Skip Header

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

Dynein heavy chain 2, axonemal

Gene

Dnah2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Force generating protein of respiratory cilia. Produces force towards the minus ends of microtubules. Dynein has ATPase activity; the force-producing power stroke is thought to occur on release of ADP. Involved in sperm motility; implicated in sperm flagellar assembly (By similarity).By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi1832 – 18398ATPSequence analysis
Nucleotide bindingi2113 – 21208ATPSequence analysis
Nucleotide bindingi2445 – 24528ATPSequence analysis
Nucleotide bindingi2791 – 27988ATPSequence analysis

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Motor protein

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Dynein heavy chain 2, axonemal
Alternative name(s):
Axonemal beta dynein heavy chain 2
Ciliary dynein heavy chain 2
Gene namesi
Name:Dnah2
Synonyms:Dnahc2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:107731. Dnah2.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB-KW
  • inner dynein arm Source: MGI
  • microtubule Source: UniProtKB-KW
  • motile primary cilium Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell projection, Cilium, Cytoplasm, Cytoskeleton, Dynein, Microtubule

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 44564456Dynein heavy chain 2, axonemalPRO_0000322543Add
BLAST

Proteomic databases

EPDiP0C6F1.
MaxQBiP0C6F1.
PaxDbiP0C6F1.
PRIDEiP0C6F1.

PTM databases

iPTMnetiP0C6F1.
PhosphoSiteiP0C6F1.

Expressioni

Gene expression databases

BgeeiENSMUSG00000005237.
CleanExiMM_DNAHC2.
ExpressionAtlasiP0C6F1. baseline and differential.
GenevisibleiP0C6F1. MM.

Interactioni

Subunit structurei

Consists of at least two heavy chains and a number of intermediate and light chains.

Protein-protein interaction databases

IntActiP0C6F1. 1 interaction.
STRINGi10090.ENSMUSP00000104299.

Structurei

3D structure databases

ProteinModelPortaliP0C6F1.
SMRiP0C6F1. Positions 3042-3671, 3874-4096.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati1439 – 147436TPR 1Add
BLAST
Repeati2750 – 278334TPR 2Add
BLAST
Repeati3101 – 313434TPR 3Add
BLAST
Repeati4101 – 413434TPR 4Add
BLAST
Repeati4135 – 416935TPR 5Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 17951795StemBy similarityAdd
BLAST
Regioni1794 – 2015222AAA 1By similarityAdd
BLAST
Regioni2075 – 2302228AAA 2By similarityAdd
BLAST
Regioni2407 – 2654248AAA 3By similarityAdd
BLAST
Regioni2751 – 3003253AAA 4By similarityAdd
BLAST
Regioni3018 – 3301284StalkBy similarityAdd
BLAST
Regioni3387 – 3617231AAA 5By similarityAdd
BLAST
Regioni3833 – 4052220AAA 6By similarityAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili1218 – 127457Sequence analysisAdd
BLAST
Coiled coili3041 – 307838Sequence analysisAdd
BLAST
Coiled coili3245 – 333389Sequence analysisAdd
BLAST
Coiled coili3552 – 359645Sequence analysisAdd
BLAST

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 (By similarity).By similarity

Sequence similaritiesi

Belongs to the dynein heavy chain family.Curated
Contains 5 TPR repeats.Curated

Keywords - Domaini

Coiled coil, Repeat, TPR repeat

Phylogenomic databases

eggNOGiKOG3595. Eukaryota.
COG5245. LUCA.
GeneTreeiENSGT00760000118964.
HOGENOMiHOG000237308.
HOVERGENiHBG104828.
InParanoidiP0C6F1.

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. 2 hits.
PfamiPF07728. AAA_5. 1 hit.
PF12780. AAA_8. 1 hit.
PF08385. DHC_N1. 2 hits.
PF08393. DHC_N2. 1 hit.
PF03028. Dynein_heavy. 1 hit.
PF12777. MT. 1 hit.
[Graphical view]
SMARTiSM00382. AAA. 2 hits.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 5 hits.

Sequencei

Sequence statusi: Complete.

