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Protein

Probable lysosomal cobalamin transporter

Gene

LMBRD1

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

Functioni

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).2 Publications

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Host-virus interaction, Transport

Keywords - Ligandi

Cobalamin, Cobalt

Enzyme and pathway databases

ReactomeiREACT_163862. Cobalamin (Cbl, vitamin B12) transport and metabolism.
REACT_169363. Defective LMBRD1 causes methylmalonic aciduria and homocystinuria type cblF.

Protein family/group databases

TCDBi9.A.54.1.1. the lysosomal cobalamin (b12) transporter (l-b12t) family.

Names & Taxonomyi

Protein namesi
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 namesi
Name:LMBRD1
Synonyms:C6orf209, NESI
ORF Names:BM-021, CD001, MSTP044
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 6

Organism-specific databases

HGNCiHGNC:23038. LMBRD1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1010ExtracellularSequence Analysis
Transmembranei11 – 3121Helical; Name=1Sequence AnalysisAdd
BLAST
Topological domaini32 – 5019CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei51 – 7121Helical; Name=2Sequence AnalysisAdd
BLAST
Topological domaini72 – 10029ExtracellularSequence AnalysisAdd
BLAST
Transmembranei101 – 12121Helical; Name=3Sequence AnalysisAdd
BLAST
Topological domaini122 – 14423CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei145 – 16521Helical; Name=4Sequence AnalysisAdd
BLAST
Topological domaini166 – 18823ExtracellularSequence AnalysisAdd
BLAST
Transmembranei189 – 20921Helical; Name=5Sequence AnalysisAdd
BLAST
Topological domaini210 – 30596CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei306 – 32621Helical; Name=6Sequence AnalysisAdd
BLAST
Topological domaini327 – 36438ExtracellularSequence AnalysisAdd
BLAST
Transmembranei365 – 38521Helical; Name=7Sequence AnalysisAdd
BLAST
Topological domaini386 – 40823CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei409 – 42921Helical; Name=8Sequence AnalysisAdd
BLAST
Topological domaini430 – 48657ExtracellularSequence AnalysisAdd
BLAST
Transmembranei487 – 50721Helical; Name=9Sequence AnalysisAdd
BLAST
Topological domaini508 – 54033CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Lysosome, Membrane

Pathology & Biotechi

Involvement in diseasei

Methylmalonic aciduria and homocystinuria type cblF (MMAHCF)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA 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.

See also OMIM:277380

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi78 – 781N → Q: Does not affect glycosylation status; when associated with Q-88. 1 Publication
Mutagenesisi88 – 881N → Q: Does not affect glycosylation status; when associated with Q-78. 1 Publication
Mutagenesisi448 – 4481N → Q: Affects glycosylation status; when associated with Q-457. 1 Publication
Mutagenesisi457 – 4571N → Q: Affects glycosylation status. Affects glycosylation status; when associated with Q-448. 1 Publication

Organism-specific databases

MIMi277380. phenotype.
Orphaneti79284. Methylmalonic acidemia with homocystinuria type cblF.
PharmGKBiPA134948847.

Polymorphism and mutation databases

BioMutaiLMBRD1.
DMDMi74752981.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 540540Probable lysosomal cobalamin transporterPRO_0000260515Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi78 – 781N-linked (GlcNAc...)Sequence Analysis
Glycosylationi88 – 881N-linked (GlcNAc...)Sequence Analysis
Glycosylationi170 – 1701N-linked (GlcNAc...)Sequence Analysis
Modified residuei238 – 2381PhosphothreonineBy similarity
Glycosylationi347 – 3471N-linked (GlcNAc...)Sequence Analysis
Glycosylationi448 – 4481N-linked (GlcNAc...)Sequence Analysis
Glycosylationi457 – 4571N-linked (GlcNAc...)1 Publication
Modified residuei528 – 5281Phosphoserine2 Publications
Modified residuei531 – 5311Phosphoserine2 Publications

Post-translational modificationi

N-glycosylated.1 Publication

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiQ9NUN5.
PaxDbiQ9NUN5.
PRIDEiQ9NUN5.

PTM databases

PhosphoSiteiQ9NUN5.

