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Protein bicaudal D homolog 2 (Bic-D 2)

 BICD2_HUMAN             Reviewed;         824 AA.
Q8TD16; O75181; Q5TBQ2; Q5TBQ3; Q96LH2; Q9BT84; Q9H561;
15-AUG-2003, integrated into UniProtKB/Swiss-Prot.
01-JUN-2002, sequence version 1.
27-SEP-2017, entry version 137.
RecName: Full=Protein bicaudal D homolog 2;
Short=Bic-D 2;
Name=BICD2; Synonyms=KIAA0699;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH NEK9,
PHOSPHORYLATION BY NEK9, AND SUBCELLULAR LOCATION.
PubMed=11864968; DOI=10.1074/jbc.M108662200;
Holland P.M., Milne A., Garka K., Johnson R.S., Willis C., Sims J.E.,
Rauch C.T., Bird T.A., Virca G.D.;
"Purification, cloning, and characterization of Nek8, a novel NIMA-
related kinase, and its candidate substrate Bicd2.";
J. Biol. Chem. 277:16229-16240(2002).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Brain;
PubMed=9734811; DOI=10.1093/dnares/5.3.169;
Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H.,
Nomura N., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. X.
The complete sequences of 100 new cDNA clones from brain which can
code for large proteins in vitro.";
DNA Res. 5:169-176(1998).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164053; DOI=10.1038/nature02465;
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
Rogers J., Dunham I.;
"DNA sequence and analysis of human chromosome 9.";
Nature 429:369-374(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 239-824 (ISOFORM 1).
TISSUE=Pancreas, and Skin;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-582, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=15144186; DOI=10.1021/ac035352d;
Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,
Peters E.C.;
"Robust phosphoproteomic profiling of tyrosine phosphorylation sites
from human T cells using immobilized metal affinity chromatography and
tandem mass spectrometry.";
Anal. Chem. 76:2763-2772(2004).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-582, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-190; SER-224; SER-343;
SER-395 AND SER-582, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-190; THR-821 AND
SER-823, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[9]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[11]
INTERACTION WITH RANBP2, AND SUBCELLULAR LOCATION.
PubMed=20386726; DOI=10.1371/journal.pbio.1000350;
Splinter D., Tanenbaum M.E., Lindqvist A., Jaarsma D., Flotho A.,
Yu K.L., Grigoriev I., Engelsma D., Haasdijk E.D., Keijzer N.,
Demmers J., Fornerod M., Melchior F., Hoogenraad C.C., Medema R.H.,
Akhmanova A.;
"Bicaudal D2, dynein, and kinesin-1 associate with nuclear pore
complexes and regulate centrosome and nuclear positioning during
mitotic entry.";
PLoS Biol. 8:E1000350-E1000350(2010).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-582, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-582, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[15]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-224; SER-318; THR-319;
SER-568; SER-574; SER-582 AND THR-602, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-582, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[18]
INTERACTION WITH KIF1C.
PubMed=24482476; DOI=10.1126/science.1247363;
Novarino G., Fenstermaker A.G., Zaki M.S., Hofree M., Silhavy J.L.,
Heiberg A.D., Abdellateef M., Rosti B., Scott E., Mansour L.,
Masri A., Kayserili H., Al-Aama J.Y., Abdel-Salam G.M., Karminejad A.,
Kara M., Kara B., Bozorgmehri B., Ben-Omran T., Mojahedi F.,
Mahmoud I.G., Bouslam N., Bouhouche A., Benomar A., Hanein S.,
Raymond L., Forlani S., Mascaro M., Selim L., Shehata N.,
Al-Allawi N., Bindu P.S., Azam M., Gunel M., Caglayan A., Bilguvar K.,
Tolun A., Issa M.Y., Schroth J., Spencer E.G., Rosti R.O., Akizu N.,
Vaux K.K., Johansen A., Koh A.A., Megahed H., Durr A., Brice A.,
Stevanin G., Gabriel S.B., Ideker T., Gleeson J.G.;
"Exome sequencing links corticospinal motor neuron disease to common
neurodegenerative disorders.";
Science 343:506-511(2014).