P0C6F1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASKAEKKRK VAGRGGARAG RVVRAPQSTA GPGATEASLL PDGQEPEPES
60 70 80 90 100
GKEDSVLGLQ AFASWRLTPA LHGEANTPPT LLHPQPLFHR RLTTLNLILS
110 120 130 140 150
CSRAGTRDLA LKPFFLSRTM LTGLADATWT GEHDMVLEHF VQDPAVPALT
160 170 180 190 200
IFIDPVFGLK LELGMPVQTQ NQIVYFIRQA PVPITPENFE ETVQYGTVRG
210 220 230 240 250
AYIPALLRLL SGVYVPQIFM NKSWPESIRN HFVSHLHRFL ASLTDTRYKL
260 270 280 290 300
EGHTVLYIPA EAVQMDPEVV VKDKELVQRL ETSMIHWTRQ IKEVLSAQES
310 320 330 340 350
VETGENLGPL EEIEFWHNRC MDLSSISKQL VKKGVKHIES ILFLAKSSYL
360 370 380 390 400
TPFRKLAQQI QDGSRQAQSN LTFLSILREP YQELAFMKPK DISEKLPKLI
410 420 430 440 450
SLIRIIWVNS PHYNTRERLT ALFRKVCECQ YHFARWEDGK QGPLPCFFGA
460 470 480 490 500
QGPQITRNLL EIEDIFHKNL QTLRAVRGGI LDVKNTSWHE DYNKFRGGIK
510 520 530 540 550
DLEVMTQNLI TSAFELVRDV EHGVLLLDTF HRLATREAIM RTYEKKAVDL
560 570 580 590 600
YMLFNSELAL VNRELNKKWP YLEPYMTQYS GQAHWVRILR RRIDRVMNCL
610 620 630 640 650
SGAHFLPHIG TGEESIHTYQ QMAQAIDEMV RKTFQEWTAT LDKDCIRRLD
660 670 680 690 700
MSLLRISQEK VGMLDVNFDK TLLILFAEID YWERLLFETP HYVMNVAERA
710 720 730 740 750
EDLRILRENL LLVARDYNRI IAMLSPDEQA LFKERIRFLD KKIHPGLKKL
760 770 780 790 800
NWALKGASAF FITECRMHAS KVQMIVNDFK ASTLTIGWKA QEMSELLLVH
810 820 830 840 850
ITGKQVYRDL EFEEAQREHR MAAQQKLVKL HQDVVNIMTN SYEVFKNDGP
860 870 880 890 900
EIQQQWLLYT IRLDHMMEDA LRLNVKWSLL ELSKAINGDG KTTPNPLFRV
910 920 930 940 950
LVILQNDVRG GGSQVEFSPT LQTLASVVND IGSHLFATIS VFRHLPDILT
960 970 980 990 1000
KRKMNREPIY VLVERDEDIR KIQAQISSGM TNNASLLQNY LKTWDMYREI
1010 1020 1030 1040 1050
WEINKDSFIR RYQRLNPPVS SFDADIARYT EVANNVQKEE TVLNIQFVML
1060 1070 1080 1090 1100
DCSHLKFSLV QHCNEWQNKF TTLLKEMAAG RLADLHSYLK DNAEKISHPP
1110 1120 1130 1140 1150
QTLEELGVSL QLMDTLQHDL PNLETQIPPI HEQFTILEKY EVPVPDTVLE
1160 1170 1180 1190 1200
MLESLNGEWL TFQQILLDSE QMLKKHKEKF KTGLIHAADD FKKKAHNLLE
1210 1220 1230 1240 1250
DFEFKGPFTS TVGHTAALDQ IAQMRAMLMA MRDEENNLRS NLGIFKIEQP
1260 1270 1280 1290 1300
VSKDLQILEK ELDALQQVWE ITRDWEESWN QWKMGCFQTL QTEAMESMAH
1310 1320 1330 1340 1350
GLFRRLTRLA KEYKDRNWEI IETTRSKIEQ FKRTMPLISD LRNPALRERH
1360 1370 1380 1390 1400
WDQVKEEVQR EFDQESESFT LEQIVKLGMD QHVEKIAEIS ASATKELAIE
1410 1420 1430 1440 1450
VGLQNIAKTW DSTQLDIVPY KDKGHHRLRG TEEVFQALED NQVALSTMKA
1460 1470 1480 1490 1500
SRFVKAFEKD VDHWERCLSL ILEVIEMVLT VQRQWMYLEN IFLGEDIRKQ
1510 1520 1530 1540 1550