Expressioni

Tissue specificityi

Isoform 3 is expressed in liver.1 Publication

Gene expression databases

BgeeiQ9NUN5.
CleanExiHS_LMBRD1.
GenevisibleiQ9NUN5. HS.

Organism-specific databases

HPAiHPA019547.

Interactioni

Subunit structurei

Isoform 3 interacts with Hepatitis delta virus NES(HDAg-L).1 Publication

Protein-protein interaction databases

BioGridi120902. 2 interactions.
IntActiQ9NUN5. 1 interaction.
STRINGi9606.ENSP00000359609.

Structurei

3D structure databases

ProteinModelPortaliQ9NUN5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the LIMR family. LMBRD1 subfamily.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG87911.
GeneTreeiENSGT00390000002581.
HOVERGENiHBG059142.
InParanoidiQ9NUN5.
KOiK14617.
OMAiCTQIKTA.
OrthoDBiEOG7BKCTF.
PhylomeDBiQ9NUN5.
TreeFamiTF329170.

Family and domain databases

InterProiIPR006876. LMBR1-like_membr_prot.
[Graphical view]
PfamiPF04791. LMBR1. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9NUN5-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MATSGAASAE LVIGWCIFGL LLLAILAFCW IYVRKYQSRR ESEVVSTITA
60 70 80 90 100
IFSLAIALIT SALLPVDIFL VSYMKNQNGT FKDWANANVS RQIEDTVLYG
110 120 130 140 150
YYTLYSVILF CVFFWIPFVY FYYEEKDDDD TSKCTQIKTA LKYTLGFVVI
160 170 180 190 200
CALLLLVGAF VPLNVPNNKN STEWEKVKSL FEELGSSHGL AALSFSISSL
210 220 230 240 250
TLIGMLAAIT YTAYGMSALP LNLIKGTRSA AYERLENTED IEEVEQHIQT
260 270 280 290 300
IKSKSKDGRP LPARDKRALK QFEERLRTLK KRERHLEFIE NSWWTKFCGA
310 320 330 340 350
LRPLKIVWGI FFILVALLFV ISLFLSNLDK ALHSAGIDSG FIIFGANLSN
360 370 380 390 400
PLNMLLPLLQ TVFPLDYILI TIIIMYFIFT SMAGIRNIGI WFFWIRLYKI
410 420 430 440 450
RRGRTRPQAL LFLCMILLLI VLHTSYMIYS LAPQYVMYGS QNYLIETNIT
460 470 480 490 500
SDNHKGNSTL SVPKRCDADA PEDQCTVTRT YLFLHKFWFF SAAYYFGNWA
510 520 530 540
FLGVFLIGLI VSCCKGKKSV IEGVDEDSDI SDDEPSVYSA
Length:540
Mass (Da):61,389
Last modified:October 1, 2000 - v1
Checksum:iCC7578B0F5FD7BA6
GO
Isoform 2 (identifier: Q9NUN5-2) [UniParc]FASTAAdd to basket

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

Note: No experimental confirmation available.
Show »
Length:392
Mass (Da):44,211
Checksum:i6DE93B0127AC0BE5
GO
Isoform 3 (identifier: Q9NUN5-3) [UniParc]FASTAAdd to basket

Also known as: NESI

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

Show »
Length:467
Mass (Da):53,435
Checksum:i51C91051CD071AC5
GO
Isoform 4 (identifier: Q9NUN5-4) [UniParc]FASTAAdd to basket

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.
Show »
Length:188
Mass (Da):21,394
Checksum:i028B19ED4912A09C
GO

Sequence cautioni

The sequence AAK26247.1 differs from that shown. Reason: Frameshift at position 137. Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti144 – 1441T → A.
Corresponds to variant rs12214456 [ dbSNP | Ensembl ].
VAR_029047
Natural varianti395 – 3951I → V.1 Publication
Corresponds to variant rs17854411 [ dbSNP | Ensembl ].
VAR_029048
Natural varianti469 – 4691D → E.
Corresponds to variant rs9354880 [ dbSNP | Ensembl ].
VAR_029049

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 204204Missing in isoform 4. 1 PublicationVSP_036539Add
BLAST
Alternative sequencei1 – 7373Missing in isoform 3. 4 PublicationsVSP_021629Add
BLAST
Alternative sequencei362 – 39231VFPLD…IGIWF → EFEILAYGSFGLDYIKSEEV EPGPKHSFFSA in isoform 2 and isoform 4. 1 PublicationVSP_021630Add
BLAST
Alternative sequencei393 – 540148Missing in isoform 2 and isoform 4. 1 PublicationVSP_036540Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS4969.1. [Q9NUN5-1]
RefSeqiNP_060838.3. NM_018368.3. [Q9NUN5-1]
UniGeneiHs.271643.
Hs.736005.

Genome annotation databases

EnsembliENST00000370570; ENSP00000359602; ENSG00000168216. [Q9NUN5-3]
ENST00000370577; ENSP00000359609; ENSG00000168216. [Q9NUN5-1]
ENST00000472827; ENSP00000433385; ENSG00000168216. [Q9NUN5-2]
GeneIDi55788.
KEGGihsa:55788.
UCSCiuc003pez.3. human. [Q9NUN5-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS4969.1. [Q9NUN5-1]
RefSeqiNP_060838.3. NM_018368.3. [Q9NUN5-1]
UniGeneiHs.271643.
Hs.736005.

3D structure databases

ProteinModelPortaliQ9NUN5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi120902. 2 interactions.
IntActiQ9NUN5. 1 interaction.
STRINGi9606.ENSP00000359609.

Protein family/group databases

TCDBi9.A.54.1.1. the lysosomal cobalamin (b12) transporter (l-b12t) family.

PTM databases

PhosphoSiteiQ9NUN5.

Polymorphism and mutation databases

BioMutaiLMBRD1.
DMDMi74752981.

Proteomic databases

MaxQBiQ9NUN5.
PaxDbiQ9NUN5.
PRIDEiQ9NUN5.

Protocols and materials databases

DNASUi55788.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000370570; ENSP00000359602; ENSG00000168216. [Q9NUN5-3]
ENST00000370577; ENSP00000359609; ENSG00000168216. [Q9NUN5-1]
ENST00000472827; ENSP00000433385; ENSG00000168216. [Q9NUN5-2]
GeneIDi55788.
KEGGihsa:55788.
UCSCiuc003pez.3. human. [Q9NUN5-1]

Organism-specific databases

CTDi55788.
GeneCardsiGC06M070385.
GeneReviewsiLMBRD1.
HGNCiHGNC:23038. LMBRD1.
HPAiHPA019547.
MIMi277380. phenotype.
612625. gene.
neXtProtiNX_Q9NUN5.
Orphaneti79284. Methylmalonic acidemia with homocystinuria type cblF.
PharmGKBiPA134948847.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG87911.
GeneTreeiENSGT00390000002581.
HOVERGENiHBG059142.
InParanoidiQ9NUN5.
KOiK14617.
OMAiCTQIKTA.
OrthoDBiEOG7BKCTF.
PhylomeDBiQ9NUN5.
TreeFamiTF329170.

Enzyme and pathway databases

ReactomeiREACT_163862. Cobalamin (Cbl, vitamin B12) transport and metabolism.
REACT_169363. Defective LMBRD1 causes methylmalonic aciduria and homocystinuria type cblF.

Miscellaneous databases

ChiTaRSiLMBRD1. human.
GeneWikiiLMBRD1.
GenomeRNAii55788.
NextBioi60892.
PROiQ9NUN5.
SOURCEiSearch...

Gene expression databases

BgeeiQ9NUN5.
CleanExiHS_LMBRD1.
GenevisibleiQ9NUN5. HS.

Family and domain databases

InterProiIPR006876. LMBR1-like_membr_prot.
[Graphical view]
PfamiPF04791. LMBR1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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. 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. Cited for: INVOLVEMENT IN MMAHCF, FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, GLYCOSYLATION, MUTAGENESIS OF ASN-78; ASN-88; ASN-448 AND ASN-457.
  12. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.

Entry informationi

Entry nameiLMBD1_HUMAN
AccessioniPrimary (citable) accession number: Q9NUN5
Secondary accession number(s): A8K204
, E1P531, Q5VUN6, Q86Y70, Q96FW4, Q9BY56, Q9NZD6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 28, 2006
Last sequence update: October 1, 2000
Last modified: June 24, 2015
This is version 113 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

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

External Data

Dasty 3

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 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.