAY ITATRQYVAQ ANSWSLEELC LEVNVTTSQG ATLDACSFGV 4560
TGLKLQGATC NNNKLSLSNA ISTALPLTQL RWVKQTNTEK KASVVTLPVY LNFTRADLIF 4620
TVDFEIATKE DPRSFYERGV AVLCTE 4646 
Gene Ontology
 GO:0005813; C:centrosome; IDA:UniProtKB.
 GO:0005868; C:cytoplasmic dynein complex; NAS:UniProtKB.
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0070062; C:extracellular vesicular exosome; IDA:UniProtKB.
 GO:0005794; C:Golgi apparatus; IDA:HPA.
 GO:0005874; C:microtubule; IDA:UniProtKB.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0042623; F:ATPase activity, coupled; NAS:UniProtKB.
 GO:0003777; F:microtubule motor activity; NAS:UniProtKB.
 GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; TAS:Reactome.
 GO:0008219; P:cell death; IEA:UniProtKB-KW.
 GO:0033962; P:cytoplasmic mRNA processing body assembly; ISS:BHF-UCL.
 GO:0000086; P:G2/M transition of mitotic cell cycle; TAS:Reactome.
 GO:0007018; P:microtubule-based movement; NAS:UniProtKB.
 GO:0007052; P:mitotic spindle organization; NAS:UniProtKB.
 GO:0034063; P:stress granule assembly; ISS:BHF-UCL.
 GO:0006810; P:transport; IEA:UniProtKB-KW. 
Interpro
 IPR003593; AAA+_ATPase.
 IPR011704; ATPase_dyneun-rel_AAA.
 IPR026983; DHC_fam.
 IPR025290; DUF4151.
 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. 
Pfam
 PF07728; AAA_5
 PF12780; AAA_8
 PF08385; DHC_N1
 PF08393; DHC_N2
 PF13666; DUF4151
 PF03028; Dynein_heavy
 PF12777; MT 
SMART
 SM00382; AAA 
PROSITE
  
PRINTS