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Q9JLB4

- CUBN_MOUSE

UniProt

Q9JLB4 - CUBN_MOUSE

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Protein
Cubilin
Gene
Cubn, Ifcr
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Cotransporter which plays a role in lipoprotein, vitamin and iron metabolism, by facilitating their uptake. Binds to ALB, MB, Kappa and lambda-light chains, TF, hemoglobin, GC, SCGB1A1, APOA1, high density lipoprotein, and the GIF-cobalamin complex. The binding of all ligands requires calcium. Serves as important transporter in several absorptive epithelia, including intestine, renal proximal tubules and embryonic yolk sac. Interaction with LRP2 mediates its trafficking throughout vesicles and facilitates the uptake of specific ligands like GC, hemoglobin, ALB, TF and SCGB1A1. Interaction with AMN controls its trafficking to the plasma membrane and facilitates endocytosis of ligands. May play an important role in the development of the peri-implantation embryo through internalization of APOA1 and cholesterol. Binds to LGALS3 at the maternal-fetal interface.4 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei32 – 332Cleavage; by furin Reviewed prediction
Metal bindingi980 – 9801Calcium 1 By similarity
Metal bindingi988 – 9881Calcium 1 By similarity
Metal bindingi1027 – 10271Calcium 1 By similarity
Metal bindingi1030 – 10301Calcium 1; via carbonyl oxygen By similarity
Metal bindingi1096 – 10961Calcium 2 By similarity
Metal bindingi1105 – 11051Calcium 2 By similarity
Metal bindingi1146 – 11461Calcium 2 By similarity
Metal bindingi1213 – 12131Calcium 3 By similarity
Metal bindingi1221 – 12211Calcium 3 By similarity
Metal bindingi1262 – 12621Calcium 3 By similarity
Metal bindingi1264 – 12641Calcium 3; via carbonyl oxygen By similarity
Metal bindingi1265 – 12651Calcium 3; via carbonyl oxygen By similarity
Metal bindingi1328 – 13281Calcium 4 By similarity
Metal bindingi1336 – 13361Calcium 4 By similarity
Metal bindingi1373 – 13731Calcium 4 By similarity
Metal bindingi1375 – 13751Calcium 4; via carbonyl oxygen By similarity

GO - Molecular functioni

  1. calcium ion binding Source: InterPro
  2. cobalamin binding Source: UniProtKB-KW
  3. protein binding Source: MGI
  4. receptor activity Source: MGI

GO - Biological processi

  1. cholesterol metabolic process Source: UniProtKB-KW
  2. lipoprotein transport Source: MGI
  3. receptor-mediated endocytosis Source: MGI
Complete GO annotation...

Keywords - Biological processi

Cholesterol metabolism, Lipid metabolism, Protein transport, Steroid metabolism, Sterol metabolism, Transport

Keywords - Ligandi

Calcium, Cobalamin, Cobalt, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_189089. Defective AMN causes hereditary megaloblastic anemia 1.
REACT_189090. Defective CUBN causes hereditary megaloblastic anemia 1.
REACT_189118. Cobalamin (Cbl, vitamin B12) transport and metabolism.
REACT_213857. HDL-mediated lipid transport.
REACT_218811. Vitamin D (calciferol) metabolism.

Names & Taxonomyi

Protein namesi
Recommended name:
Cubilin
Alternative name(s):
Intrinsic factor-cobalamin receptor
Gene namesi
Name:Cubn
Synonyms:Ifcr
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 2

Organism-specific databases

MGIiMGI:1931256. Cubn.

Subcellular locationi

Endosome membrane; Peripheral membrane protein By similarity. Lysosome membrane; Peripheral membrane protein By similarity
Note: Colocalizes with AMN and LRP2 in the endocytotic apparatus of epithelial cells By similarity.

