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Protein

Brother of CDO

Gene

BOC

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Component of a cell-surface receptor complex that mediates cell-cell interactions between muscle precursor cells. Promotes differentiation of myogenic cells.

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Cell adhesion

Enzyme and pathway databases

ReactomeiR-HSA-375170. CDO in myogenesis.
R-HSA-5632681. Ligand-receptor interactions.
SignaLinkiQ9BWV1.

Names & Taxonomyi

Protein namesi
Recommended name:
Brother of CDO
Short name:
Protein BOC
Gene namesi
Name:BOC
ORF Names:UNQ604/PRO1190
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 3

Organism-specific databases

HGNCiHGNC:17173. BOC.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini31 – 855825ExtracellularSequence analysisAdd
BLAST
Transmembranei856 – 87621HelicalSequence analysisAdd
BLAST
Topological domaini877 – 1114238CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA143485316.

Polymorphism and mutation databases

BioMutaiBOC.
DMDMi74761309.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 30301 PublicationAdd
BLAST
Chaini31 – 11141084Brother of CDOPRO_0000234052Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi57 ↔ 106PROSITE-ProRule annotation
Glycosylationi65 – 651N-linked (GlcNAc...)Sequence analysis
Glycosylationi76 – 761N-linked (GlcNAc...)Sequence analysis
Glycosylationi98 – 981N-linked (GlcNAc...)Sequence analysis
Disulfide bondi150 ↔ 200PROSITE-ProRule annotation
Glycosylationi189 – 1891N-linked (GlcNAc...)Sequence analysis
Disulfide bondi252 ↔ 299PROSITE-ProRule annotation
Glycosylationi275 – 2751N-linked (GlcNAc...)Sequence analysis
Disulfide bondi344 ↔ 391PROSITE-ProRule annotation
Glycosylationi517 – 5171N-linked (GlcNAc...)Sequence analysis
Glycosylationi725 – 7251N-linked (GlcNAc...)Sequence analysis
Glycosylationi759 – 7591N-linked (GlcNAc...)Sequence analysis

Post-translational modificationi

N-glycosylated.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ9BWV1.
PRIDEiQ9BWV1.

PTM databases

PhosphoSiteiQ9BWV1.

Expressioni

Tissue specificityi

Detected in skeletal muscle, heart, thymus, kidney and small intestine. Detected at lower levels in brain, placenta, lung and colon mucosa.1 Publication

Gene expression databases

BgeeiQ9BWV1.
CleanExiHS_BOC.
ExpressionAtlasiQ9BWV1. baseline and differential.
GenevisibleiQ9BWV1. HS.

Organism-specific databases

HPAiCAB025806.
HPA060778.
HPA061787.

Interactioni

Subunit structurei

Part of a complex that contains BOC, CDON, NEO1, cadherins and CTNNB1. Interacts with NTN3 (By similarity). Interacts with SHH, DHH and IHH. Interacts with CDH2 and CTNNB1. Interacts with CDH15 only during the early stages of myoblast differentiation.By similarity3 Publications

Protein-protein interaction databases

BioGridi124859. 10 interactions.
IntActiQ9BWV1. 3 interactions.
STRINGi9606.ENSP00000347546.

Structurei

Secondary structure

1
1114
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi717 – 7259Combined sources
Beta strandi728 – 7347Combined sources
Helixi737 – 7404Combined sources
Beta strandi746 – 7549Combined sources
Helixi760 – 7623Combined sources
Beta strandi764 – 7696Combined sources
Beta strandi774 – 7774Combined sources
Beta strandi785 – 79410Combined sources
Beta strandi805 – 8084Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3N1GX-ray1.90C/D710-817[»]
3N1MX-ray1.69C710-817[»]
3N1PX-ray2.70C710-817[»]
ProteinModelPortaliQ9BWV1.
SMRiQ9BWV1. Positions 597-703, 710-813.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9BWV1.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini36 – 12388Ig-like C2-type 1Add
BLAST
Domaini129 – 21385Ig-like C2-type 2Add
BLAST
Domaini235 – 31581Ig-like C2-type 3Add
BLAST
Domaini323 – 40987Ig-like C2-type 4Add
BLAST
Domaini474 – 57198Fibronectin type-III 1PROSITE-ProRule annotationAdd
BLAST
Domaini608 – 70396Fibronectin type-III 2PROSITE-ProRule annotationAdd
BLAST
Domaini712 – 812101Fibronectin type-III 3PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 3 fibronectin type-III domains.PROSITE-ProRule annotation