[19]
FUNCTION.
PubMed=25962623; DOI=10.1016/j.bbamcr.2015.05.005;
Matsuto M., Kano F., Murata M.;
"Reconstitution of the targeting of Rab6A to the Golgi apparatus in
semi-intact HeLa cells: A role of BICD2 in stabilizing Rab6A on Golgi
membranes and a concerted role of Rab6A/BICD2 interactions in Golgi-
to-ER retrograde transport.";
Biochim. Biophys. Acta 1853:2592-2609(2015).
[20]
INTERACTION WITH DYNC1H1.
PubMed=25512093; DOI=10.1002/humu.22744;
Peeters K., Bervoets S., Chamova T., Litvinenko I., De Vriendt E.,
Bichev S., Kancheva D., Mitev V., Kennerson M., Timmerman V.,
De Jonghe P., Tournev I., MacMillan J., Jordanova A.;
"Novel mutations in the DYNC1H1 tail domain refine the genetic and
clinical spectrum of dyneinopathies.";
Hum. Mutat. 36:287-291(2015).
[21]
VARIANTS SMALED2 LEU-107 AND GLY-774, CHARACTERIZATION OF VARIANTS
SMALED2 LEU-107 AND GLY-774, INTERACTION WITH DNAI1 AND RAB6A, AND
SUBCELLULAR LOCATION.
PubMed=23664119; DOI=10.1016/j.ajhg.2013.04.013;
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.;
"Molecular defects in the motor adaptor BICD2 cause proximal spinal
muscular atrophy with autosomal-dominant inheritance.";
Am. J. Hum. Genet. 92:955-964(2013).
[22]
VARIANTS SMALED2 LEU-107; PHE-189; PRO-501 AND THR-508,
CHARACTERIZATION OF VARIANTS SMALED2 LEU-107 AND PRO-501, INTERACTION
WITH DNAI1, AND SUBCELLULAR LOCATION.
PubMed=23664120; DOI=10.1016/j.ajhg.2013.04.018;
UK10K;
Oates E.C., Rossor A.M., Hafezparast M., Gonzalez M., Speziani F.,
Macarthur D.G., Lek M., Cottenie E., Scoto M., Foley A.R., Hurles M.,
Houlden H., Greensmith L., Auer-Grumbach M., Pieber T.R., Strom T.M.,
Schule R., Herrmann D.N., Sowden J.E., Acsadi G., Menezes M.P.,
Clarke N.F., Zuechner S., Muntoni F., North K.N., Reilly M.M.;
"Mutations in BICD2 cause dominant congenital spinal muscular atrophy
and hereditary spastic paraplegia.";
Am. J. Hum. Genet. 92:965-973(2013).
[23]
VARIANTS SMALED2 LEU-107; THR-188 AND MET-703, CHARACTERIZATION OF
VARIANTS SMALED2 LEU-107; THR-188 AND MET-703, VARIANT ARG-90, AND
SUBCELLULAR LOCATION.
PubMed=23664116; DOI=10.1016/j.ajhg.2013.04.011;
Neveling K., Martinez-Carrera L.A., Hoelker I., Heister A.,
Verrips A., Hosseini-Barkooie S.M., Gilissen C., Vermeer S.,
Pennings M., Meijer R., Te Riele M., Frijns C.J., Suchowersky O.,
Maclaren L., Rudnik-Schoeneborn S., Sinke R.J., Zerres K., Lowry R.B.,
Lemmink H.H., Garbes L., Veltman J.A., Schelhaas H.J., Scheffer H.,
Wirth B.;
"Mutations in BICD2, which encodes a golgin and important motor
adaptor, cause congenital autosomal-dominant spinal muscular
atrophy.";
Am. J. Hum. Genet. 92:946-954(2013).
-!- FUNCTION: Acts as an adapter protein linking the dynein motor
complex to various cargos and converts dynein from a non-
processive to a highly processive motor in the presence of
dynactin. Facilitates and stabilizes the interaction between
dynein and dynactin and activates dynein processivity (the ability
to move along a microtubule for a long distance without falling
off the track) (By similarity). Facilitates the binding of RAB6A
to the Golgi by stabilizing its GTP-bound form. Regulates coat
complex coatomer protein I (COPI)-independent Golgi-endoplasmic
reticulum transport via its interaction with RAB6A and recruitment
of the dynein-dynactin motor complex (PubMed:25962623).
Contributes to nuclear and centrosomal positioning prior to
mitotic entry through regulation of both dynein and kinesin-1.
During G2 phase of the cell cycle, associates with RANBP2 at the
nuclear pores and recruits dynein and dynactin to the nuclear
envelope to ensure proper positioning of the nucleus relative to
centrosomes prior to the onset of mitosis (By similarity).
{ECO:0000250|UniProtKB:Q921C5, ECO:0000269|PubMed:25962623}.
-!- SUBUNIT: Interacts with CPNE4 (via VWFA domain) (By similarity).
Interacts with RAB6A (PubMed:23664119). Interacts with NEK9
(PubMed:11864968). Interacts with DNAI1 (PubMed:23664119,
PubMed:23664120). Interacts with DYNC1H1 (PubMed:25512093).
Interacts with RANBP2 (PubMed:20386726). Forms a complex with
dynein and dynactin. Binds preferentially to tyrosinated
microtubules than to detyrosinated microtubules. Interacts with
DYNLL1, DYNC1I2; DCTN1, DCTN2 and KIF5A (By similarity). Interacts
with KIF1C (PubMed:24482476). {ECO:0000250|UniProtKB:Q921C5,
ECO:0000269|PubMed:11864968, ECO:0000269|PubMed:20386726,
ECO:0000269|PubMed:23664119, ECO:0000269|PubMed:23664120,
ECO:0000269|PubMed:24482476, ECO:0000269|PubMed:25512093}.
-!- INTERACTION:
Q9Y247:FAM50B; NbExp=4; IntAct=EBI-11975051, EBI-742802;
Q15560:TCEA2; NbExp=4; IntAct=EBI-11975051, EBI-710310;
-!- SUBCELLULAR LOCATION: Golgi apparatus
{ECO:0000269|PubMed:23664116, ECO:0000269|PubMed:23664119}.
Cytoplasm, cytoskeleton {ECO:0000269|PubMed:11864968}. Cytoplasm
{ECO:0000269|PubMed:23664116, ECO:0000269|PubMed:23664120}.
Nucleus envelope {ECO:0000269|PubMed:20386726}. Nucleus, nuclear
pore complex {ECO:0000269|PubMed:20386726}. Note=In interphase
cells mainly localizes to the Golgi complex and colocalizes with
dynactin at microtubule plus ends (By similarity). Localizes to
the nuclear envelope and cytoplasmic stacks of nuclear pore
complex known as annulate lamellae in a RANBP2-dependent manner
during G2 phase of the cell cycle (PubMed:20386726).
{ECO:0000250|UniProtKB:Q921C5, ECO:0000269|PubMed:11864968,
ECO:0000269|PubMed:20386726}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q8TD16-1; Sequence=Displayed;
Name=2;
IsoId=Q8TD16-2; Sequence=VSP_007969;
Note=Due to intron retention. No experimental confirmation
available.;
-!- TISSUE SPECIFICITY: Ubiquitous.
-!- DOMAIN: The fourth coiled coil region is involved in Golgi
targeting and in the interaction with DCTN2.
{ECO:0000250|UniProtKB:Q921C5}.
-!- PTM: Phosphorylated by NEK9 in vitro.
{ECO:0000269|PubMed:11864968}.
-!- DISEASE: Spinal muscular atrophy, lower extremity-predominant 2,
autosomal dominant (SMALED2) [MIM:615290]: An autosomal dominant
form of spinal muscular atrophy characterized by early-childhood
onset of muscle weakness and atrophy predominantly affecting the
proximal and distal muscles of the lower extremity, although some
patients may show upper extremity involvement. The disorder
results in delayed walking, waddling gait, difficulty walking, and
loss of distal reflexes. Some patients may have foot deformities
or hyperlordosis, and some show mild upper motor signs, such as
spasticity. Sensation, bulbar function, and cognitive function are
preserved. The disorder shows very slow progression throughout
life. {ECO:0000269|PubMed:23664116, ECO:0000269|PubMed:23664119,
ECO:0000269|PubMed:23664120}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the BicD family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAA31674.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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EMBL; AY052562; AAL12246.1; -; mRNA.
EMBL; AB014599; BAA31674.1; ALT_INIT; mRNA.
EMBL; AL137074; CAI14369.1; -; Genomic_DNA.
EMBL; AL136981; CAI14369.1; JOINED; Genomic_DNA.
EMBL; AL137074; CAI14370.1; -; Genomic_DNA.
EMBL; AL136981; CAI14370.1; JOINED; Genomic_DNA.
EMBL; AL136981; CAI41013.1; -; Genomic_DNA.
EMBL; AL137074; CAI41013.1; JOINED; Genomic_DNA.
EMBL; AL136981; CAI41014.1; -; Genomic_DNA.
EMBL; AL137074; CAI41014.1; JOINED; Genomic_DNA.
EMBL; BC004296; AAH04296.1; -; mRNA.
EMBL; BC073970; AAH73970.1; -; mRNA.
CCDS; CCDS35064.1; -. [Q8TD16-2]
CCDS; CCDS6700.1; -. [Q8TD16-1]
RefSeq; NP_001003800.1; NM_001003800.1. [Q8TD16-2]
RefSeq; NP_056065.1; NM_015250.3. [Q8TD16-1]
UniGene; Hs.436939; -.
ProteinModelPortal; Q8TD16; -.
SMR; Q8TD16; -.
BioGrid; 116891; 40.
DIP; DIP-53426N; -.
IntAct; Q8TD16; 51.
MINT; MINT-5006473; -.
STRING; 9606.ENSP00000349351; -.
iPTMnet; Q8TD16; -.
PhosphoSitePlus; Q8TD16; -.
BioMuta; BICD2; -.
DMDM; 34098604; -.
EPD; Q8TD16; -.
MaxQB; Q8TD16; -.
PaxDb; Q8TD16; -.
PeptideAtlas; Q8TD16; -.
PRIDE; Q8TD16; -.
Ensembl; ENST00000356884; ENSP00000349351; ENSG00000185963. [Q8TD16-2]
Ensembl; ENST00000375512; ENSP00000364662; ENSG00000185963. [Q8TD16-1]
GeneID; 23299; -.
KEGG; hsa:23299; -.
UCSC; uc004aso.2; human. [Q8TD16-1]
CTD; 23299; -.
DisGeNET; 23299; -.
EuPathDB; HostDB:ENSG00000185963.13; -.
GeneCards; BICD2; -.
HGNC; HGNC:17208; BICD2.
HPA; HPA023013; -.
HPA; HPA024452; -.
MalaCards; BICD2; -.
MIM; 609797; gene.
MIM; 615290; phenotype.
neXtProt; NX_Q8TD16; -.
OpenTargets; ENSG00000185963; -.
Orphanet; 363454; Autosomal dominant childhood-onset proximal spinal muscular atrophy with contractures.
PharmGKB; PA134969018; -.
eggNOG; KOG0999; Eukaryota.
eggNOG; ENOG410XR47; LUCA.
GeneTree; ENSGT00390000004114; -.
HOVERGEN; HBG050686; -.
InParanoid; Q8TD16; -.
KO; K18739; -.
OMA; DRDSHED; -.
OrthoDB; EOG091G01P4; -.
PhylomeDB; Q8TD16; -.
TreeFam; TF323833; -.
Reactome; R-HSA-6811436; COPI-independent Golgi-to-ER retrograde traffic.
ChiTaRS; BICD2; human.
GeneWiki; BICD2; -.
GenomeRNAi; 23299; -.
PRO; PR:Q8TD16; -.
Proteomes; UP000005640; Chromosome 9.
Bgee; ENSG00000185963; -.
CleanEx; HS_BICD2; -.
Genevisible; Q8TD16; HS.
GO; GO:0005642; C:annulate lamellae; IDA:UniProtKB.
GO; GO:0031410; C:cytoplasmic vesicle; ISS:BHF-UCL.
GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
GO; GO:0005635; C:nuclear envelope; IDA:UniProtKB.
GO; GO:0005643; C:nuclear pore; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:HPA.
GO; GO:0034452; F:dynactin binding; ISS:UniProtKB.
GO; GO:0070840; F:dynein complex binding; ISS:UniProtKB.
GO; GO:0051959; F:dynein light intermediate chain binding; IEA:Ensembl.
GO; GO:0017137; F:Rab GTPase binding; ISS:BHF-UCL.
GO; GO:0051642; P:centrosome localization; IMP:UniProtKB.
GO; GO:0072393; P:microtubule anchoring at microtubule organizing center; ISS:BHF-UCL.
GO; GO:0072385; P:minus-end-directed organelle transport along microtubule; ISS:BHF-UCL.
GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
GO; GO:0000042; P:protein targeting to Golgi; IMP:UniProtKB.
GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to ER; IMP:UniProtKB.
InterPro; IPR018477; Bicaudal-D_microtubule-assoc.
PANTHER; PTHR31233; PTHR31233; 1.
Pfam; PF09730; BicD; 1.
1: Evidence at protein level;
Acetylation; Alternative splicing; Coiled coil; Complete proteome;
Cytoplasm; Cytoskeleton; Disease mutation; Golgi apparatus;
mRNA transport; Neurodegeneration; Nuclear pore complex; Nucleus;
Phosphoprotein; Protein transport; Reference proteome; Translocation;
Transport.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22814378}.
CHAIN 2 824 Protein bicaudal D homolog 2.
/FTId=PRO_0000205359.
REGION 25 398 Interacts with DYNLL1, DYNC1H1, DYNC1I2,
DCTN1 and DCTN2.
{ECO:0000250|UniProtKB:Q921C5}.
REGION 334 599 Interaction with KIF5A.
{ECO:0000250|UniProtKB:Q921C5}.
REGION 590 824 Interaction with RANBP2.
{ECO:0000250|UniProtKB:Q921C5}.
REGION 666 814 Interacts with RAB6A.
{ECO:0000250|UniProtKB:Q921C5}.
COILED 20 269 {ECO:0000255}.
COILED 338 537 {ECO:0000255}.
COILED 666 808 {ECO:0000255}.
MOD_RES 2 2 N-acetylserine.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22814378}.
MOD_RES 190 190 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:18691976}.
MOD_RES 224 224 Phosphoserine.
{ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:23186163}.
MOD_RES 318 318 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 319 319 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 343 343 Phosphoserine.
{ECO:0000244|PubMed:18691976}.
MOD_RES 395 395 Phosphoserine.
{ECO:0000244|PubMed:18691976}.
MOD_RES 568 568 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 574 574 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 582 582 Phosphoserine.
{ECO:0000244|PubMed:15144186,
ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 602 602 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 821 821 Phosphothreonine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 823 823 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
VAR_SEQ 824 824 L -> VSHTCACASDRAEGTGLANQVFCSEKHSIYCD (in
isoform 2). {ECO:0000303|PubMed:9734811}.
/FTId=VSP_007969.