GO - Cellular componenti

  1. Golgi apparatus Source: MGI
  2. apical part of cell Source: MGI
  3. apical plasma membrane Source: MGI
  4. brush border Source: MGI
  5. coated pit Source: MGI
  6. cytoplasm Source: MGI
  7. endocytic vesicle Source: MGI
  8. endoplasmic reticulum Source: MGI
  9. endosome Source: MGI
  10. endosome membrane Source: UniProtKB-SubCell
  11. lysosomal membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Endosome, Lysosome, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020 Reviewed prediction
Add
BLAST
Propeptidei21 – 3212Removed in mature form By similarity
PRO_0000046074Add
BLAST
Chaini33 – 36233591Cubilin
PRO_0000046075Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi95 – 951N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi133 ↔ 144 By similarity
Disulfide bondi138 ↔ 153 By similarity
Disulfide bondi155 ↔ 164 By similarity
Disulfide bondi171 ↔ 187 By similarity
Disulfide bondi181 ↔ 196 By similarity
Disulfide bondi198 ↔ 207 By similarity
Disulfide bondi264 ↔ 277 By similarity
Disulfide bondi271 ↔ 286 By similarity
Disulfide bondi289 ↔ 300 By similarity
Disulfide bondi350 ↔ 363 By similarity
Disulfide bondi357 ↔ 376 By similarity
Disulfide bondi399 ↔ 409 By similarity
Disulfide bondi404 ↔ 418 By similarity
Disulfide bondi420 ↔ 429 By similarity
Glycosylationi428 – 4281N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi436 ↔ 447 By similarity
Disulfide bondi441 ↔ 456 By similarity
Disulfide bondi458 ↔ 467 By similarity
Disulfide bondi474 ↔ 500 By similarity
Glycosylationi491 – 4911N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi527 ↔ 549 By similarity
Disulfide bondi590 ↔ 616 By similarity
Disulfide bondi643 ↔ 665 By similarity
Disulfide bondi708 ↔ 734 By similarity
Glycosylationi711 – 7111N-linked (GlcNAc...) Reviewed prediction
Glycosylationi749 – 7491N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi761 ↔ 779 By similarity
Glycosylationi781 – 7811N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi817 ↔ 842 By similarity
Glycosylationi857 – 8571N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi869 ↔ 891 By similarity
Disulfide bondi932 ↔ 958 By similarity
Glycosylationi957 – 9571N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi985 ↔ 1005 By similarity
Glycosylationi1043 – 10431N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi1048 ↔ 1074 By similarity
Disulfide bondi1165 ↔ 1191 By similarity
Glycosylationi1168 – 11681N-linked (GlcNAc...) Reviewed prediction
Glycosylationi1217 – 12171N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi1218 ↔ 1240 By similarity
Disulfide bondi1278 ↔ 1306 By similarity
Glycosylationi1285 – 12851N-linked (GlcNAc...) Reviewed prediction
Glycosylationi1307 – 13071N-linked (GlcNAc...) Reviewed prediction
Glycosylationi1319 – 13191N-linked (GlcNAc...) Reviewed prediction
Glycosylationi1332 – 13321N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi1333 ↔ 1351 By similarity
Disulfide bondi1391 ↔ 1417 By similarity
Disulfide bondi1444 ↔ 1466 By similarity
Glycosylationi1500 – 15001N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi1510 ↔ 1536 By similarity
Glycosylationi1551 – 15511N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi1563 ↔ 1581 By similarity
Disulfide bondi1620 ↔ 1647 By similarity
Glycosylationi1646 – 16461N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi1675 ↔ 1697 By similarity
Disulfide bondi1738 ↔ 1764 By similarity
Disulfide bondi1791 ↔ 1812 By similarity
Glycosylationi1802 – 18021N-linked (GlcNAc...) Reviewed prediction
Glycosylationi1819 – 18191N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi1905 ↔ 1927 By similarity
Glycosylationi1967 – 19671N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi1978 ↔ 2006 By similarity
Disulfide bondi2032 ↔ 2054 By similarity
Glycosylationi2085 – 20851N-linked (GlcNAc...)1 Publication
Disulfide bondi2092 ↔ 2118 By similarity
Glycosylationi2117 – 21171N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi2217 ↔ 2247 By similarity
Glycosylationi2274 – 22741N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi2275 ↔ 2297 By similarity
Disulfide bondi2336 ↔ 2363 By similarity
Disulfide bondi2390 ↔ 2411 By similarity
Glycosylationi2400 – 24001N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi2452 ↔ 2478 By similarity
Disulfide bondi2505 ↔ 2527 By similarity
Glycosylationi2531 – 25311N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi2570 ↔ 2599 By similarity
Glycosylationi2581 – 25811N-linked (GlcNAc...) Reviewed prediction
Glycosylationi2610 – 26101N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi2628 ↔ 2649 By similarity
Disulfide bondi2689 ↔ 2715 By similarity
Disulfide bondi2742 ↔ 2764 By similarity
Disulfide bondi2805 ↔ 2831 By similarity
Glycosylationi2813 – 28131N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi2860 ↔ 2883 By similarity
Disulfide bondi2920 ↔ 2946 By similarity
Glycosylationi2925 – 29251N-linked (GlcNAc...)1 Publication
Disulfide bondi2977 ↔ 2999 By similarity
Glycosylationi2989 – 29891N-linked (GlcNAc...) Reviewed prediction
Modified residuei3008 – 30081Phosphothreonine By similarity
Disulfide bondi3037 ↔ 3064 By similarity
Disulfide bondi3091 ↔ 3113 By similarity
Glycosylationi3106 – 31061N-linked (GlcNAc...) Reviewed prediction
Glycosylationi3125 – 31251N-linked (GlcNAc...)1 Publication
Disulfide bondi3157 ↔ 3185 By similarity
Disulfide bondi3215 ↔ 3237 By similarity
Glycosylationi3268 – 32681N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi3278 ↔ 3306 By similarity
Glycosylationi3283 – 32831N-linked (GlcNAc...) Reviewed prediction
Glycosylationi3290 – 32901N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi3332 ↔ 3354 By similarity
Glycosylationi3357 – 33571N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi3395 ↔ 3421 By similarity
Disulfide bondi3448 ↔ 3470 By similarity
Glycosylationi3457 – 34571N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi3511 ↔ 3537 By similarity
Glycosylationi3533 – 35331N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi3564 ↔ 3586 By similarity

Post-translational modificationi

The precursor is cleaved by a trans-Golgi proteinase furin. The result is a propeptide cleaved off By similarity.
N-glycosylated.1 Publication

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiQ9JLB4.
PaxDbiQ9JLB4.
PRIDEiQ9JLB4.

PTM databases

PhosphoSiteiQ9JLB4.

Expressioni

Tissue specificityi

Expressed in kidney, thymus, ileum, placenta, small intestine and yolk sac. In kidney expressed on the apical brush border surface of proximal tubular cells, in particular in endosomes and recycling membranes vesicles, so-called dense apical tubules, which carry internalized receptors back to the cell surface. Expressed in fetal membranes of yolk sac, placenta of pregnant females.2 Publications

Developmental stagei

Detected in yolk sac endoderm as early as day 6 and is present at the apical surface of those cells throughout the remainder of pregnancy. Apical expression is pronounced in the extraembryonic visceral endoderm (VE) of 6-9.5 dpc. Expressed by a subpopulation of cells dispersed within the 7.5 dpc embryonic endoderm and having a migratory morphology. First detected at the eight-cell stage. At the 32-cell stage expressed in all outer cells which are at the origin of the trophectoderm (TE). During the blastocyst stage, expression is predominant at the apical membrane of the TE cells.3 Publications

Gene expression databases

BgeeiQ9JLB4.
CleanExiMM_CUBN.
GenevestigatoriQ9JLB4.

Interactioni

Subunit structurei

Interacts with LRP2 in a dual-receptor complex in a calcium-dependent manner By similarity. Component of the cubam complex composed of CUBN and AMN. The cubam complex can oligomerize and form cubam trimers. Found in a complex with PID1/PCLI1, LRP1 and CUBNI By similarity. Interacts with LRP1 and PID1/PCLI1 By similarity.4 Publications

Protein-protein interaction databases

BioGridi211163. 4 interactions.
IntActiQ9JLB4. 2 interactions.
MINTiMINT-4130272.
STRINGi10090.ENSMUSP00000089009.