Keywords - Domaini

Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IHIH. Eukaryota.
ENOG410XSVT. LUCA.
GeneTreeiENSGT00840000129688.
HOVERGENiHBG061102.
InParanoidiQ9BWV1.
OMAiDSPDSCQ.
OrthoDBiEOG7MD4PB.
PhylomeDBiQ9BWV1.
TreeFamiTF332268.

Family and domain databases

Gene3Di2.60.40.10. 7 hits.
InterProiIPR032982. BOC.
IPR003961. FN3_dom.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR013151. Immunoglobulin.
[Graphical view]
PANTHERiPTHR10489:SF11. PTHR10489:SF11. 2 hits.
PfamiPF00041. fn3. 3 hits.
PF07679. I-set. 1 hit.
PF00047. ig. 1 hit.
[Graphical view]
SMARTiSM00060. FN3. 3 hits.
SM00409. IG. 4 hits.
SM00408. IGc2. 4 hits.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 4 hits.
SSF49265. SSF49265. 2 hits.
PROSITEiPS50853. FN3. 3 hits.
PS50835. IG_LIKE. 4 hits.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9BWV1-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MLRGTMTAWR GMRPEVTLAC LLLATAGCFA DLNEVPQVTV QPASTVQKPG
60 70 80 90 100
GTVILGCVVE PPRMNVTWRL NGKELNGSDD ALGVLITHGT LVITALNNHT
110 120 130 140 150
VGRYQCVARM PAGAVASVPA TVTLANLQDF KLDVQHVIEV DEGNTAVIAC
160 170 180 190 200
HLPESHPKAQ VRYSVKQEWL EASRGNYLIM PSGNLQIVNA SQEDEGMYKC
210 220 230 240 250
AAYNPVTQEV KTSGSSDRLR VRRSTAEAAR IIYPPEAQTI IVTKGQSLIL
260 270 280 290 300
ECVASGIPPP RVTWAKDGSS VTGYNKTRFL LSNLLIDTTS EEDSGTYRCM
310 320 330 340 350
ADNGVGQPGA AVILYNVQVF EPPEVTMELS QLVIPWGQSA KLTCEVRGNP
360 370 380 390 400
PPSVLWLRNA VPLISSQRLR LSRRALRVLS MGPEDEGVYQ CMAENEVGSA
410 420 430 440 450
HAVVQLRTSR PSITPRLWQD AELATGTPPV SPSKLGNPEQ MLRGQPALPR
460 470 480 490 500
PPTSVGPASP QCPGEKGQGA PAEAPIILSS PRTSKTDSYE LVWRPRHEGS
510 520 530 540 550
GRAPILYYVV KHRKVTNSSD DWTISGIPAN QHRLTLTRLD PGSLYEVEMA
560 570 580 590 600
AYNCAGEGQT AMVTFRTGRR PKPEIMASKE QQIQRDDPGA SPQSSSQPDH
610 620 630 640 650
GRLSPPEAPD RPTISTASET SVYVTWIPRG NGGFPIQSFR VEYKKLKKVG
660 670 680 690 700
DWILATSAIP PSRLSVEITG LEKGTSYKFR VRALNMLGES EPSAPSRPYV
710 720 730 740 750
VSGYSGRVYE RPVAGPYITF TDAVNETTIM LKWMYIPASN NNTPIHGFYI
760 770 780 790 800
YYRPTDSDND SDYKKDMVEG DKYWHSISHL QPETSYDIKM QCFNEGGESE
810 820 830 840 850
FSNVMICETK ARKSSGQPGR LPPPTLAPPQ PPLPETIERP VGTGAMVARS
860 870 880 890 900
SDLPYLIVGV VLGSIVLIIV TFIPFCLWRA WSKQKHTTDL GFPRSALPPS
910 920 930 940 950
CPYTMVPLGG LPGHQASGQP YLSGISGRAC ANGIHMNRGC PSAAVGYPGM
960 970 980 990 1000
KPQQHCPGEL QQQSDTSSLL RQTHLGNGYD PQSHQITRGP KSSPDEGSFL
1010 1020 1030 1040 1050
YTLPDDSTHQ LLQPHHDCCQ RQEQPAAVGQ SGVRRAPDSP VLEAVWDPPF
1060 1070 1080 1090 1100
HSGPPCCLGL VPVEEVDSPD SCQVSGGDWC PQHPVGAYVG QEPGMQLSPG
1110
PLVRVSFETP PLTI
Length:1,114
Mass (Da):121,059
Last modified:June 1, 2001 - v1
Checksum:iBDA9021D39CFE3BC
GO
Isoform 2 (identifier: Q9BWV1-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-183: Missing.
     184-223: NLQIVNASQE...GSSDRLRVRR → KTRNGCLIPS...SVLALLAPPG

