Q9NUN5 (LMBD1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Probable lysosomal cobalamin transporter

Alternative name(s):
HDAg-L-interacting protein NESI
LMBR1 domain-containing protein 1
Nuclear export signal-interacting protein

Gene names

Name:	LMBRD1
Synonyms:	C6orf209, NESI
ORF Names:	BM-021, CD001, MSTP044

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	540 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Probable lysosomal cobalamin transporter. Required to export cobalamin from lysosomes allowing its conversion to cofactors. Isoform 3 may play a role in the assembly of hepatitis delta virus (HDV). Ref.1 Ref.10
Subunit structure	Isoform 3 interacts with Hepatitis delta virus NES(HDAg-L). Ref.1
Subcellular location	Lysosome membrane; Multi-pass membrane protein Ref.10.
Tissue specificity	Isoform 3 is expressed in liver. Ref.1
Post-translational modification	N-glycosylated. Ref.10
Involvement in disease	Methylmalonic aciduria and homocystinuria type cblF (MMAHCF) [MIM:277380]: A disorder of cobalamin metabolism characterized by decreased levels of the coenzymes adenosylcobalamin (AdoCbl) and methylcobalamin (MeCbl). It is due to accumulation of free cobalamin in lysosomes, thus hindering its conversion to cofactors. Clinical features include developmental delay, stomatitis, glossitis, seizures and methylmalonic aciduria responsive to vitamin B12. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.10
Sequence similarities	Belongs to the LIMR family. LMBRD1 subfamily.
Sequence caution	The sequence AAK26247.1 differs from that shown. Reason: Frameshift at position 137.

Ontologies

Keywords
Biological process	Host-virus interaction Transport
Cellular component	Lysosome Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Transmembrane Transmembrane helix
Ligand	Cobalamin Cobalt
PTM	Glycoprotein Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	transport Inferred from electronic annotation. Source: UniProtKB-KW virus-host interaction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW lysosomal membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	cobalamin binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9NUN5-1)

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.

Isoform 2 (identifier: Q9NUN5-2)

The sequence of this isoform differs from the canonical sequence as follows:
     362-392: VFPLDYILITIIIMYFIFTSMAGIRNIGIWF → EFEILAYGSFGLDYIKSEEVEPGPKHSFFSA
     393-540: Missing.

Note: No experimental confirmation available.

Isoform 3 (identifier: Q9NUN5-3)

Also known as: NESI;

The sequence of this isoform differs from the canonical sequence as follows:
     1-73: Missing.