Structurei

3D structure databases

ProteinModelPortaliQ9JLB4.
SMRiQ9JLB4. Positions 932-1388.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini129 – 16537EGF-like 1
Add
BLAST
Domaini167 – 20842EGF-like 2; calcium-binding Reviewed prediction
Add
BLAST
Domaini260 – 30142EGF-like 3; calcium-binding Reviewed prediction
Add
BLAST
Domaini302 – 34544EGF-like 4; calcium-binding Reviewed prediction
Add
BLAST
Domaini346 – 38540EGF-like 5
Add
BLAST
Domaini395 – 43036EGF-like 6
Add
BLAST
Domaini432 – 46837EGF-like 7; calcium-binding Reviewed prediction
Add
BLAST
Domaini474 – 586113CUB 1
Add
BLAST
Domaini590 – 702113CUB 2
Add
BLAST
Domaini708 – 816109CUB 3
Add
BLAST
Domaini817 – 928112CUB 4
Add
BLAST
Domaini932 – 1042111CUB 5
Add
BLAST
Domaini1048 – 1161114CUB 6
Add
BLAST
Domaini1165 – 1277113CUB 7
Add
BLAST
Domaini1278 – 1389112CUB 8
Add
BLAST
Domaini1391 – 1506116CUB 9
Add
BLAST
Domaini1510 – 1619110CUB 10
Add
BLAST
Domaini1620 – 1734115CUB 11
Add
BLAST
Domaini1738 – 1850113CUB 12
Add
BLAST
Domaini1852 – 1963112CUB 13
Add
BLAST
Domaini1978 – 2091114CUB 14
Add
BLAST
Domaini2092 – 2213122CUB 15
Add
BLAST
Domaini2217 – 2334118CUB 16
Add
BLAST
Domaini2336 – 2448113CUB 17
Add
BLAST
Domaini2452 – 2565114CUB 18
Add
BLAST
Domaini2570 – 2687118CUB 19
Add
BLAST
Domaini2689 – 2801113CUB 20
Add
BLAST
Domaini2805 – 2919115CUB 21
Add
BLAST
Domaini2920 – 3035116CUB 22
Add
BLAST
Domaini3037 – 3150114CUB 23
Add
BLAST
Domaini3157 – 3274118CUB 24
Add
BLAST
Domaini3278 – 3393116CUB 25
Add
BLAST
Domaini3395 – 3507113CUB 26
Add
BLAST
Domaini3511 – 3623113CUB 27
Add
BLAST

Domaini

The CUB domains 5 to 8 mediate binding to GIF and ALB. CUB domains 1 and 2 mediate interaction with LRP2 By similarity.

Sequence similaritiesi

Contains 27 CUB domains.
Contains 7 EGF-like domains.

Keywords - Domaini

EGF-like domain, Repeat, Signal

Phylogenomic databases

eggNOGiNOG287752.
GeneTreeiENSGT00740000115149.
HOGENOMiHOG000049236.
HOVERGENiHBG080357.
InParanoidiB1AX10.
KOiK14616.
OMAiSIQLTIH.
OrthoDBiEOG741Z18.
TreeFamiTF316224.

Family and domain databases

Gene3Di2.60.120.290. 27 hits.
InterProiIPR000859. CUB_dom.
IPR028876. Cubilin.
IPR000742. EG-like_dom.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR024731. EGF_dom_MSP1-like.
[Graphical view]
PANTHERiPTHR10127:SF561. PTHR10127:SF561. 1 hit.
PfamiPF00431. CUB. 27 hits.
PF00008. EGF. 3 hits.
PF12947. EGF_3. 1 hit.
PF07645. EGF_CA. 3 hits.
[Graphical view]
SMARTiSM00042. CUB. 27 hits.
SM00181. EGF. 4 hits.
SM00179. EGF_CA. 4 hits.
[Graphical view]
SUPFAMiSSF49854. SSF49854. 27 hits.
PROSITEiPS00010. ASX_HYDROXYL. 3 hits.
PS01180. CUB. 27 hits.
PS00022. EGF_1. 4 hits.
PS01186. EGF_2. 2 hits.
PS50026. EGF_3. 6 hits.
PS01187. EGF_CA. 4 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q9JLB4-1 [UniParc]FASTAAdd to Basket

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MASHFLWGFV TLLMVPGLDG ETGTPEQKLQ KRIADLHQPR MTTEEGNLVF     50
LTSSAQNIEF RTGSLGKIKL NDDDLGECLH QIQRNKDDII DLKRNTTGLP 100
QNILSQVHQL NSKLVDLERD FQSLQQNVER KVCSSNPCHN GGTCVNLHDS 150
FICICPSQWK GLFCSEDVNE CVLYAGTPFG CQSGSTCVNT MGSFRCDCTP 200
DTYGPQCASK YNDCEQGSQQ LCKHGICEDL QRVYHGQLRF NCICDAGWTT 250
LPNGISCTED KDECSLQPSP CSEHAQCFNT QGSFYCGACP KGWQGNGYQC 300
QDINECEINN GGCSQAPLVP CLNTPGSFTC GNCPAGFSGD GRVCTPLDIC 350
SIHNGGCHPD ATCSSSSVLG SLLPVCTCPP GYTGNGYGSN GCVRLSNMCS 400
RHPCVNGQCI ETVSSYFCKC DSGWFGQNCT ENINECVSNP CLNGGTCIDG 450
VNGFTCDCTS SWTGYYCQTP QAACGGILSG TQGTFAYQSP NDTYVHNVNC 500
FWVVRTDEEK VLHITFTFFD LESASNCPRE YLQIHDGDSS ADFPLGRYCG 550
STPPQGVHSS ANSLYFHLYS EYIKRGRGFT ARWEAKLPEC GGILTGNYGS 600
ITSPGYPGNY PPGRDCVWNL LVSPGSLITF TFGTLSLESH NDCSKDYLEI 650
RDGPFHHDPI LGKFCTSLST PPLQTTGPAA RIHFHSDSET SDKGFHITYL 700
TTPSDLYCGG NYTDTEGELL LPPLTGPFSH SRQCVYLISQ PQGEQIVINF 750
THVELESQRG CSHTFIEVGD HESLLRKICG NETLFPIRSI SNNVWIRLRI 800
DALVQKASFR ADYQVACGGE LRGEGVIRSP FYPNAYAGRR TCRWTISQPP 850
REVVLLNFTD FQIGSSSSCD TDYIEIGPSS VLGSPGNEKF CGTNIPSFIT 900
SVYNVLYVTF VKSSSMENRG FMAMFSSEKL ECGKVLTEST GIIESPGHPN 950
VYPSGVNCTW HIVVQRGQLI RLVFSSFYLE FHYNCANDYL EVYDTIAQTS 1000
LGRYCGKSIP PSLTSSSHSI KLIFVSDSAL AHEGFSINYE AINASSVCLY 1050
DYTDNFGRLS SPNFPNNYPH NWNCVYRITV GLNQQIALHF TDFALEDYFG 1100
PKCVDFVEIR DGGFETSPLI GIYCGSVFPP RIISHSNKLW LRFKSDTALT 1150
ARGFSAYWDA SSTGCGGNLT TPTGVLTSPN YPMPYYHSSE CYWRLEASRG 1200
SPFLLEFQDF HLEHHPNCSL DYLAVFDGPS TNSRLINKLC GDTPPAPIRS 1250
SKDIVLLKLR TDAGQQGRGF EINYRQTCDN VVIVNKTSGI LESINYPNPY 1300
DKDQRCNWTI QATTGNTVNY TFLEFDVENY VNCSTDYLEL YDGPQRIGRY 1350
CGENIPPPGA TTGSKLIVVF HTDGVDSGEK GFKMHWFIHG CGGEMSGTMG 1400
SFSSPGYPNS YPHNKECIWN IRVAPGNSIQ LTIHDFDVEY HASCKYDTLE 1450
IYTGLDFHSP RIAQLCSRSP SANPMQISST DNELAIRFKT DSSLNGRGFN 1500
ASWRAVPGGC GGIFQVSRGE IHSPNYPNNY RANTECSWII QVEKYHRVLL 1550
NITDFDLEAT DSCLMTYDGS SSANTRVATV CGRQQPPNSI TSSGNSLFVR 1600
FQSGSSSQSR GFRAQFRQEC GAHIITDSSD SISSPLYPAN YPNNQNCTWI 1650
IEAQPPFNHI ALSFTHFHLQ SSTDCTRDFV EILDGRDSDA PVQGRYCGTS 1700
LPHPIISFGN ALTVRFVSDS VYGFDGFHAI YSASTSACGG TFYTGDGIFN 1750
SPGYPEDYHS NTECVWNIAS SPGNHLQLSF LSFQLENSLN CNKDFVEIRE 1800
GNATGHLMGR YCGNSLPGNY SSIEGHNLWV RFVSDGSGTG MGFQARFKNI 1850
FGNDNIVGTH GKIATPFWPG NYPLNSNYRW TVNVDSSHII HGRILEMDIE 1900
LTTNCFYDSL KIYDGFDIHS RLIGTYCGTQ RESFSSSRNS LTFQFSSDSS 1950
KSGRGFLLEW FAVDVSNVTL PTIAPGACGG YMVTGDTPVF FFSPGWPGPY 2000
GNGADCIWII YAPDSTVELN ILSMDIEAQL SCSYDKLIIK DGDSRLSQQL 2050
AVLCGRSVPG PIRSTGEYMY IRFTSDGSVT GAGFNASFQK SCGGYLHADR 2100
GIITSPKYPD NYLPNLNCSW HVLVQSGLTI AVHFEQPFQI QNRDSSCSQG 2150
DYLVLRNGPD NHSPPLGPSG GNGRFCGIYT PSTLFTSDNE MFIQFISDNS 2200
