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Q921C5 (BICD2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 100. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein bicaudal D homolog 2

Short name=Bic-D 2
Gene names
Name:Bicd2
Synonyms:Kiaa0699
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length820 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May play a role in the dynein-dynactin interactions on the surface of membranous organelles, by associating with these complexes. Regulates coat complex coatomer protein I (COPI)-independent Golgi-endoplasmic reticulum transport by recruiting the dynein-dynactin motor complex.

Subunit structure

Interacts with NEK9 By similarity. Interacts with DCTN2 and RAB6A. Interacs with DNAI1 By similarity.

Subcellular location

Golgi apparatus. Cytoplasmcytoskeleton. Note: In interphase cells mainly localizes to the Golgi complex and colocalizes with dynactin at microtubule plus ends.

Tissue specificity

Ubiquitously expressed with high expression in the spinal cord. Ref.7

Domain

The fourth coiled coil region is involved in Golgi targeting and in the interaction with DCTN2.

Post-translational modification

Phosphorylated by NEK9 in vitro By similarity.

Sequence similarities

Belongs to the BicD family.

Sequence caution

The sequence BAC65630.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Isoform 3: The sequence BAB22282.1 differs from that shown. Reason: Frameshift at position 70.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Rab6aP352793EBI-642984,EBI-444674

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q921C5-1)

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: Q921C5-2)

The sequence of this isoform differs from the canonical sequence as follows:
     820-820: L → VSHTCACASERAEGAGLANQVFCSEKHSIYCD
Note: No experimental confirmation available.
Isoform 3 (identifier: Q921C5-3)

The sequence of this isoform differs from the canonical sequence as follows:
     328-338: APPSPSLVSDL → VHPLHALCLTV
     339-820: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 820819Protein bicaudal D homolog 2
PRO_0000205360

Regions

Region662 – 804143Interacts with RAB6A
Coiled coil20 – 270251 Potential
Coiled coil340 – 539200 Potential
Coiled coil662 – 804143 Potential

Amino acid modifications

Modified residue21N-acetylserine By similarity
Modified residue1901Phosphoserine By similarity
Modified residue2241Phosphoserine By similarity
Modified residue3451Phosphoserine By similarity
Modified residue3971Phosphoserine By similarity
Modified residue5781Phosphoserine By similarity
Modified residue8191Phosphoserine By similarity

Natural variations

Alternative sequence328 – 33811APPSPSLVSDL → VHPLHALCLTV in isoform 3.
VSP_007971
Alternative sequence339 – 820482Missing in isoform 3.
VSP_007972
Alternative sequence8201L → VSHTCACASERAEGAGLANQ VFCSEKHSIYCD in isoform 2.
VSP_007970

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: 0C1A1754CD74DDE1

FASTA82093,391
        10         20         30         40         50         60 
MSAPSEEEEY ARLVMEAQPE WLRAEVKRLS HELAETTREK IQAAEYGLAV LEEKHQLKLQ 

        70         80         90        100        110        120 
FEELEVDYEA IRSEMEQLKE AFGQAHTNHK KVAADGESRE ESLIQESASK EQYYVRKVLE 

       130        140        150        160        170        180 
LQTELKQLRN VLTNTQSENE RLTSVAQELK EINQNVEIQR GRLRDDIKEY KFREARLLQD 

       190        200        210        220        230        240 
YSELEEENIS LQKQVSVLRQ NQVEFEGLKH EIKRLEEETE YLNSQLEDAI RLKEISERQL 

       250        260        270        280        290        300 
EEALETLKTE REQKNNLRKE LSHYMSINDS FYTSHLQVSL DGLKFSDDTV TAEPNNDAEA 

       310        320        330        340        350        360 
LVNGFEHSGL VKSSLDNKTS TPRKDGLAPP SPSLVSDLLS ELHISEIQKL KQQLVQMERE 

       370        380        390        400        410        420 
KVGLLATLQD TQKQLEQARG TLSEQHEKVN RLTENLSALR RLQAGKERQT SLDNEKDRDS 

       430        440        450        460        470        480 
HEDGDYYEVD INGPEILACK YHVAVAEAGE LREQLKALRS THEAREAQHA EEKGRYEAEG 

       490        500        510        520        530        540 
QALTEKISLL EKASHQDREL LAHLEKELKK VSDVAGETQG SLNVAQDELV TFSEELANLY 

       550        560        570        580        590        600 
HHVCMCNNET PNRVMLDYYR EGQGKAGRTS PEGRGRRSPV LLPKGLLATE VGRADGGTGD 

       610        620        630        640        650        660 
NSPSPSSSLP SPLSDPRREP MNIYNLIAII RDQIKHLQAA VDRTTELSRQ RIASQELGPA 

       670        680        690        700        710        720 
VDKDKEALME EILKLKSLLS TKREQITTLR TVLKANKQTA EVALANLKSK YENEKAMVTE 

       730        740        750        760        770        780 
TMMKLRNELK ALKEDAATFS SLRAMFATRC DEYITQLDEM QRQLAAAEDE KKTLNSLLRM 

       790        800        810        820 
AIQQKLALTQ RLELLELDHE QTRRGRSKAA SKAKPASPSL 

« Hide

Isoform 2 [UniParc].

