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Q9JLB4

- CUBN_MOUSE

UniProt

Q9JLB4 - CUBN_MOUSE

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Protein

Cubilin

Gene

Cubn

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 furinSequence Analysis
Metal bindingi980 – 9801Calcium 1By similarity
Metal bindingi988 – 9881Calcium 1By similarity
Metal bindingi1027 – 10271Calcium 1By similarity
Metal bindingi1030 – 10301Calcium 1; via carbonyl oxygenBy similarity
Metal bindingi1096 – 10961Calcium 2By similarity
Metal bindingi1105 – 11051Calcium 2By similarity
Metal bindingi1146 – 11461Calcium 2By similarity
Metal bindingi1213 – 12131Calcium 3By similarity
Metal bindingi1221 – 12211Calcium 3By similarity
Metal bindingi1262 – 12621Calcium 3By similarity
Metal bindingi1264 – 12641Calcium 3; via carbonyl oxygenBy similarity
Metal bindingi1265 – 12651Calcium 3; via carbonyl oxygenBy similarity
Metal bindingi1328 – 13281Calcium 4By similarity
Metal bindingi1336 – 13361Calcium 4By similarity
Metal bindingi1373 – 13731Calcium 4By similarity
Metal bindingi1375 – 13751Calcium 4; via carbonyl oxygenBy similarity

GO - Molecular functioni

  1. calcium ion binding Source: InterPro
  2. cobalamin binding Source: UniProtKB-KW
  3. 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 By similarity; Peripheral membrane protein By similarity. Lysosome membrane By similarity; Peripheral membrane protein By similarity
Note: Colocalizes with AMN and LRP2 in the endocytotic apparatus of epithelial cells.By similarity

GO - Cellular componenti

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

Keywords - Cellular componenti

Endosome, Lysosome, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020Sequence AnalysisAdd
BLAST
Propeptidei21 – 3212Removed in mature formBy similarityPRO_0000046074Add
BLAST
Chaini33 – 36233591CubilinPRO_0000046075Add
BLAST

Amino acid modifications

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

Post-translational modificationi

The precursor is cleaved by a trans-Golgi proteinase furin. The result is a propeptide cleaved off (By similarity).By similarity
N-glycosylated.2 Publications

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).By similarity

Protein-protein interaction databases

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

Structurei

3D structure databases

ProteinModelPortaliQ9JLB4.
SMRiQ9JLB4. Positions 932-1388.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

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

Sequence similaritiesi

Contains 27 CUB domains.PROSITE-ProRule annotation
Contains 7 EGF-like domains.PROSITE-ProRule annotation