NGGQGFKIRY EAKSLACGGT IYIHDANSDG YVTSPNYPAN YPQHAECIWI 2250
LEAPSGRSIQ LQFEDQFNIE ETPNCSASYL ELRDGANSNA PVLSKLCGHT 2300
LPRNWVSSRG LMYLKFHTEG GSGYMGFKAK YSIVSCGGTV SGDSGVIESV 2350
GYPTRLYANN VFCQWHIQGL PGHYLTIRFE DFNLQSSPGC AKDFVEIWEN 2400
HTSGILLGRY CGNSIPSSVD TSSNVASIRF VTDGSVTDSG FRLQFKSSRE 2450
VCGGDLHGPT GTFTSPNYPN PNPHPRICEW TINVHEGRQI ILTFTNLRLS 2500
TQQSCNTEHL IVFNGIRNNS PRLQKLCSRV NVTNEFKSSG NTMKVIFFTD 2550
GSRPYGGFTA SYTSSEDAVC GGTLPSVSGG NFSSPGYNGI RDYARNLDCE 2600
WTLSNPNREN SSISIHFLGL SLESHQDCTF DVLEFRVGNA DGPLIEKFCS 2650
LSAPRVPLVI PYPQVWIHFV SNERVEYTGF YVEYSFTNCG GIQTGENGVI 2700
SSPNYPNLYS RWTQCSWLLE APEGHTITLT FSDFSVENHP TCTSDSVTVR 2750
NGDSPGSPII GRYCGQSVPG PIQSGSNQLV VTFNTNNQGQ SRGFYATWNT 2800
NTLGCGGTLH SDNGTIKSPH WPQTFPENSR CSWTAVTHES KHWEISFDSN 2850
FRIPSSDSQC RNSFVKVWEG MLETNDALLA TSCGNVAPSP IVTLGNIFTA 2900
VFQSEEMPAQ GFSASFISRC GRTFNSSTGD IVSPNFPKHY DNNMNCNYYI 2950
DVAPQSLVIL TFVSFHLEDR SAVSGTCDYD GLHIIKGHNL SSTPLVTICG 3000
SETLRPLTID GPVMLNFYSD AYITDFGFKI SYRVANCGGI YSGTYGVLNS 3050
PSFSYTNYPN NVYCVYSLQV RNDRLILLRF NDFEIVPSNL CSHDYLEVFD 3100
GPSIGNRSIG KFCGSTLPQV IKSTNNSLTL LFKTDSSQTA RGWKVSFRET 3150
IGPQQGCGGY LTEDSKSFVS PDHDSDGLYD KGLNCIWYII APENKLVKLT 3200
FNAFTLEEPS SPGKCTFDYV QIADGASINS YLGGRFCGSS RPAPFISSGN 3250
FLTVQFVSDI SIQMRGFNAT YTFVDMPCGG TYNATSMPQN TSSPQLSNIR 3300
RPFSTCTWVI EAPPHQQVQI TVWKLQLPSQ DCSRSSLELQ DSEQTNGNQV 3350
TQFCGANYTT LPVFYSSGST AVVVFKSDFL NRNSRVHFTY EIADCNREYN 3400
QAFGNLKSPG WPQGYANNLD CSIILRAPQN HRISLFFYWF QLEDSRQCMN 3450
DFLEVRNGSS SSSPLLGKYC SNLLPNPIFS QSNELYLHFH SDDSDTHHGY 3500
EIIWASSPTG CGGTLLGNEG ILANPGFPDS YPNNTHCEWT IVAPSGRPLS 3550
VGFPFLSIDS PGGCDQNYLI LFNGPDANSP PFGPFCGIDT VVAPFHASSN 3600
RVFIRFHAEY ATVSSGFEIM WSS 3623
Length:3,623
Mass (Da):399,097
Last modified:July 27, 2011 - v3
Checksum:iC105089FE0E0F1ED
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti811 – 8133ADY → NDL AA sequence 1 Publication
Sequence conflicti819 – 8191G → S AA sequence 1 Publication
Sequence conflicti822 – 8232RG → QD AA sequence 1 Publication
Sequence conflicti1859 – 18591T → Q AA sequence 1 Publication
Sequence conflicti2105 – 21051S → P AA sequence 1 Publication
Sequence conflicti2146 – 21483SCS → YGA AA sequence 1 Publication
Sequence conflicti2152 – 21521Y → L AA sequence 1 Publication
Sequence conflicti2156 – 21561R → S AA sequence 1 Publication
Sequence conflicti2531 – 25311N → S AA sequence 1 Publication
Sequence conflicti2536 – 25383FKS → WTK AA sequence 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AL773538, AL928807 Genomic DNA. Translation: CAM15444.1.
AL928807, AL773538 Genomic DNA. Translation: CAM27472.1.
AF197159 mRNA. Translation: AAF61487.1.
CCDSiCCDS38048.1.
RefSeqiNP_001074553.1. NM_001081084.2.
UniGeneiMm.313915.

Genome annotation databases

EnsembliENSMUST00000091436; ENSMUSP00000089009; ENSMUSG00000026726.
GeneIDi65969.
KEGGimmu:65969.
UCSCiuc008ijz.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AL773538 , AL928807 Genomic DNA. Translation: CAM15444.1 .
AL928807 , AL773538 Genomic DNA. Translation: CAM27472.1 .
AF197159 mRNA. Translation: AAF61487.1 .
CCDSi CCDS38048.1.
RefSeqi NP_001074553.1. NM_001081084.2.
UniGenei Mm.313915.

3D structure databases

ProteinModelPortali Q9JLB4.
SMRi Q9JLB4. Positions 932-1388.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 211163. 4 interactions.
IntActi Q9JLB4. 2 interactions.
MINTi MINT-4130272.
STRINGi 10090.ENSMUSP00000089009.

PTM databases

PhosphoSitei Q9JLB4.

Proteomic databases

MaxQBi Q9JLB4.
PaxDbi Q9JLB4.
PRIDEi Q9JLB4.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000091436 ; ENSMUSP00000089009 ; ENSMUSG00000026726 .
GeneIDi 65969.
KEGGi mmu:65969.
UCSCi uc008ijz.1. mouse.

Organism-specific databases

CTDi 8029.
MGIi MGI:1931256. Cubn.

Phylogenomic databases

eggNOGi NOG287752.
GeneTreei ENSGT00740000115149.
HOGENOMi HOG000049236.
HOVERGENi HBG080357.
InParanoidi B1AX10.
KOi K14616.
OMAi SIQLTIH.
OrthoDBi EOG741Z18.
TreeFami TF316224.

Enzyme and pathway databases

Reactomei REACT_189089. Defective AMN causes hereditary megaloblastic anemia 1.
REACT_189090. Defective CUBN causes hereditary megaloblastic anemia 1.
REACT_189118. Cobalamin (Cbl, vitamin B12) transport and metabolism.
REACT_213857. HDL-mediated lipid transport.
REACT_218811. Vitamin D (calciferol) metabolism.

Miscellaneous databases

NextBioi 320408.
PROi Q9JLB4.
SOURCEi Search...

Gene expression databases

Bgeei Q9JLB4.
CleanExi MM_CUBN.
Genevestigatori Q9JLB4.

Family and domain databases

Gene3Di 2.60.120.290. 27 hits.
InterProi IPR000859. CUB_dom.
IPR028876. Cubilin.
IPR000742. EG-like_dom.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR024731. EGF_dom_MSP1-like.
[Graphical view ]
PANTHERi PTHR10127:SF561. PTHR10127:SF561. 1 hit.
Pfami PF00431. CUB. 27 hits.
PF00008. EGF. 3 hits.
PF12947. EGF_3. 1 hit.
PF07645. EGF_CA. 3 hits.
[Graphical view ]
SMARTi SM00042. CUB. 27 hits.
SM00181. EGF. 4 hits.
SM00179. EGF_CA. 4 hits.
[Graphical view ]
SUPFAMi SSF49854. SSF49854. 27 hits.
PROSITEi PS00010. ASX_HYDROXYL. 3 hits.
PS01180. CUB. 27 hits.
PS00022. EGF_1. 4 hits.
PS01186. EGF_2. 2 hits.
PS50026. EGF_3. 6 hits.
PS01187. EGF_CA. 4 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  2. "Cubilin, a binding partner for galectin-3 in the murine utero-placental complex."
    Crider-Pirkle S., Billingsley P., Faust C., Hardy D.M., Lee V., Weitlauf H.
    J. Biol. Chem. 277:15904-15912(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 811-823; 1849-1862; 2101-2107; 2146-2157; 2530-2538; 2545-2553 AND 3399-3407, INTERACTION WITH LGALS3, GLYCOSYLATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, FUNCTION.
  3. "Megalin acts in concert with cubilin to mediate endocytosis of high density lipoproteins."
    Hammad S.M., Barth J.L., Knaak C., Argraves W.S.
    J. Biol. Chem. 275:12003-12008(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2792-3623, TISSUE SPECIFICITY, INTERACTION WITH HIGH DENSITY LIPOPROTEIN, FUNCTION.
    Tissue: Ectoplacental cone.
  4. "A two-receptor pathway for catabolism of Clara cell secretory protein in the kidney."
    Burmeister R., Boee I.-M., Nykjaer A., Jacobsen C., Moestrup S.K., Verroust P., Christensen E.I., Lund J., Willnow T.E.
    J. Biol. Chem. 276:13295-13301(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SCGB1A1, FUNCTION.
  5. "Differential distribution of cubilin and megalin expression in the mouse embryo."
    Drake C.J., Fleming P.A., Larue A.C., Barth J.L., Chintalapudi M.R., Argraves W.S.
    Anat. Rec. 277:163-170(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: DEVELOPMENTAL STAGE.
  6. "Mouse amnionless, which is required for primitive streak assembly, mediates cell-surface localization and endocytic function of cubilin on visceral endoderm and kidney proximal tubules."
    Strope S., Rivi R., Metzger T., Manova K., Lacy E.
    Development 131:4787-4795(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH AMN, FUNCTION.
  7. "Expression and role of cubilin in the internalization of nutrients during the peri-implantation development of the rodent embryo."
    Assemat E., Vinot S., Gofflot F., Linsel-Nitschke P., Illien F., Chatelet F., Verroust P.J., Louvet-Vallee S., Rinninger F., Kozyraki R.
    Biol. Reprod. 72:1079-1086(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: DEVELOPMENTAL STAGE.
  8. "Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."
    Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D.
    Nat. Biotechnol. 27:378-386(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-2085; ASN-2925 AND ASN-3125.

Entry informationi

Entry nameiCUBN_MOUSE
AccessioniPrimary (citable) accession number: Q9JLB4
Secondary accession number(s): B1AX10
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 7, 2006
Last sequence update: July 27, 2011
Last modified: September 3, 2014
This is version 110 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, 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

External Data

Dasty 3

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