Checksum: 25A80CD34D97587F
Show »

FASTA85196,647
Isoform 3 [UniParc].

Checksum: E2DF08B87A283BFE
Show »

FASTA33839,315

References

« Hide 'large scale' references
[1]"Mammalian Golgi-associated Bicaudal-D2 functions in the dynein-dynactin pathway by interacting with these complexes."
Hoogenraad C.C., Akhmanova A., Howell S.A., Dortland B.R., de Zeeuw C.I., Willemsen R., Visser P., Grosveld F., Galjart N.
EMBO J. 20:4041-4054(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CHARACTERIZATION.
[2]"Prediction of the coding sequences of mouse homologues of KIAA gene: II. The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S., Nakajima D., Nagase T., Ohara O., Koga H.
DNA Res. 10:35-48(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Brain.
[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 1).
Tissue: Mammary tumor.
[4]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: PARTIAL NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
Strain: C57BL/6J.
Tissue: Embryo and Kidney.
[5]"Bicaudal-D regulates COPI-independent Golgi-ER transport by recruiting the dynein-dynactin motor complex."
Matanis T., Akhmanova A., Wulf P., Del Nery E., Weide T., Stepanova T., Galjart N., Grosveld F., Goud B., De Zeeuw C.I., Barnekow A., Hoogenraad C.C.
Nat. Cell Biol. 4:986-992(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
[6]"Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
[7]"Molecular defects in the motor adaptor BICD2 cause proximal spinal muscular atrophy with autosomal-dominant inheritance."
Peeters K., Litvinenko I., Asselbergh B., Almeida-Souza L., Chamova T., Geuens T., Ydens E., Zimon M., Irobi J., De Vriendt E., De Winter V., Ooms T., Timmerman V., Tournev I., Jordanova A.
Am. J. Hum. Genet. 92:955-964(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ250106 mRNA. Translation: CAC51393.1.
AK122348 mRNA. Translation: BAC65630.1. Different initiation.
BC032198 mRNA. Translation: AAH32198.1.
AK002683 mRNA. Translation: BAB22282.1. Frameshift.
AK003456 mRNA. Translation: BAC25035.1.
CCDSCCDS36656.1. [Q921C5-1]
CCDS36657.1. [Q921C5-2]
RefSeqNP_001034268.1. NM_001039179.2. [Q921C5-2]
NP_001034269.1. NM_001039180.2.
NP_084067.1. NM_029791.4. [Q921C5-1]
UniGeneMm.197387.

3D structure databases

ProteinModelPortalQ921C5.
SMRQ921C5. Positions 712-793.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid218383. 1 interaction.
DIPDIP-49453N.
IntActQ921C5. 4 interactions.
MINTMINT-1572114.

PTM databases

PhosphoSiteQ921C5.

Proteomic databases

MaxQBQ921C5.
PaxDbQ921C5.
PRIDEQ921C5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000048544; ENSMUSP00000039394; ENSMUSG00000037933. [Q921C5-2]
ENSMUST00000110085; ENSMUSP00000105712; ENSMUSG00000037933. [Q921C5-1]
GeneID76895.
KEGGmmu:76895.
UCSCuc007qjg.1. mouse. [Q921C5-1]
uc007qji.1. mouse. [Q921C5-2]

Organism-specific databases

CTD23299.
MGIMGI:1924145. Bicd2.
RougeSearch...

Phylogenomic databases

eggNOGNOG291306.
GeneTreeENSGT00390000004114.
HOGENOMHOG000261658.
HOVERGENHBG050686.
OMARNVLTNT.
OrthoDBEOG7BZVRK.
PhylomeDBQ921C5.
TreeFamTF323833.

Gene expression databases

ArrayExpressQ921C5.
BgeeQ921C5.
CleanExMM_BICD2.
GenevestigatorQ921C5.

Family and domain databases

InterProIPR018477. Bicaudal-D_microtubule-assoc.
[Graphical view]
PANTHERPTHR31233. PTHR31233. 1 hit.
PfamPF09730. BicD. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio346027.
PROQ921C5.
SOURCESearch...

Entry information

Entry nameBICD2_MOUSE
AccessionPrimary (citable) accession number: Q921C5
Secondary accession number(s): Q80TU1, Q8BTE3, Q9DCL3
Entry history
Integrated into UniProtKB/Swiss-Prot: August 15, 2003
Last sequence update: December 1, 2001
Last modified: July 9, 2014
This is version 100 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot