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Protein

Cubilin

Gene

Cubn

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: 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)DescriptionActionsGraphical viewLength
Metal bindingi980Calcium 1By similarity1
Metal bindingi988Calcium 1By similarity1
Metal bindingi1027Calcium 1By similarity1
Metal bindingi1030Calcium 1; via carbonyl oxygenBy similarity1
Metal bindingi1096Calcium 2By similarity1
Metal bindingi1105Calcium 2By similarity1
Metal bindingi1146Calcium 2By similarity1
Metal bindingi1213Calcium 3By similarity1
Metal bindingi1221Calcium 3By similarity1
Metal bindingi1262Calcium 3By similarity1
Metal bindingi1264Calcium 3; via carbonyl oxygenBy similarity1
Metal bindingi1265Calcium 3; via carbonyl oxygenBy similarity1
Metal bindingi1328Calcium 4By similarity1
Metal bindingi1336Calcium 4By similarity1
Metal bindingi1373Calcium 4By similarity1
Metal bindingi1375Calcium 4; via carbonyl oxygenBy similarity1

GO - Molecular functioni

  • calcium ion binding Source: InterPro
  • cobalamin binding Source: UniProtKB-KW
  • protein homodimerization activity Source: MGI
  • receptor activity Source: MGI

GO - Biological processi

  • cholesterol metabolic process Source: UniProtKB-KW
  • lipoprotein transport Source: MGI
  • protein transport Source: UniProtKB-KW
  • 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

ReactomeiR-MMU-194223. HDL-mediated lipid transport.
R-MMU-196741. Cobalamin (Cbl, vitamin B12) transport and metabolism.
R-MMU-196791. 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
Proteomesi
  • UP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:1931256. Cubn.

Subcellular locationi

  • Apical cell membrane 1 Publication; Peripheral membrane protein Curated
  • Cell membrane By similarity; Peripheral membrane protein By similarity
  • Membranecoated pit By similarity
  • Endosome 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

  • apical part of cell Source: MGI
  • apical plasma membrane Source: MGI
  • brush border Source: MGI
  • clathrin-coated pit Source: MGI
  • cytoplasm Source: MGI
  • endocytic vesicle Source: MGI
  • endoplasmic reticulum Source: MGI
  • endosome Source: MGI
  • extracellular exosome Source: MGI
  • Golgi apparatus Source: MGI
  • lysosomal membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Coated pit, Endosome, Lysosome, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 20Sequence analysisAdd BLAST20
PropeptideiPRO_000004607421 – 32Removed in mature formBy similarityAdd BLAST12
ChainiPRO_000004607533 – 3623CubilinAdd BLAST3591

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi95N-linked (GlcNAc...)Sequence analysis1
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
Glycosylationi428N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi436 ↔ 447By similarity
Disulfide bondi441 ↔ 456By similarity
Disulfide bondi458 ↔ 467By similarity
Disulfide bondi474 ↔ 500By similarity
Glycosylationi491N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi527 ↔ 549By similarity
Disulfide bondi590 ↔ 616By similarity
Disulfide bondi643 ↔ 665By similarity
Disulfide bondi708 ↔ 734By similarity
Glycosylationi711N-linked (GlcNAc...)Sequence analysis1
Glycosylationi749N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi761 ↔ 779By similarity
Glycosylationi781N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi817 ↔ 842By similarity
Glycosylationi857N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi869 ↔ 891By similarity
Disulfide bondi932 ↔ 958By similarity
Glycosylationi957N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi985 ↔ 1005By similarity
Glycosylationi1043N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1048 ↔ 1074By similarity
Disulfide bondi1165 ↔ 1191By similarity
Glycosylationi1168N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1217N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1218 ↔ 1240By similarity
Disulfide bondi1278 ↔ 1306By similarity
Glycosylationi1285N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1307N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1319N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1332N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1333 ↔ 1351By similarity
Disulfide bondi1391 ↔ 1417By similarity
Disulfide bondi1444 ↔ 1466By similarity
Glycosylationi1500N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1510 ↔ 1536By similarity
Glycosylationi1551N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1563 ↔ 1581By similarity
Disulfide bondi1620 ↔ 1647By similarity
Glycosylationi1646N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1675 ↔ 1697By similarity
Disulfide bondi1738 ↔ 1764By similarity
Disulfide bondi1791 ↔ 1812By similarity
Glycosylationi1802N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1819N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1905 ↔ 1927By similarity
Glycosylationi1967N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1978 ↔ 2006By similarity
Disulfide bondi2032 ↔ 2054By similarity
Glycosylationi2085N-linked (GlcNAc...)1 Publication1
Disulfide bondi2092 ↔ 2118By similarity
Glycosylationi2117N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi2217 ↔ 2247By similarity
Glycosylationi2274N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi2275 ↔ 2297By similarity
Disulfide bondi2336 ↔ 2363By similarity
Disulfide bondi2390 ↔ 2411By similarity
Glycosylationi2400N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi2452 ↔ 2478By similarity
Disulfide bondi2505 ↔ 2527By similarity
Glycosylationi2531N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi2570 ↔ 2599By similarity
Glycosylationi2581N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2610N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi2628 ↔ 2649By similarity
Disulfide bondi2689 ↔ 2715By similarity
Disulfide bondi2742 ↔ 2764By similarity
Disulfide bondi2805 ↔ 2831By similarity
Glycosylationi2813N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi2860 ↔ 2883By similarity
Disulfide bondi2920 ↔ 2946By similarity
Glycosylationi2925N-linked (GlcNAc...)1 Publication1
Disulfide bondi2977 ↔ 2999By similarity
Glycosylationi2989N-linked (GlcNAc...)Sequence analysis1
Modified residuei3008PhosphothreonineBy similarity1
Disulfide bondi3037 ↔ 3064By similarity
Disulfide bondi3091 ↔ 3113By similarity
Glycosylationi3106N-linked (GlcNAc...)Sequence analysis1
Glycosylationi3125N-linked (GlcNAc...)1 Publication1
Disulfide bondi3157 ↔ 3185By similarity
Disulfide bondi3215 ↔ 3237By similarity
Glycosylationi3268N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi3278 ↔ 3306By similarity
Glycosylationi3283N-linked (GlcNAc...)Sequence analysis1
Glycosylationi3290N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi3332 ↔ 3354By similarity
Glycosylationi3357N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi3395 ↔ 3421By similarity
Disulfide bondi3448 ↔ 3470By similarity
Glycosylationi3457N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi3511 ↔ 3537By similarity
Glycosylationi3533N-linked (GlcNAc...)Sequence analysis1
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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei32 – 33Cleavage; by furinSequence analysis2

Keywords - PTMi

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

Proteomic databases

MaxQBiQ9JLB4.
PaxDbiQ9JLB4.
PeptideAtlasiQ9JLB4.
PRIDEiQ9JLB4.

PTM databases

iPTMnetiQ9JLB4.
PhosphoSitePlusiQ9JLB4.

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

BgeeiENSMUSG00000026726.
CleanExiMM_CUBN.
GenevisibleiQ9JLB4. MM.

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

GO - Molecular functioni

Protein-protein interaction databases

BioGridi211163. 5 interactors.
IntActiQ9JLB4. 2 interactors.
MINTiMINT-4130272.
STRINGi10090.ENSMUSP00000089009.

Structurei

3D structure databases

ProteinModelPortaliQ9JLB4.
SMRiQ9JLB4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini129 – 165EGF-like 1PROSITE-ProRule annotationAdd BLAST37
Domaini167 – 208EGF-like 2; calcium-bindingPROSITE-ProRule annotationAdd BLAST42
Domaini260 – 301EGF-like 3; calcium-bindingPROSITE-ProRule annotationAdd BLAST42
Domaini302 – 345EGF-like 4; calcium-bindingPROSITE-ProRule annotationAdd BLAST44
Domaini346 – 385EGF-like 5PROSITE-ProRule annotationAdd BLAST40
Domaini395 – 430EGF-like 6PROSITE-ProRule annotationAdd BLAST36
Domaini432 – 468EGF-like 7; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini474 – 586CUB 1PROSITE-ProRule annotationAdd BLAST113
Domaini590 – 702CUB 2PROSITE-ProRule annotationAdd BLAST113
Domaini708 – 816CUB 3PROSITE-ProRule annotationAdd BLAST109
Domaini817 – 928CUB 4PROSITE-ProRule annotationAdd BLAST112
Domaini932 – 1042CUB 5PROSITE-ProRule annotationAdd BLAST111
Domaini1048 – 1161CUB 6PROSITE-ProRule annotationAdd BLAST114
Domaini1165 – 1277CUB 7PROSITE-ProRule annotationAdd BLAST113
Domaini1278 – 1389CUB 8PROSITE-ProRule annotationAdd BLAST112
Domaini1391 – 1506CUB 9PROSITE-ProRule annotationAdd BLAST116
Domaini1510 – 1619CUB 10PROSITE-ProRule annotationAdd BLAST110
Domaini1620 – 1734CUB 11PROSITE-ProRule annotationAdd BLAST115
Domaini1738 – 1850CUB 12PROSITE-ProRule annotationAdd BLAST113
Domaini1852 – 1963CUB 13PROSITE-ProRule annotationAdd BLAST112
Domaini1978 – 2091CUB 14PROSITE-ProRule annotationAdd BLAST114
Domaini2092 – 2213CUB 15PROSITE-ProRule annotationAdd BLAST122
Domaini2217 – 2334CUB 16PROSITE-ProRule annotationAdd BLAST118
Domaini2336 – 2448CUB 17PROSITE-ProRule annotationAdd BLAST113
Domaini2452 – 2565CUB 18PROSITE-ProRule annotationAdd BLAST114
Domaini2570 – 2687CUB 19PROSITE-ProRule annotationAdd BLAST118
Domaini2689 – 2801CUB 20PROSITE-ProRule annotationAdd BLAST113
Domaini2805 – 2919CUB 21PROSITE-ProRule annotationAdd BLAST115
Domaini2920 – 3035CUB 22PROSITE-ProRule annotationAdd BLAST116
Domaini3037 – 3150CUB 23PROSITE-ProRule annotationAdd BLAST114
Domaini3157 – 3274CUB 24PROSITE-ProRule annotationAdd BLAST118
Domaini3278 – 3393CUB 25PROSITE-ProRule annotationAdd BLAST116
Domaini3395 – 3507CUB 26PROSITE-ProRule annotationAdd BLAST113
Domaini3511 – 3623CUB 27PROSITE-ProRule annotationAdd BLAST113

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

eggNOGiKOG3714. Eukaryota.
ENOG410ZPX7. LUCA.
GeneTreeiENSGT00760000119018.
HOGENOMiHOG000049236.
HOVERGENiHBG080357.
InParanoidiQ9JLB4.
KOiK14616.
OMAiYSFTDCG.
OrthoDBiEOG091G009U.
TreeFamiTF316224.

Family and domain databases

CDDicd00041. CUB. 27 hits.
Gene3Di2.60.120.290. 27 hits.
InterProiIPR000859. CUB_dom.
IPR028876. Cubilin.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR024731. EGF_dom.
[Graphical view]
PANTHERiPTHR10127:SF645. PTHR10127:SF645. 5 hits.
PfamiPF00431. CUB. 27 hits.
PF00008. EGF. 2 hits.
PF12947. EGF_3. 1 hit.
PF07645. EGF_CA. 3 hits.
PF12661. hEGF. 1 hit.
[Graphical view]
SMARTiSM00042. CUB. 27 hits.
SM00181. EGF. 8 hits.
SM00179. EGF_CA. 7 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

« Hide

        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)DescriptionActionsGraphical viewLength
Sequence conflicti811 – 813ADY → NDL AA sequence (PubMed:11856751).Curated3
Sequence conflicti819G → S AA sequence (PubMed:11856751).Curated1
Sequence conflicti822 – 823RG → QD AA sequence (PubMed:11856751).Curated2
Sequence conflicti1859T → Q AA sequence (PubMed:11856751).Curated1
Sequence conflicti2105S → P AA sequence (PubMed:11856751).Curated1
Sequence conflicti2146 – 2148SCS → YGA AA sequence (PubMed:11856751).Curated3
Sequence conflicti2152Y → L AA sequence (PubMed:11856751).Curated1
Sequence conflicti2156R → S AA sequence (PubMed:11856751).Curated1
Sequence conflicti2531N → S AA sequence (PubMed:11856751).Curated1
Sequence conflicti2536 – 2538FKS → WTK AA sequence (PubMed:11856751).Curated3

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

ProteinModelPortaliQ9JLB4.
SMRiQ9JLB4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi211163. 5 interactors.
IntActiQ9JLB4. 2 interactors.
MINTiMINT-4130272.
STRINGi10090.ENSMUSP00000089009.

PTM databases

iPTMnetiQ9JLB4.
PhosphoSitePlusiQ9JLB4.

Proteomic databases

MaxQBiQ9JLB4.
PaxDbiQ9JLB4.
PeptideAtlasiQ9JLB4.
PRIDEiQ9JLB4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi8029.
MGIiMGI:1931256. Cubn.

Phylogenomic databases

eggNOGiKOG3714. Eukaryota.
ENOG410ZPX7. LUCA.
GeneTreeiENSGT00760000119018.
HOGENOMiHOG000049236.
HOVERGENiHBG080357.
InParanoidiQ9JLB4.
KOiK14616.
OMAiYSFTDCG.
OrthoDBiEOG091G009U.
TreeFamiTF316224.

Enzyme and pathway databases

ReactomeiR-MMU-194223. HDL-mediated lipid transport.
R-MMU-196741. Cobalamin (Cbl, vitamin B12) transport and metabolism.
R-MMU-196791. Vitamin D (calciferol) metabolism.

Miscellaneous databases

PROiQ9JLB4.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000026726.
CleanExiMM_CUBN.
GenevisibleiQ9JLB4. MM.

Family and domain databases

CDDicd00041. CUB. 27 hits.
Gene3Di2.60.120.290. 27 hits.
InterProiIPR000859. CUB_dom.
IPR028876. Cubilin.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR024731. EGF_dom.
[Graphical view]
PANTHERiPTHR10127:SF645. PTHR10127:SF645. 5 hits.
PfamiPF00431. CUB. 27 hits.
PF00008. EGF. 2 hits.
PF12947. EGF_3. 1 hit.
PF07645. EGF_CA. 3 hits.
PF12661. hEGF. 1 hit.
[Graphical view]
SMARTiSM00042. CUB. 27 hits.
SM00181. EGF. 8 hits.
SM00179. EGF_CA. 7 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]
ProtoNetiSearch...

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: November 30, 2016
This is version 128 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

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.