Note: No experimental confirmation available. Incomplete sequence.
Show »
Length:931
Mass (Da):100,978
Checksum:iCA65A54A8B86F63E
GO
Isoform 3 (identifier: Q9BWV1-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     514-514: K → KQ

Show »
Length:1,115
Mass (Da):121,188
Checksum:iA46602F71E323561
GO

Sequence cautioni

The sequence BAC11057.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti461 – 4611Q → K in AAQ88694 (PubMed:12975309).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti713 – 7131V → M in a breast cancer sample; somatic mutation. 1 Publication
VAR_035503
Natural varianti883 – 8831K → N.
Corresponds to variant rs35536878 [ dbSNP | Ensembl ].
VAR_033600
Natural varianti915 – 9151Q → H.
Corresponds to variant rs3814405 [ dbSNP | Ensembl ].
VAR_033601

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 183183Missing in isoform 2. CuratedVSP_037603Add
BLAST
Alternative sequencei184 – 22340NLQIV…LRVRR → KTRNGCLIPSPCSLGLPPGH ALQDILVHTPSVLALLAPPG in isoform 2. CuratedVSP_037604Add
BLAST
Alternative sequencei514 – 5141K → KQ in isoform 3. 2 PublicationsVSP_034684

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY027658 mRNA. Translation: AAK14795.1.
AY358328 mRNA. Translation: AAQ88694.1.
AK074556 mRNA. Translation: BAC11057.1. Different initiation.
AK090455 mRNA. Translation: BAC03436.1.
AC026329 Genomic DNA. No translation available.
CH471052 Genomic DNA. Translation: EAW79643.1.
CH471052 Genomic DNA. Translation: EAW79644.1.
CH471052 Genomic DNA. Translation: EAW79646.1.
BC136390 mRNA. Translation: AAI36391.1.
CCDSiCCDS2971.1. [Q9BWV1-1]
CCDS77788.1. [Q9BWV1-3]
RefSeqiNP_001288790.1. NM_001301861.1. [Q9BWV1-3]
NP_150279.1. NM_033254.3. [Q9BWV1-1]
XP_005247948.1. XM_005247891.1. [Q9BWV1-3]
XP_005247949.1. XM_005247892.1. [Q9BWV1-3]
XP_005247951.1. XM_005247894.1. [Q9BWV1-3]
XP_011511602.1. XM_011513300.1. [Q9BWV1-3]
XP_011511603.1. XM_011513301.1. [Q9BWV1-3]
XP_011511604.1. XM_011513302.1. [Q9BWV1-3]
XP_011511605.1. XM_011513303.1. [Q9BWV1-3]
XP_011511606.1. XM_011513304.1. [Q9BWV1-3]
XP_011511607.1. XM_011513305.1. [Q9BWV1-1]
UniGeneiHs.591318.

