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Q24246 (DYIN_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 138. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cytoplasmic dynein 1 intermediate chain

Short name=DH IC
Alternative name(s):
Dynein intermediate chain, cytosolic
Protein short wing
Gene names
Name:sw
Synonyms:Cdic, Dic19B
ORF Names:CG18000
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length663 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Acts as one of several non-catalytic accessory components of the cytoplasmic dynein 1 complex that are thought to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function. Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. The intermediate chains mediate the help dynein bind to dynactin 150 kDa component By similarity. Ref.2

Subunit structure

Homodimer By similarity. The cytoplasmic dynein 1 complex consists of two catalytic heavy chains (HCs) and a number of non-catalytic subunits presented by intermediate chains (ICs), light intermediate chains (LICs) and light chains (LCs) By similarity.

Subcellular location

Cytoplasmcytoskeleton Ref.1.

Isoform 2c: Lysosome membrane; Peripheral membrane protein; Cytoplasmic side. Note: Aggregates in cytoplasm around lysosomes. Ref.1

Isoform 2a: Nucleus membrane; Peripheral membrane protein; Cytoplasmic side. Note: Aggregates in cytoplasm around the nucleus. Ref.1

Isoform 2b: Nucleus membrane; Peripheral membrane protein; Cytoplasmic side. Note: Aggregates in cytoplasm around the nucleus. Ref.1

Tissue specificity

High levels of isoform 1b, isoform 1c, isoform 3a and isoform 4 accumulate in early egg chambers and at stage 9 become concentrated at the posterior of the oocyte. Isoform 5a and isoform 5b are highly expressed in adult head and to a lesser extent in adult torso. Isoform 1a, isoform 2a and isoform 2b are found in all tissues examined, including ovaries, midgut, torso and head. Ref.1 Ref.2

Developmental stage

Expressed both maternally and zygotically. Abundant in embryos and adults, low levels in larva and pupae. Isoform 1a, isoform 2a and isoform 2b are constitutively expressed at high levels and isoform 2c at low levels in embryos and adults. Ref.1

Sequence similarities

Belongs to the dynein intermediate chain family.

Contains 7 WD repeats.

Sequence caution

The sequence AAC70942.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence AAC78306.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
   Biological processTransport
   Cellular componentCytoplasm
Cytoskeleton
Dynein
Lysosome
Membrane
Microtubule
Nucleus
   Coding sequence diversityAlternative splicing
   DomainRepeat
WD repeat
   Molecular functionMotor protein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processaxon cargo transport

Inferred from mutant phenotype PubMed 18758451. Source: FlyBase

centrosome localization

Inferred from mutant phenotype PubMed 15888542. Source: FlyBase

cytoplasmic transport

Inferred from mutant phenotype PubMed 16077093. Source: FlyBase

eye photoreceptor cell differentiation

Inferred from genetic interaction PubMed 15329347. Source: FlyBase

protein localization to kinetochore

Inferred from mutant phenotype PubMed 16105886. Source: FlyBase

sperm individualization

Inferred from mutant phenotype PubMed 15829565. Source: FlyBase

spindle organization

Inferred from mutant phenotype PubMed 15888542. Source: FlyBase

   Cellular_componentcytoplasmic dynein complex

Inferred from electronic annotation. Source: InterPro

lysosomal membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

microtubule

Inferred from electronic annotation. Source: UniProtKB-KW

microtubule associated complex

Inferred from direct assay PubMed 18433294. Source: FlyBase

nuclear membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionmotor activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Alternative products

This entry describes 11 isoforms produced by alternative splicing. [Align] [Select]
Isoform 5a (identifier: Q24246-11)

Also known as: J;

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 1a (identifier: Q24246-2)

Also known as: A;

The sequence of this isoform differs from the canonical sequence as follows:
     144-187: VLSCHSSPLSGYMEDWWRPRKAHATDYYDEYNLNPGLEWEDEFT → AHATDYYVLAFDAQG
Isoform 1b (identifier: Q24246-3)

Also known as: B;

The sequence of this isoform differs from the canonical sequence as follows:
     144-187: VLSCHSSPLSGYMEDWWRPRKAHATDYYDEYNLNPGLEWEDEFT → AHATDYYG
Isoform 1c (identifier: Q24246-4)

Also known as: C;

The sequence of this isoform differs from the canonical sequence as follows:
     144-187: VLSCHSSPLSGYMEDWWRPRKAHATDYYDEYNLNPGLEWEDEFT → AHATDYY
Isoform 2a (identifier: Q24246-5)

Also known as: D;

The sequence of this isoform differs from the canonical sequence as follows:
     144-164: Missing.
     187-187: T → TG
Isoform 2b (identifier: Q24246-6)

Also known as: E;

The sequence of this isoform differs from the canonical sequence as follows:
     144-164: Missing.
Isoform 2c (identifier: Q24246-7)

Also known as: F;

The sequence of this isoform differs from the canonical sequence as follows:
     144-164: Missing.
     187-187: T → TVLAFDAQG
Isoform 3a (identifier: Q24246-8)

Also known as: G;

The sequence of this isoform differs from the canonical sequence as follows:
     144-171: Missing.
     187-187: T → TG
Isoform 3b (identifier: Q24246-9)

Also known as: H;

The sequence of this isoform differs from the canonical sequence as follows:
     144-171: Missing.
Isoform 4 (identifier: Q24246-10)

Also known as: I;

The sequence of this isoform differs from the canonical sequence as follows:
     146-187: SCHSSPLSGYMEDWWRPRKAHATDYYDEYNLNPGLEWEDEFT → AFDAQG
Isoform 5b (identifier: Q24246-12)

Also known as: K;

The sequence of this isoform differs from the canonical sequence as follows:
     144-153: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 663663Cytoplasmic dynein 1 intermediate chain
PRO_0000114661

Regions

Repeat311 – 36050WD 1
Repeat364 – 40441WD 2
Repeat413 – 45442WD 3
Repeat463 – 50341WD 4
Repeat508 – 55346WD 5
Repeat556 – 59641WD 6
Repeat602 – 64140WD 7

Natural variations

Alternative sequence144 – 18744VLSCH…EDEFT → AHATDYYVLAFDAQG in isoform 1a.
VSP_001345
Alternative sequence144 – 18744VLSCH…EDEFT → AHATDYYG in isoform 1b.
VSP_001346
Alternative sequence144 – 18744VLSCH…EDEFT → AHATDYY in isoform 1c.
VSP_001347
Alternative sequence144 – 17128Missing in isoform 3a and isoform 3b.
VSP_001342
Alternative sequence144 – 16421Missing in isoform 2a, isoform 2b and isoform 2c.
VSP_007686
Alternative sequence144 – 15310Missing in isoform 5b.
VSP_007685
Alternative sequence146 – 18742SCHSS…EDEFT → AFDAQG in isoform 4.
VSP_001343
Alternative sequence1871T → TG in isoform 2a and isoform 3a.
VSP_001348
Alternative sequence1871T → TVLAFDAQG in isoform 2c.
VSP_007687

Experimental info

Sequence conflict471D → G in AAC78306. Ref.1
Sequence conflict471D → G in AAC70933. Ref.1
Sequence conflict471D → G in AAC70934. Ref.1
Sequence conflict471D → G in AAC70935. Ref.1
Sequence conflict471D → G in AAC70936. Ref.1
Sequence conflict471D → G in AAC70937. Ref.1
Sequence conflict471D → G in AAC70938. Ref.1
Sequence conflict471D → G in AAC70939. Ref.1
Sequence conflict471D → G in AAC70940. Ref.1
Sequence conflict471D → G in AAC70941. Ref.1
Sequence conflict471D → G in AAC70942. Ref.1
Sequence conflict471D → G in AAC70943. Ref.1
Sequence conflict139 – 1457GGNGDVL → AETAMV in AAB51185. Ref.6
Sequence conflict2351V → L in AAB51185. Ref.6
Sequence conflict296 – 2972HA → SM in AAB51185. Ref.6
Sequence conflict521 – 5222NQ → KP in AAB51185. Ref.6
Sequence conflict537 – 54812DWTIK…SLKDT → KIWSLKLPISSCQFSVVSGI NSN in AAB51185. Ref.6
Sequence conflict5791G → A in AAB51185. Ref.6
Sequence conflict5931E → K in AAB51185. Ref.6
Sequence conflict6281L → Q in AAB51185. Ref.6
Sequence conflict645 – 66319WSRFN…QSDEV → IKMNQSVRSRTI in AAB51185. Ref.6

Secondary structure

......... 663
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 5a (J) [UniParc].

Last modified July 3, 2003. Version 3.
Checksum: 4C726D4C5F47FAF7

FASTA66373,917
        10         20         30         40         50         60 
MDRKAELERK KAKLAALREE KDRRRREKEI KDMEEAAGRI GGGAGIDKDQ RKDLDEMLSS 

        70         80         90        100        110        120 
LGVAPVSEVL SSLSSVNSMT SDNSNTQTPD ASLQATVNGQ SGGKKQPLNL SVYNVQATNI 

       130        140        150        160        170        180 
PPKETLVYTK QTQTTSTGGG NGDVLSCHSS PLSGYMEDWW RPRKAHATDY YDEYNLNPGL 

       190        200        210        220        230        240 
EWEDEFTDDE ESSLQNLGNG FTSKLPPGYL THGLPTVKDV APAITPLEIK KETEVKKEVN 

       250        260        270        280        290        300 
ELSEEQKQMI ILSENFQRFV VRAGRVIERA LSENVDIYTD YIGGGDSEEA NDERSHARLS 

       310        320        330        340        350        360 
LNRVFYDERW SKNRCITSMD WSTHFPELVV GSYHNNEESP NEPDGVVMVW NTKFKKSTPE 

       370        380        390        400        410        420 
DVFHCQSAVM STCFAKFNPN LILGGTYSGQ IVLWDNRVQK RTPIQRTPLS AAAHTHPVYC 

       430        440        450        460        470        480 
LQMVGTQNAH NVISISSDGK LCSWSLDMLS QPQDTLELQQ RQSKAIAITS MAFPANEINS 

       490        500        510        520        530        540 
LVMGSEDGYV YSASRHGLRS GVNEVYERHL GPITGISTHY NQLSPDFGHL FLTSSIDWTI 

       550        560        570        580        590        600 
KLWSLKDTKP LYSFEDNSDY VMDVAWSPVH PALFAAVDGS GRLDLWNLNQ DTEVPTASIV 

       610        620        630        640        650        660 
VAGAPALNRV SWTPSGLHVC IGDEAGKLYV YDVAENLAQP SRDEWSRFNT HLSEIKMNQS 


DEV 

« Hide

Isoform 1a (A) [UniParc].

Checksum: F3267D4090F25E05
Show »

FASTA63470,249
Isoform 1b (B) [UniParc].

Checksum: AB436F70A431915B
Show »

FASTA62769,505
Isoform 1c (C) [UniParc].

Checksum: D96D9CD9AA89814A
Show »

FASTA62669,447
Isoform 2a (D) [UniParc].

Checksum: 900A25F62B24A451
Show »

FASTA64371,458
Isoform 2b (E) [UniParc].

Checksum: 10271A56BFBC8B62
Show »

FASTA64271,400
Isoform 2c (F) [UniParc].

Checksum: 937440311CA820DE
Show »

FASTA65072,202
Isoform 3a (G) [UniParc].

Checksum: 10882999594FBDD9
Show »

FASTA63670,636
Isoform 3b (H) [UniParc].

Checksum: 422B7524D4A50381
Show »

FASTA63570,579
Isoform 4 (I) [UniParc].

Checksum: 6D17F8435B8C8BF8
Show »

FASTA62769,428
Isoform 5b (K) [UniParc].

Checksum: 3073C8F8F3B2FB59
Show »

FASTA65372,906

References

« Hide 'large scale' references
[1]"Cytoplasmic dynein intermediate-chain isoforms with different targeting properties created by tissue-specific alternative splicing."
Nurminsky D.I., Nurminskaya M.V., Benevolenskaya E.V., Shevelyov Y.Y., Hartl D.L., Gvozdev V.A.
Mol. Cell. Biol. 18:6816-6825(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1A; 1B; 1C; 2A; 2B; 2C; 3A; 3B; 4; 5A AND 5B), SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
Tissue: Ovary.
[2]"A molecular genetic analysis of the interaction between the cytoplasmic dynein intermediate chain and the glued (Dynactin) complex."
Boylan K., Serr M., Hays T.S.
Mol. Biol. Cell 11:3791-3803(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2B), FUNCTION, TISSUE SPECIFICITY.
Tissue: Ovary.
[3]"The genome sequence of Drosophila melanogaster."
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. expand/collapse author list , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Berkeley.
[4]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. expand/collapse author list , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING.
Strain: Berkeley.
[5]Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M., Park S., Wan K.H., Yu C., Rubin G.M., Celniker S.E.
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1B).
Strain: Berkeley.
Tissue: Embryo.
[6]"Cluster of tandem repeats in Drosophila genome comprising putative genes encoding cytoplasmic dynein intermediate chain and 3'-part of annexin X."
Benevolenskaya E.V., Gvozdev V.A.
Submitted (MAY-1995) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 101-663 (ISOFORM 4).
Strain: GT WA.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF070687 Genomic DNA. Translation: AAC78306.1. Sequence problems.
AF070689 mRNA. Translation: AAC70933.1.
AF070690 mRNA. Translation: AAC70934.1.
AF070691 mRNA. Translation: AAC70935.1.
AF070692 mRNA. Translation: AAC70936.1.
AF070693 mRNA. Translation: AAC70937.1.
AF070694 mRNA. Translation: AAC70938.1.
AF070695 mRNA. Translation: AAC70939.1.
AF070696 mRNA. Translation: AAC70940.1.
AF070697 mRNA. Translation: AAC70941.1.
AF070698 mRNA. Translation: AAC70942.1. Sequence problems.
AF070699 mRNA. Translation: AAC70943.1.
AF263371 mRNA. Translation: AAF73046.1.
AE014298 Genomic DNA. Translation: AAF50928.2.
AE014298 Genomic DNA. Translation: AAN09553.1.
AE014298 Genomic DNA. Translation: AAN09554.1.
AE014298 Genomic DNA. Translation: AAN09555.1.
AE014298 Genomic DNA. Translation: AAN09556.1.
AE014298 Genomic DNA. Translation: AAN09557.1.
AE014298 Genomic DNA. Translation: AAN09558.1.
AE014298 Genomic DNA. Translation: AAN09559.1.
AE014298 Genomic DNA. Translation: AAN09560.1.
AE014298 Genomic DNA. Translation: AAN09561.1.
AE014298 Genomic DNA. Translation: AAN09562.1.
BT016101 mRNA. Translation: AAV36986.1.
L41945 Genomic DNA. Translation: AAB51185.1.
RefSeqNP_477069.1. NM_057721.3.
NP_477070.1. NM_057722.3.
NP_477071.1. NM_057723.3.
NP_477072.1. NM_057724.3.
NP_477073.1. NM_057725.3.
NP_477074.1. NM_057726.3.
NP_477075.2. NM_057727.4.
NP_477076.1. NM_057728.3.
NP_477077.1. NM_057729.3.
NP_477078.1. NM_057730.4.
NP_477079.1. NM_057731.3.
NP_996521.1. NM_206798.1.
NP_996522.1. NM_206799.1.
UniGeneDm.20780.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2P2TX-ray3.00C123-138[»]
3FM7X-ray3.50C/D109-135[»]
3L9KX-ray3.00W/X/Y/Z242-279[»]
ProteinModelPortalQ24246.
SMRQ24246. Positions 109-135, 242-279, 320-637.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-19664N.
IntActQ24246. 1 interaction.
MINTMINT-1717948.

Proteomic databases

PaxDbQ24246.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0089406; FBpp0088428; FBgn0003654.
GeneID44160.
KEGGdme:Dmel_CG18000.

Organism-specific databases

CTD44160.
FlyBaseFBgn0003654. sw.

Phylogenomic databases

eggNOGNOG308180.
GeneTreeENSGT00690000101848.
InParanoidQ24246.
KOK10415.
OMASAGHEDS.
OrthoDBEOG4WWQ0J.
PhylomeDBQ24246.

Gene expression databases

BgeeQ24246.
GermOnlineCG18000. Drosophila melanogaster.

Family and domain databases

Gene3D2.130.10.10. 1 hit.
InterProIPR025956. Dynein_IC_1/2.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamPF11540. Dynein_IC2. 1 hit.
PF00400. WD40. 1 hit.
[Graphical view]
SMARTSM00320. WD40. 6 hits.
[Graphical view]
SUPFAMSSF50978. WD40_like. 1 hit.
PROSITEPS00678. WD_REPEATS_1. False negative.
PS50082. WD_REPEATS_2. 1 hit.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSLC4A1. drosophila.
EvolutionaryTraceQ24246.
GenomeRNAi44160.
NextBio836907.

Entry information

Entry nameDYIN_DROME
AccessionPrimary (citable) accession number: Q24246
Secondary accession number(s): O96508 expand/collapse secondary AC list , O96510, O96511, O96512, O96513, O96514, O96515, O96516, Q5U0Z1, Q86BQ5, Q9NG49, Q9TZR7, Q9TZR8, Q9TZR9, Q9TZS0, Q9VR78
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 3, 2003
Last modified: May 1, 2013
This is version 138 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families