LPNESALFDQ VNNNWKAIMD RMNKDNNALR STHYPGLLET LIEMNAILED
1560 1570 1580 1590 1600
IQKSLDMYLE TKRHIFPRFY FLSNDDLLEI LGQSRNPEAV QPHLKKCFDN
1610 1620 1630 1640 1650
IKLLKIQKVG GSSSKWEAVG MFSGDGEYID FLHPVLLEGP VESWLGDVER
1660 1670 1680 1690 1700
AMRMTLRDLL RNCRVALKKF LNKRDKWVKD WAGQVVITAS QIQWTADVTK
1710 1720 1730 1740 1750
CLMTAKERSD KKILKVSILN KYSEAIRGNL TKIMRLKIVA LVTIEIHARD
1760 1770 1780 1790 1800
VLEKLYKSGL MDVSSFDWLS QLRFYWEKDV DDCIIRQTNT QFQYGYEYLG
1810 1820 1830 1840 1850
NSGRLVITPL TDRCYMTLTT ALHLHRGGSP KGPAGTGKTE TVKDLGKALG
1860 1870 1880 1890 1900
IYVIVVNCSE GLDYKSMGRM YSGLAQSGAW GCFDEFNRIN IEVLSVVAQQ
1910 1920 1930 1940 1950
ILSILSALTA NLTRFYFEGF EINLVWSCGI FITMNPGYAG RTELPENLKS
1960 1970 1980 1990 2000
MFRPIAMVVP DSTLIAEIIL FGEGFGNCKI LAKKVYTLYS LAVQQLSRQD
2010 2020 2030 2040 2050
HYDFGLRALT SLLRYAGKKR RLQPDLSDEE VLLLSMRDMN IAKLTSVDVP
2060 2070 2080 2090 2100
LFNAIVQDLF PNIELPVIDY GKLRDTIEQE IREMGLQITP FTLTKVLQLY
2110 2120 2130 2140 2150
ETKNSRHSTM IVGGTGSSKT TSWKILQASL TSLCRAGEPN YNIVREFPLN
2160 2170 2180 2190 2200
PKALSLGELY GEYDLNTNEW TDGILSSVMR VACADEKPDE KWILFDGPVD
2210 2220 2230 2240 2250
TLWIESMNSV MDDNKVLTLI NGERIAMPEQ VSLLFEVENL AVASPATVSR
2260 2270 2280 2290 2300
CGMVYTDYVD LGWKPYVQSW LEKRPKTEVE PLQRMFEKFI NKILSFKKDN
2310 2320 2330 2340 2350
CNELVPVPEY SGIISLCKLY TVLATPENGV NPADAENYSF MVEMTFVFSM
2360 2370 2380 2390 2400
IWSVCASVDE DGRKKIDSYL REIEGSFPNK DTVYEYYVNP KMRTWTSFEE
2410 2420 2430 2440 2450
KLPKSWRYPP NAPFYKIMVP TVDTVRYNYL VSTLVANQNP VLLVGPVGTG
2460 2470 2480 2490 2500
KTSIAQSVLQ SLPSSQWSVL VVNMSAQTTS NNVQSIIESR VEKRTKGVYV
2510 2520 2530 2540 2550
PFGGKSMITF MDDLNMPAKD MFGSQPPLEL IRLWIDYGFW YDRVKQSIKH
2560 2570 2580 2590 2600
IRDMFLMAAM GPPGGGRTVI SPRLQSRFNI INMTFPTESQ IIRIFGTMIN
2610 2620 2630 2640 2650
QKLQDFEEEV KPIGNVVTEA TLDVYNTVVQ RFLPTPAKIH YLFNLRDISK
2660 2670 2680 2690 2700
VFQGMLRANK DFHDTKASIT RLWIHECFRV FSDRLVDTAD MEAFMGILSD
2710 2720 2730 2740 2750
KLGTFFDLTF HHLCPNKRPP IFGDFLKEPK VYEDLVDLTV LKTAMETALN
2760 2770 2780 2790 2800
EYNLSPSVVP MQLVLFREAI EHITRIVRVI GQPRGNMLLV GIGGSGRQSL
2810 2820 2830 2840 2850
ARLASSICDY NTFQIEVTKH YRKQEFRDDI KRLYRQAGVE LQTTSFLFVD
2860 2870 2880 2890 2900
TQIADESFLE DINNILSSGE VPNLYKSDEF EEIQNHIIDQ ARAEQIPESS
2910 2920 2930 2940 2950
DSLFAYLIER VRNNLHIVLC LSPVGDPFRN WIRQYPALVN CTTINWFSEW
2960 2970 2980 2990 3000
PREALLEVAE KYIIGVDLGT QENIHRKVAQ IFVTMHWSVA QYSQKMLLEL
3010 3020 3030 3040 3050
RRYNYVTPTN YLELVSGYKK LLGEKRQELL DQANKLRTGL FKIDETREKV
3060 3070 3080 3090 3100
EVMSLELEDA KKKVAEFQKQ CEEYLVIIVQ QKREADEQQK AVTANSEKIA
3110 3120 3130 3140 3150
IEEVKCQALA DNAQKDLEEA LPALEEAMRA LESLNKKDIG EIKSYGRPPA
3160 3170 3180 3190 3200
QVEIVMQAVM ILRGNEPTWA EAKRQLGEQN FIKSLINFDK DNISDKVLKK
3210 3220 3230 3240 3250
IGAYCAQPDF QPDIIGRVSL AAKSLCMWVR AMELYGRLYR VVEPKRIRMN
3260 3270 3280 3290 3300
AAMAQLQEKQ AALAEAQEKL REVAEKLEML KKQYDEKLAQ KEELRKKSEE
3310 3320 3330 3340 3350
MELKLERAGM LVSGLAGEKA RWEETVQGLE EDLGYLVGDC LIAAAFLSYM
3360 3370 3380 3390 3400
GPFLTNYRDE IINQIWIRKI RELQVPCSPR FAIDNFLTNP TKVRDWNIQG
3410 3420 3430 3440 3450
LPSDAFSTEN GIIVTRGNRW ALMIDPQGQA LKWIKNMEGN QGLKIIDLQM
3460 3470 3480 3490 3500
HDYLRVLEHA IQFGFPVLLQ NVQEYLDPTL NPVLNKSVAR IGGRMLIRIG
3510 3520 3530 3540 3550
DKEVEYNPNF RFYLTTKLSN PHYNPETSAK TTIVNFAVKE QGLEAQLLGI
3560 3570 3580 3590 3600
VVRKERPELE EQKDSLVINI AAGKRKLKEL EDEILRLLNE ATGSLLDDVQ
3610 3620 3630 3640 3650
LVNTLQTSKI TATEVTEQLE TSETTEINID LAREAYRPCA QRASVLFFVL
3660 3670 3680 3690 3700
NDMGRIDPMY QFSLDAYIGL FILSIDKSHR SNKLEDRIEY LNDYHTYAVY
3710 3720 3730 3740 3750
RYTCRTLFER HKLLFSFHMC AKILETSGKL NMDEYNFFLR GGVVLDREGQ
3760 3770 3780 3790 3800
MDNPCTSWLA DAYWDNITEL DKLTNFHGLM NSFEQYPRDW HLWYTNSSPE
3810 3820 3830 3840 3850
KAMLPGEWEN ACNEMQRMLI VRSLRQDRVA FCVTSFIVSN LGSRFIEPPV
3860 3870 3880 3890 3900
LNMKSVMEDS TPRSPLVFIL SPGVDPTSAL LQLAEHTGMA HRFHALSLGQ
3910 3920 3930 3940 3950
GQAPIAARLL REGVNQGHWV FLANCHLSLS WMPNLDKLVE QLQVEDPHPS
3960 3970 3980 3990 4000
FRLWLSSSPH PDFPISILQA SIKMTTEPPK GLKANMTRLY QLMTEAQFTH
4010 4020 4030 4040 4050
CSKPAKYKKL LFALCFFHSI LLERKKFLQL GWNIIYGFND SDFEVSENLL
4060 4070 4080 4090 4100
SLYLDEYEET PWDALKYLIA GVNYGGHVTD DWDRRLLTTY INDYFCDLSL
4110 4120 4130 4140 4150
TTPFYRLSVL DTYYIPKDGS LASYKEYISM LPSMDPPEAF GQHPNADVAS
4160 4170 4180 4190 4200
QITEARTLFE TLLSLQPQIT PTRVGGQSRE EKVLELAADV KQKIPEMIDY
4210 4220 4230 4240 4250
EGTRKLLALD PSPLNVVLLQ EIQRYNKLMK TILFSLTDLE KGIQGLIVMS
4260 4270 4280 4290 4300
TSLEEIFNCI FDAHVPPLWG KVYPSQKPLA SWTRDLAVRV EQFETWASRA
4310 4320 4330 4340 4350
RPPVLFWLSG FTFPTGFLTA VLQSAARQNN ISVDSLSWEF IVSTVDDSNL
4360 4370 4380 4390 4400
VYPPKDGVWV RGLYLEGAGW DRKNSCLVEA EPMQLVCLMP TIHFRPAESR
4410 4420 4430 4440 4450
KKSAKGMYSC PCYYYPNRAG STDRASFVIG IDLRSGSMTS DHWIKRGTAL

LMSLDS
Length:4,456
Mass (Da):511,565
Last modified:March 18, 2008 - v1
Checksum:iC57E71F45BDC3C58
GO

Sequence cautioni

The sequence BAC26619 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1893 – 18931V → L in CAB06067 (PubMed:9373155).Curated
Sequence conflicti1895 – 18951S → P in CAB06067 (PubMed:9373155).Curated
Sequence conflicti1898 – 18981A → P in CAB06067 (PubMed:9373155).Curated
Sequence conflicti1900 – 19001Q → K in CAB06067 (PubMed:9373155).Curated
Sequence conflicti1909 – 19091T → S in CAB06067 (PubMed:9373155).Curated
Sequence conflicti2004 – 20041F → Y in CAB06067 (PubMed:9373155).Curated
Sequence conflicti2006 – 20061L → M in CAB06067 (PubMed:9373155).Curated
Sequence conflicti2007 – 20071R → S in CAB06067 (PubMed:9373155).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL596125, AL731687 Genomic DNA. Translation: CAI35997.2.
Z83813 mRNA. Translation: CAB06067.1.
AK029791 mRNA. Translation: BAC26619.1. Different initiation.
UniGeneiMm.247478.

Genome annotation databases

EnsembliENSMUST00000035539; ENSMUSP00000047329; ENSMUSG00000005237.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL596125, AL731687 Genomic DNA. Translation: CAI35997.2.
Z83813 mRNA. Translation: CAB06067.1.
AK029791 mRNA. Translation: BAC26619.1. Different initiation.
UniGeneiMm.247478.

3D structure databases

ProteinModelPortaliP0C6F1.
SMRiP0C6F1. Positions 3042-3671, 3874-4096.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP0C6F1. 1 interaction.
STRINGi10090.ENSMUSP00000104299.

PTM databases

iPTMnetiP0C6F1.
PhosphoSiteiP0C6F1.

Proteomic databases

EPDiP0C6F1.
MaxQBiP0C6F1.
PaxDbiP0C6F1.
PRIDEiP0C6F1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000035539; ENSMUSP00000047329; ENSMUSG00000005237.

Organism-specific databases

MGIiMGI:107731. Dnah2.

Phylogenomic databases

eggNOGiKOG3595. Eukaryota.
COG5245. LUCA.
GeneTreeiENSGT00760000118964.
HOGENOMiHOG000237308.
HOVERGENiHBG104828.
InParanoidiP0C6F1.

Miscellaneous databases

PROiP0C6F1.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000005237.
CleanExiMM_DNAHC2.
ExpressionAtlasiP0C6F1. baseline and differential.
GenevisibleiP0C6F1. MM.

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. 2 hits.
PfamiPF07728. AAA_5. 1 hit.
PF12780. AAA_8. 1 hit.
PF08385. DHC_N1. 2 hits.
PF08393. DHC_N2. 1 hit.
PF03028. Dynein_heavy. 1 hit.
PF12777. MT. 1 hit.
[Graphical view]
SMARTiSM00382. AAA. 2 hits.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 5 hits.
ProtoNetiSearch...

Entry informationi

Entry nameiDYH2_MOUSE
AccessioniPrimary (citable) accession number: P0C6F1
Secondary accession number(s): B1AR18, O08826, Q8C0U5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: March 18, 2008
Last modified: September 7, 2016
This is version 72 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

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.