Keywords - Domaini

EGF-like domain, Repeat, Signal

Phylogenomic databases

eggNOGiNOG287752.
GeneTreeiENSGT00760000119018.
HOGENOMiHOG000049236.
HOVERGENiHBG080357.
InParanoidiQ9JLB4.
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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        10         20         30         40         50
MASHFLWGFV TLLMVPGLDG ETGTPEQKLQ KRIADLHQPR MTTEEGNLVF
60 70 80 90 100
LTSSAQNIEF RTGSLGKIKL NDDDLGECLH QIQRNKDDII DLKRNTTGLP
110 120 130 140 150
QNILSQVHQL NSKLVDLERD FQSLQQNVER KVCSSNPCHN GGTCVNLHDS
160 170 180 190 200
FICICPSQWK GLFCSEDVNE CVLYAGTPFG CQSGSTCVNT MGSFRCDCTP
210 220 230 240 250
DTYGPQCASK YNDCEQGSQQ LCKHGICEDL QRVYHGQLRF NCICDAGWTT
260 270 280 290 300
LPNGISCTED KDECSLQPSP CSEHAQCFNT QGSFYCGACP KGWQGNGYQC
310 320 330 340 350
QDINECEINN GGCSQAPLVP CLNTPGSFTC GNCPAGFSGD GRVCTPLDIC
360 370 380 390 400
SIHNGGCHPD ATCSSSSVLG SLLPVCTCPP GYTGNGYGSN GCVRLSNMCS
410 420 430 440 450
RHPCVNGQCI ETVSSYFCKC DSGWFGQNCT ENINECVSNP CLNGGTCIDG
460 470 480 490 500
VNGFTCDCTS SWTGYYCQTP QAACGGILSG TQGTFAYQSP NDTYVHNVNC
510 520 530 540 550
FWVVRTDEEK VLHITFTFFD LESASNCPRE YLQIHDGDSS ADFPLGRYCG
560 570 580 590 600
STPPQGVHSS ANSLYFHLYS EYIKRGRGFT ARWEAKLPEC GGILTGNYGS
610 620 630 640 650
ITSPGYPGNY PPGRDCVWNL LVSPGSLITF TFGTLSLESH NDCSKDYLEI
660 670 680 690 700
RDGPFHHDPI LGKFCTSLST PPLQTTGPAA RIHFHSDSET SDKGFHITYL
710 720 730 740 750
TTPSDLYCGG NYTDTEGELL LPPLTGPFSH SRQCVYLISQ PQGEQIVINF
760 770 780 790 800
THVELESQRG CSHTFIEVGD HESLLRKICG NETLFPIRSI SNNVWIRLRI
810 820 830 840 850
DALVQKASFR ADYQVACGGE LRGEGVIRSP FYPNAYAGRR TCRWTISQPP
860 870 880 890 900
REVVLLNFTD FQIGSSSSCD TDYIEIGPSS VLGSPGNEKF CGTNIPSFIT
910 920 930 940 950
SVYNVLYVTF VKSSSMENRG FMAMFSSEKL ECGKVLTEST GIIESPGHPN
960 970 980 990 1000
VYPSGVNCTW HIVVQRGQLI RLVFSSFYLE FHYNCANDYL EVYDTIAQTS
1010 1020 1030 1040 1050
LGRYCGKSIP PSLTSSSHSI KLIFVSDSAL AHEGFSINYE AINASSVCLY
1060 1070 1080 1090 1100
DYTDNFGRLS SPNFPNNYPH NWNCVYRITV GLNQQIALHF TDFALEDYFG
1110 1120 1130 1140 1150
PKCVDFVEIR DGGFETSPLI GIYCGSVFPP RIISHSNKLW LRFKSDTALT
1160 1170 1180 1190 1200
ARGFSAYWDA SSTGCGGNLT TPTGVLTSPN YPMPYYHSSE CYWRLEASRG
1210 1220 1230 1240 1250
SPFLLEFQDF HLEHHPNCSL DYLAVFDGPS TNSRLINKLC GDTPPAPIRS
1260 1270 1280 1290 1300
SKDIVLLKLR TDAGQQGRGF EINYRQTCDN VVIVNKTSGI LESINYPNPY
1310 1320 1330 1340 1350
DKDQRCNWTI QATTGNTVNY TFLEFDVENY VNCSTDYLEL YDGPQRIGRY
1360 1370 1380 1390 1400
CGENIPPPGA TTGSKLIVVF HTDGVDSGEK GFKMHWFIHG CGGEMSGTMG
1410 1420 1430 1440 1450
SFSSPGYPNS YPHNKECIWN IRVAPGNSIQ LTIHDFDVEY HASCKYDTLE
1460 1470 1480 1490 1500
IYTGLDFHSP RIAQLCSRSP SANPMQISST DNELAIRFKT DSSLNGRGFN
1510 1520 1530 1540 1550
ASWRAVPGGC GGIFQVSRGE IHSPNYPNNY RANTECSWII QVEKYHRVLL
1560 1570 1580 1590 1600
NITDFDLEAT DSCLMTYDGS SSANTRVATV CGRQQPPNSI TSSGNSLFVR
1610 1620 1630 1640 1650
FQSGSSSQSR GFRAQFRQEC GAHIITDSSD SISSPLYPAN YPNNQNCTWI
1660 1670 1680 1690 1700
IEAQPPFNHI ALSFTHFHLQ SSTDCTRDFV EILDGRDSDA PVQGRYCGTS
1710 1720 1730 1740 1750
LPHPIISFGN ALTVRFVSDS VYGFDGFHAI YSASTSACGG TFYTGDGIFN
1760 1770 1780 1790 1800
SPGYPEDYHS NTECVWNIAS SPGNHLQLSF LSFQLENSLN CNKDFVEIRE
1810 1820 1830 1840 1850
GNATGHLMGR YCGNSLPGNY SSIEGHNLWV RFVSDGSGTG MGFQARFKNI
1860 1870 1880 1890 1900
FGNDNIVGTH GKIATPFWPG NYPLNSNYRW TVNVDSSHII HGRILEMDIE
1910 1920 1930 1940 1950
LTTNCFYDSL KIYDGFDIHS RLIGTYCGTQ RESFSSSRNS LTFQFSSDSS
1960 1970 1980 1990 2000
KSGRGFLLEW FAVDVSNVTL PTIAPGACGG YMVTGDTPVF FFSPGWPGPY
2010 2020 2030 2040 2050
GNGADCIWII YAPDSTVELN ILSMDIEAQL SCSYDKLIIK DGDSRLSQQL
2060 2070 2080 2090 2100
AVLCGRSVPG PIRSTGEYMY IRFTSDGSVT GAGFNASFQK SCGGYLHADR
2110 2120 2130 2140 2150
GIITSPKYPD NYLPNLNCSW HVLVQSGLTI AVHFEQPFQI QNRDSSCSQG
2160 2170 2180 2190 2200
DYLVLRNGPD NHSPPLGPSG GNGRFCGIYT PSTLFTSDNE MFIQFISDNS
2210 2220 2230 2240 2250
NGGQGFKIRY EAKSLACGGT IYIHDANSDG YVTSPNYPAN YPQHAECIWI
2260 2270 2280 2290 2300
LEAPSGRSIQ LQFEDQFNIE ETPNCSASYL ELRDGANSNA PVLSKLCGHT
2310 2320 2330 2340 2350
LPRNWVSSRG LMYLKFHTEG GSGYMGFKAK YSIVSCGGTV SGDSGVIESV
2360 2370 2380 2390 2400
GYPTRLYANN VFCQWHIQGL PGHYLTIRFE DFNLQSSPGC AKDFVEIWEN
2410 2420 2430 2440 2450
HTSGILLGRY CGNSIPSSVD TSSNVASIRF VTDGSVTDSG FRLQFKSSRE
2460 2470 2480 2490 2500
VCGGDLHGPT GTFTSPNYPN PNPHPRICEW TINVHEGRQI ILTFTNLRLS
2510 2520 2530 2540 2550
TQQSCNTEHL IVFNGIRNNS PRLQKLCSRV NVTNEFKSSG NTMKVIFFTD
2560 2570 2580 2590 2600
GSRPYGGFTA SYTSSEDAVC GGTLPSVSGG NFSSPGYNGI RDYARNLDCE
2610 2620 2630 2640 2650
WTLSNPNREN SSISIHFLGL SLESHQDCTF DVLEFRVGNA DGPLIEKFCS
2660 2670 2680 2690 2700
LSAPRVPLVI PYPQVWIHFV SNERVEYTGF YVEYSFTNCG GIQTGENGVI
2710 2720 2730 2740 2750
SSPNYPNLYS RWTQCSWLLE APEGHTITLT FSDFSVENHP TCTSDSVTVR
2760 2770 2780 2790 2800
NGDSPGSPII GRYCGQSVPG PIQSGSNQLV VTFNTNNQGQ SRGFYATWNT
2810 2820 2830 2840 2850
NTLGCGGTLH SDNGTIKSPH WPQTFPENSR CSWTAVTHES KHWEISFDSN