VARIANT 90 90 K -> R (in dbSNP:rs61754130).
{ECO:0000269|PubMed:23664116}.
/FTId=VAR_070111.
VARIANT 107 107 S -> L (in SMALED2; causes Golgi
fragmentation; affects interaction with
RAB6A and DNAI1 and the subcellular
location of the protein;
dbSNP:rs398123028).
{ECO:0000269|PubMed:23664116,
ECO:0000269|PubMed:23664119,
ECO:0000269|PubMed:23664120}.
/FTId=VAR_070112.
VARIANT 188 188 N -> T (in SMALED2; causes Golgi
fragmentation; dbSNP:rs398123029).
{ECO:0000269|PubMed:23664116}.
/FTId=VAR_070113.
VARIANT 189 189 I -> F (in SMALED2).
{ECO:0000269|PubMed:23664120}.
/FTId=VAR_070114.
VARIANT 501 501 R -> P (in SMALED2; the mutation causes
increased interaction with dynein; the
mutant protein accumulates abnormally in
the perinuclear region where it forms
ring-like structures that colocalize with
RAB6A; dbSNP:rs398123032).
{ECO:0000269|PubMed:23664120}.
/FTId=VAR_070115.
VARIANT 508 508 K -> T (in SMALED2; dbSNP:rs398123031).
{ECO:0000269|PubMed:23664120}.
/FTId=VAR_070116.
VARIANT 703 703 T -> M (in SMALED2; causes Golgi
fragmentation; dbSNP:rs371707778).
{ECO:0000269|PubMed:23664116}.
/FTId=VAR_070117.
VARIANT 774 774 E -> G (in SMALED2; affects interaction
with RAB6A and DNAI1 and the subcellular
location of the protein;
dbSNP:rs398123030).
{ECO:0000269|PubMed:23664119}.
/FTId=VAR_070118.
SEQUENCE 824 AA; 93533 MW; 9C49138FF416378D CRC64;
MSAPSEEEEY ARLVMEAQPE WLRAEVKRLS HELAETTREK IQAAEYGLAV LEEKHQLKLQ
FEELEVDYEA IRSEMEQLKE AFGQAHTNHK KVAADGESRE ESLIQESASK EQYYVRKVLE
LQTELKQLRN VLTNTQSENE RLASVAQELK EINQNVEIQR GRLRDDIKEY KFREARLLQD
YSELEEENIS LQKQVSVLRQ NQVEFEGLKH EIKRLEEETE YLNSQLEDAI RLKEISERQL
EEALETLKTE REQKNSLRKE LSHYMSINDS FYTSHLHVSL DGLKFSDDAA EPNNDAEALV
NGFEHGGLAK LPLDNKTSTP KKEGLAPPSP SLVSDLLSEL NISEIQKLKQ QLMQMEREKA
GLLATLQDTQ KQLEHTRGSL SEQQEKVTRL TENLSALRRL QASKERQTAL DNEKDRDSHE
DGDYYEVDIN GPEILACKYH VAVAEAGELR EQLKALRSTH EAREAQHAEE KGRYEAEGQA
LTEKVSLLEK ASRQDRELLA RLEKELKKVS DVAGETQGSL SVAQDELVTF SEELANLYHH
VCMCNNETPN RVMLDYYREG QGGAGRTSPG GRTSPEARGR RSPILLPKGL LAPEAGRADG
GTGDSSPSPG SSLPSPLSDP RREPMNIYNL IAIIRDQIKH LQAAVDRTTE LSRQRIASQE
LGPAVDKDKE ALMEEILKLK SLLSTKREQI TTLRTVLKAN KQTAEVALAN LKSKYENEKA
MVTETMMKLR NELKALKEDA ATFSSLRAMF ATRCDEYITQ LDEMQRQLAA AEDEKKTLNS
LLRMAIQQKL ALTQRLELLE LDHEQTRRGR AKAAPKTKPA TPSL


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