Isoform 4 (identifier: Q9NUN5-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-204: Missing.
     362-392: VFPLDYILITIIIMYFIFTSMAGIRNIGIWF → EFEILAYGSFGLDYIKSEEVEPGPKHSFFSA
     393-540: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 540	540	Probable lysosomal cobalamin transporter		PRO_0000260515
Regions
	Topological domain	1 – 10	10	Extracellular Potential
	Transmembrane	11 – 31	21	Helical; Name=1; Potential
	Topological domain	32 – 50	19	Cytoplasmic Potential
	Transmembrane	51 – 71	21	Helical; Name=2; Potential
	Topological domain	72 – 100	29	Extracellular Potential
	Transmembrane	101 – 121	21	Helical; Name=3; Potential
	Topological domain	122 – 144	23	Cytoplasmic Potential
	Transmembrane	145 – 165	21	Helical; Name=4; Potential
	Topological domain	166 – 188	23	Extracellular Potential
	Transmembrane	189 – 209	21	Helical; Name=5; Potential
	Topological domain	210 – 305	96	Cytoplasmic Potential
	Transmembrane	306 – 326	21	Helical; Name=6; Potential
	Topological domain	327 – 364	38	Extracellular Potential
	Transmembrane	365 – 385	21	Helical; Name=7; Potential
	Topological domain	386 – 408	23	Cytoplasmic Potential
	Transmembrane	409 – 429	21	Helical; Name=8; Potential
	Topological domain	430 – 486	57	Extracellular Potential
	Transmembrane	487 – 507	21	Helical; Name=9; Potential
	Topological domain	508 – 540	33	Cytoplasmic Potential
Amino acid modifications
	Modified residue	238	1	Phosphothreonine By similarity
	Modified residue	528	1	Phosphoserine Ref.9 Ref.11
	Modified residue	531	1	Phosphoserine Ref.9 Ref.11
	Glycosylation	78	1	N-linked (GlcNAc...) Potential
	Glycosylation	88	1	N-linked (GlcNAc...) Potential
	Glycosylation	170	1	N-linked (GlcNAc...) Potential
	Glycosylation	347	1	N-linked (GlcNAc...) Potential
	Glycosylation	448	1	N-linked (GlcNAc...) Potential
	Glycosylation	457	1	N-linked (GlcNAc...) Probable
Natural variations
	Alternative sequence	1 – 204	204	Missing in isoform 4.		VSP_036539
	Alternative sequence	1 – 73	73	Missing in isoform 3.		VSP_021629
	Alternative sequence	362 – 392	31	VFPLD…IGIWF → EFEILAYGSFGLDYIKSEEV EPGPKHSFFSA in isoform 2 and isoform 4.		VSP_021630
	Alternative sequence	393 – 540	148	Missing in isoform 2 and isoform 4.		VSP_036540
	Natural variant	144	1	T → A. Corresponds to variant rs12214456 [ dbSNP | Ensembl ].		VAR_029047
	Natural variant	395	1	I → V. Ref.7 Corresponds to variant rs17854411 [ dbSNP | Ensembl ].		VAR_029048
	Natural variant	469	1	D → E. Corresponds to variant rs9354880 [ dbSNP | Ensembl ].		VAR_029049
Experimental info
	Mutagenesis	78	1	N → Q: Does not affect glycosylation status; when associated with Q-88. Ref.10
	Mutagenesis	88	1	N → Q: Does not affect glycosylation status; when associated with Q-78. Ref.10
	Mutagenesis	448	1	N → Q: Affects glycosylation status; when associated with Q-457. Ref.10
	Mutagenesis	457	1	N → Q: Affects glycosylation status. Affects glycosylation status; when associated with Q-448. Ref.10

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: CC7578B0F5FD7BA6	FASTA	540	61,389
	10 20 30 40 50 60 MATSGAASAE LVIGWCIFGL LLLAILAFCW IYVRKYQSRR ESEVVSTITA IFSLAIALIT 70 80 90 100 110 120 SALLPVDIFL VSYMKNQNGT FKDWANANVS RQIEDTVLYG YYTLYSVILF CVFFWIPFVY 130 140 150 160 170 180 FYYEEKDDDD TSKCTQIKTA LKYTLGFVVI CALLLLVGAF VPLNVPNNKN STEWEKVKSL 190 200 210 220 230 240 FEELGSSHGL AALSFSISSL TLIGMLAAIT YTAYGMSALP LNLIKGTRSA AYERLENTED 250 260 270 280 290 300 IEEVEQHIQT IKSKSKDGRP LPARDKRALK QFEERLRTLK KRERHLEFIE NSWWTKFCGA 310 320 330 340 350 360 LRPLKIVWGI FFILVALLFV ISLFLSNLDK ALHSAGIDSG FIIFGANLSN PLNMLLPLLQ 370 380 390 400 410 420 TVFPLDYILI TIIIMYFIFT SMAGIRNIGI WFFWIRLYKI RRGRTRPQAL LFLCMILLLI 430 440 450 460 470 480 VLHTSYMIYS LAPQYVMYGS QNYLIETNIT SDNHKGNSTL SVPKRCDADA PEDQCTVTRT 490 500 510 520 530 540 YLFLHKFWFF SAAYYFGNWA FLGVFLIGLI VSCCKGKKSV IEGVDEDSDI SDDEPSVYSA
	Isoform 2 [UniParc]. Checksum: 6DE93B0127AC0BE5	FASTA	392	44,211
	10 20 30 40 50 60 MATSGAASAE LVIGWCIFGL LLLAILAFCW IYVRKYQSRR ESEVVSTITA IFSLAIALIT 70 80 90 100 110 120 SALLPVDIFL VSYMKNQNGT FKDWANANVS RQIEDTVLYG YYTLYSVILF CVFFWIPFVY 130 140 150 160 170 180 FYYEEKDDDD TSKCTQIKTA LKYTLGFVVI CALLLLVGAF VPLNVPNNKN STEWEKVKSL 190 200 210 220 230 240 FEELGSSHGL AALSFSISSL TLIGMLAAIT YTAYGMSALP LNLIKGTRSA AYERLENTED 250 260 270 280 290 300 IEEVEQHIQT IKSKSKDGRP LPARDKRALK QFEERLRTLK KRERHLEFIE NSWWTKFCGA 310 320 330 340 350 360 LRPLKIVWGI FFILVALLFV ISLFLSNLDK ALHSAGIDSG FIIFGANLSN PLNMLLPLLQ 370 380 390 TEFEILAYGS FGLDYIKSEE VEPGPKHSFF SA
	Isoform 3 (NESI) [UniParc]. Checksum: 51C91051CD071AC5	FASTA	467	53,435
	10 20 30 40 50 60 MKNQNGTFKD WANANVSRQI EDTVLYGYYT LYSVILFCVF FWIPFVYFYY EEKDDDDTSK 70 80 90 100 110 120 CTQIKTALKY TLGFVVICAL LLLVGAFVPL NVPNNKNSTE WEKVKSLFEE LGSSHGLAAL 130 140 150 160 170 180 SFSISSLTLI GMLAAITYTA YGMSALPLNL IKGTRSAAYE RLENTEDIEE VEQHIQTIKS 190 200 210 220 230 240 KSKDGRPLPA RDKRALKQFE ERLRTLKKRE RHLEFIENSW WTKFCGALRP LKIVWGIFFI 250 260 270 280 290 300 LVALLFVISL FLSNLDKALH SAGIDSGFII FGANLSNPLN MLLPLLQTVF PLDYILITII 310 320 330 340 350 360 IMYFIFTSMA GIRNIGIWFF WIRLYKIRRG RTRPQALLFL CMILLLIVLH TSYMIYSLAP 370 380 390 400 410 420 QYVMYGSQNY LIETNITSDN HKGNSTLSVP KRCDADAPED QCTVTRTYLF LHKFWFFSAA 430 440 450 460 YYFGNWAFLG VFLIGLIVSC CKGKKSVIEG VDEDSDISDD EPSVYSA
	Isoform 4 [UniParc]. Checksum: 028B19ED4912A09C	FASTA	188	21,394
	10 20 30 40 50 60 MLAAITYTAY GMSALPLNLI KGTRSAAYER LENTEDIEEV EQHIQTIKSK SKDGRPLPAR 70 80 90 100 110 120 DKRALKQFEE RLRTLKKRER HLEFIENSWW TKFCGALRPL KIVWGIFFIL VALLFVISLF 130 140 150 160 170 180 LSNLDKALHS AGIDSGFIIF GANLSNPLNM LLPLLQTEFE ILAYGSFGLD YIKSEEVEPG PKHSFFSA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Novel nuclear export signal-interacting protein, NESI, critical for the assembly of hepatitis delta virus." Wang Y.-H., Chang S.C., Huang C., Li Y.-P., Lee C.-H., Chang M.-F. J. Virol. 79:8113-8120(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION, TISSUE SPECIFICITY, INTERACTION WITH HDAG-L.
[2]	Liu B., Liu Y.Q., Wang X.Y., Zhao B., Sheng H., Zhao X.W., Liu S., Xu Y.Y., Ye J., Song L., Gao Y., Zhang C.L., Zhang J., Wei Y.J., Cao H.Q., Zhao Y., Liu L.S., Ding J.F. , Gao R.L., Wu Q.Y., Qiang B.Q., Yuan J.G., Liew C.C., Zhao M.S., Hui R.T. Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3). Tissue: Heart.
[3]	"Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells." Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., Tao J., Huang Q.-H., Zhou J., Hu G.-X. , Gu J., Chen S.-J., Chen Z. Genome Res. 10:1546-1560(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). Tissue: Bone marrow.
[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: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3). Tissue: Placenta and Substantia nigra.
[5]	"The DNA sequence and analysis of human chromosome 6." Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S. Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"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] (ISOFORMS 1 AND 4), VARIANT VAL-395. Tissue: Brain.
[8]	"A novel gene expressed in human pheochromocytoma." Li N., Song H., Peng Y., Xiao H., Han Z., Chen Z. Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 130-540 (ISOFORMS 1/3). Tissue: Pheochromocytoma.
[9]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-528 AND SER-531, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"Identification of a putative lysosomal cobalamin exporter altered in the cblF defect of vitamin B12 metabolism." Rutsch F., Gailus S., Miousse I.R., Suormala T., Sagne C., Toliat M.R., Nuernberg G., Wittkampf T., Buers I., Sharifi A., Stucki M., Becker C., Baumgartner M., Robenek H., Marquardt T., Hoehne W., Gasnier B., Rosenblatt D.S., Fowler B., Nuernberg P. Nat. Genet. 41:234-239(2009) [PubMed] [Europe PMC] [Abstract] Cited for: INVOLVEMENT IN MMAHCF, FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, GLYCOSYLATION, MUTAGENESIS OF ASN-78; ASN-88; ASN-448 AND ASN-457.
[11]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-528 AND SER-531, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AY136817 mRNA. Translation: AAN11301.1. AF113224 mRNA. Translation: AAG39295.1. AF208863 mRNA. Translation: AAF64277.1. AK002102 mRNA. Translation: BAA92087.1. AK290069 mRNA. Translation: BAF82758.1. AL583831, AL358133, AL590702 Genomic DNA. Translation: CAH74081.1. AL583831, AL358133, AL590702 Genomic DNA. Translation: CAH74083.1. AL358133, AL583831, AL590702 Genomic DNA. Translation: CAI16835.1. AL358133, AL583831, AL590702 Genomic DNA. Translation: CAI16836.1. AL590702, AL358133, AL583831 Genomic DNA. Translation: CAI17314.1. AL590702, AL358133, AL583831 Genomic DNA. Translation: CAI17316.1. CH471051 Genomic DNA. Translation: EAW48832.1. CH471051 Genomic DNA. Translation: EAW48833.1. CH471051 Genomic DNA. Translation: EAW48835.1. BC010360 mRNA. Translation: AAH10360.1. BC047073 mRNA. Translation: AAH47073.1. AF211480 mRNA. Translation: AAK26247.1. Frameshift.
IPI	IPI00020007. IPI00640628. IPI00807437. IPI00871937.
RefSeq	NP_060838.3. NM_018368.3.
UniGene	Hs.271643. Hs.736005.
3D structure databases
ProteinModelPortal	Q9NUN5.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9NUN5. 1 interaction.
STRING	9606.ENSP00000359609.
Protein family/group databases
TCDB	9.A.54.1.1. lysosomal cobalamin (B12) transporter (L-B12T) family.
PTM databases
PhosphoSite	Q9NUN5.
Polymorphism databases
DMDM	74752981.
Proteomic databases
PaxDb	Q9NUN5.
PRIDE	Q9NUN5.
Protocols and materials databases
DNASU	55788.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000370570; ENSP00000359602; ENSG00000168216. ENST00000370577; ENSP00000359609; ENSG00000168216. ENST00000472827; ENSP00000433385; ENSG00000168216.
GeneID	55788.
KEGG	hsa:55788.
UCSC	uc003pez.3. human.
Organism-specific databases
CTD	55788.
GeneCards	GC06M070385.
HGNC	HGNC:23038. LMBRD1.
HPA	HPA019547.
MIM	277380. phenotype. 612625. gene.
neXtProt	NX_Q9NUN5.
Orphanet	79284. Methylmalonic acidemia with homocystinuria, type cblF.
PharmGKB	PA134948847.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG87911.
HOVERGEN	HBG059142.
KO	K14617.
OMA	ADAPEDQ.
OrthoDB	EOG4933HV.
PhylomeDB	Q9NUN5.
Gene expression databases
Bgee	Q9NUN5.
CleanEx	HS_LMBRD1.
Genevestigator	Q9NUN5.
GermOnline	ENSG00000168216. Homo sapiens.
Family and domain databases
InterPro	IPR006876. LMBR1-like_membr_prot. [Graphical view]
Pfam	PF04791. LMBR1. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	LMBRD1. human.
GenomeRNAi	55788.
NextBio	60892.
SOURCE	Search...

Entry information

Entry name

LMBD1_HUMAN

Accession

Primary (citable) accession number: Q9NUN5
Secondary accession number(s): A8K204 , E1P531, Q5VUN6, Q86Y70, Q96FW4, Q9BY56, Q9NZD6

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 28, 2006
Last sequence update:	October 1, 2000
Last modified:	May 1, 2013
This is version 94 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.