Genome annotation databases

EnsembliENST00000273395; ENSP00000273395; ENSG00000144857. [Q9BWV1-3]
ENST00000355385; ENSP00000347546; ENSG00000144857. [Q9BWV1-1]
ENST00000495514; ENSP00000418663; ENSG00000144857. [Q9BWV1-1]
GeneIDi91653.
KEGGihsa:91653.
UCSCiuc003dzx.4. human. [Q9BWV1-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY027658 mRNA. Translation: AAK14795.1.
AY358328 mRNA. Translation: AAQ88694.1.
AK074556 mRNA. Translation: BAC11057.1. Different initiation.
AK090455 mRNA. Translation: BAC03436.1.
AC026329 Genomic DNA. No translation available.
CH471052 Genomic DNA. Translation: EAW79643.1.
CH471052 Genomic DNA. Translation: EAW79644.1.
CH471052 Genomic DNA. Translation: EAW79646.1.
BC136390 mRNA. Translation: AAI36391.1.
CCDSiCCDS2971.1. [Q9BWV1-1]
CCDS77788.1. [Q9BWV1-3]
RefSeqiNP_001288790.1. NM_001301861.1. [Q9BWV1-3]
NP_150279.1. NM_033254.3. [Q9BWV1-1]
XP_005247948.1. XM_005247891.1. [Q9BWV1-3]
XP_005247949.1. XM_005247892.1. [Q9BWV1-3]
XP_005247951.1. XM_005247894.1. [Q9BWV1-3]
XP_011511602.1. XM_011513300.1. [Q9BWV1-3]
XP_011511603.1. XM_011513301.1. [Q9BWV1-3]
XP_011511604.1. XM_011513302.1. [Q9BWV1-3]
XP_011511605.1. XM_011513303.1. [Q9BWV1-3]
XP_011511606.1. XM_011513304.1. [Q9BWV1-3]
XP_011511607.1. XM_011513305.1. [Q9BWV1-1]
UniGeneiHs.591318.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3N1GX-ray1.90C/D710-817[»]
3N1MX-ray1.69C710-817[»]
3N1PX-ray2.70C710-817[»]
ProteinModelPortaliQ9BWV1.
SMRiQ9BWV1. Positions 597-703, 710-813.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi124859. 10 interactions.
IntActiQ9BWV1. 3 interactions.
STRINGi9606.ENSP00000347546.

PTM databases

PhosphoSiteiQ9BWV1.

Polymorphism and mutation databases

BioMutaiBOC.
DMDMi74761309.

Proteomic databases

PaxDbiQ9BWV1.
PRIDEiQ9BWV1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000273395; ENSP00000273395; ENSG00000144857. [Q9BWV1-3]
ENST00000355385; ENSP00000347546; ENSG00000144857. [Q9BWV1-1]
ENST00000495514; ENSP00000418663; ENSG00000144857. [Q9BWV1-1]
GeneIDi91653.
KEGGihsa:91653.
UCSCiuc003dzx.4. human. [Q9BWV1-1]

Organism-specific databases

CTDi91653.
GeneCardsiBOC.
HGNCiHGNC:17173. BOC.
HPAiCAB025806.
HPA060778.
HPA061787.
MIMi608708. gene.
neXtProtiNX_Q9BWV1.
PharmGKBiPA143485316.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IHIH. Eukaryota.
ENOG410XSVT. LUCA.
GeneTreeiENSGT00840000129688.
HOVERGENiHBG061102.
InParanoidiQ9BWV1.
OMAiDSPDSCQ.
OrthoDBiEOG7MD4PB.
PhylomeDBiQ9BWV1.
TreeFamiTF332268.