2860 2870 2880 2890 2900
FRIPSSDSQC RNSFVKVWEG MLETNDALLA TSCGNVAPSP IVTLGNIFTA
2910 2920 2930 2940 2950
VFQSEEMPAQ GFSASFISRC GRTFNSSTGD IVSPNFPKHY DNNMNCNYYI
2960 2970 2980 2990 3000
DVAPQSLVIL TFVSFHLEDR SAVSGTCDYD GLHIIKGHNL SSTPLVTICG
3010 3020 3030 3040 3050
SETLRPLTID GPVMLNFYSD AYITDFGFKI SYRVANCGGI YSGTYGVLNS
3060 3070 3080 3090 3100
PSFSYTNYPN NVYCVYSLQV RNDRLILLRF NDFEIVPSNL CSHDYLEVFD
3110 3120 3130 3140 3150
GPSIGNRSIG KFCGSTLPQV IKSTNNSLTL LFKTDSSQTA RGWKVSFRET
3160 3170 3180 3190 3200
IGPQQGCGGY LTEDSKSFVS PDHDSDGLYD KGLNCIWYII APENKLVKLT
3210 3220 3230 3240 3250
FNAFTLEEPS SPGKCTFDYV QIADGASINS YLGGRFCGSS RPAPFISSGN
3260 3270 3280 3290 3300
FLTVQFVSDI SIQMRGFNAT YTFVDMPCGG TYNATSMPQN TSSPQLSNIR
3310 3320 3330 3340 3350
RPFSTCTWVI EAPPHQQVQI TVWKLQLPSQ DCSRSSLELQ DSEQTNGNQV
3360 3370 3380 3390 3400
TQFCGANYTT LPVFYSSGST AVVVFKSDFL NRNSRVHFTY EIADCNREYN
3410 3420 3430 3440 3450
QAFGNLKSPG WPQGYANNLD CSIILRAPQN HRISLFFYWF QLEDSRQCMN
3460 3470 3480 3490 3500
DFLEVRNGSS SSSPLLGKYC SNLLPNPIFS QSNELYLHFH SDDSDTHHGY
3510 3520 3530 3540 3550
EIIWASSPTG CGGTLLGNEG ILANPGFPDS YPNNTHCEWT IVAPSGRPLS
3560 3570 3580 3590 3600
VGFPFLSIDS PGGCDQNYLI LFNGPDANSP PFGPFCGIDT VVAPFHASSN
3610 3620
RVFIRFHAEY ATVSSGFEIM WSS
Length:3,623
Mass (Da):399,097
Last modified:July 27, 2011 - v3
Checksum:iC105089FE0E0F1ED
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti811 – 8133ADY → NDL AA sequence (PubMed:11856751)Curated
Sequence conflicti819 – 8191G → S AA sequence (PubMed:11856751)Curated
Sequence conflicti822 – 8232RG → QD AA sequence (PubMed:11856751)Curated
Sequence conflicti1859 – 18591T → Q AA sequence (PubMed:11856751)Curated
Sequence conflicti2105 – 21051S → P AA sequence (PubMed:11856751)Curated
Sequence conflicti2146 – 21483SCS → YGA AA sequence (PubMed:11856751)Curated
Sequence conflicti2152 – 21521Y → L AA sequence (PubMed:11856751)Curated
Sequence conflicti2156 – 21561R → S AA sequence (PubMed:11856751)Curated
Sequence conflicti2531 – 25311N → S AA sequence (PubMed:11856751)Curated
Sequence conflicti2536 – 25383FKS → WTK AA sequence (PubMed:11856751)Curated

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 ENSGT00760000119018.
HOGENOMi HOG000049236.
HOVERGENi HBG080357.
InParanoidi Q9JLB4.
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: October 29, 2014
This is version 112 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