Enzyme and pathway databases

ReactomeiR-HSA-375170. CDO in myogenesis.
R-HSA-5632681. Ligand-receptor interactions.
SignaLinkiQ9BWV1.

Miscellaneous databases

ChiTaRSiBOC. human.
EvolutionaryTraceiQ9BWV1.
GeneWikiiBOC_(gene).
GenomeRNAii91653.
NextBioi77360.
PROiQ9BWV1.
SOURCEiSearch...

Gene expression databases

BgeeiQ9BWV1.
CleanExiHS_BOC.
ExpressionAtlasiQ9BWV1. baseline and differential.
GenevisibleiQ9BWV1. HS.

Family and domain databases

Gene3Di2.60.40.10. 7 hits.
InterProiIPR032982. BOC.
IPR003961. FN3_dom.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR013151. Immunoglobulin.
[Graphical view]
PANTHERiPTHR10489:SF11. PTHR10489:SF11. 2 hits.
PfamiPF00041. fn3. 3 hits.
PF07679. I-set. 1 hit.
PF00047. ig. 1 hit.
[Graphical view]
SMARTiSM00060. FN3. 3 hits.
SM00409. IG. 4 hits.
SM00408. IGc2. 4 hits.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 4 hits.
SSF49265. SSF49265. 2 hits.
PROSITEiPS50853. FN3. 3 hits.
PS50835. IG_LIKE. 4 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "BOC, an Ig superfamily member, associates with CDO to positively regulate myogenic differentiation."
    Kang J.-S., Mulieri P.J., Hu Y., Taliana L., Krauss R.S.
    EMBO J. 21:114-124(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH CDON, GLYCOSYLATION, TISSUE SPECIFICITY.
    Tissue: Fetal brain.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 317-1114 (ISOFORM 3).
    Tissue: Embryo and Spleen.
  5. "The DNA sequence, annotation and analysis of human chromosome 3."
    Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
    , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
    Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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).
  7. "Signal peptide prediction based on analysis of experimentally verified cleavage sites."
    Zhang Z., Henzel W.J.
    Protein Sci. 13:2819-2824(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 31-45.
  8. "Promyogenic members of the Ig and cadherin families associate to positively regulate differentiation."
    Kang J.-S., Feinleib J.L., Knox S., Ketteringham M.A., Krauss R.S.
    Proc. Natl. Acad. Sci. U.S.A. 100:3989-3994(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A COMPLEX WITH CDON; CDH2; CDH15 AND CTNNB1, SUBCELLULAR LOCATION.
  9. "All mammalian Hedgehog proteins interact with cell adhesion molecule, down-regulated by oncogenes (CDO) and brother of CDO (BOC) in a conserved manner."
    Kavran J.M., Ward M.D., Oladosu O.O., Mulepati S., Leahy D.J.
    J. Biol. Chem. 285:24584-24590(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.69 ANGSTROMS) OF 710-817 IN COMPLEXES WITH DHH AND IHH, INTERACTION WITH SHH; DHH AND IHH.
  10. Cited for: VARIANT [LARGE SCALE ANALYSIS] MET-713.

Entry informationi

Entry nameiBOC_HUMAN
AccessioniPrimary (citable) accession number: Q9BWV1
Secondary accession number(s): A6NJ30
, B2RMS8, D3DN70, Q6UXJ5, Q8N2P7, Q8NF26
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 2, 2006
Last sequence update: June 1, 2001
Last modified: May 11, 2016
This is version 127 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Miscellaneous

The C-terminal cytoplasmic domain is not required for the stimuation of myogenesis.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 3
    Human chromosome 3: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. 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.