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Q8NA29 (NLS1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 90. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Sodium-dependent lysophosphatidylcholine symporter 1

Short name=NLS1
Short name=Sodium-dependent LPC symporter 1
Alternative name(s):
Major facilitator superfamily domain-containing protein 2A
Gene names
Name:MFSD2A
Synonyms:MFSD2, NLS1
ORF Names:HMFN0656, PP9177, UNQ300/PRO341
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length543 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Sodium-dependent lysophosphatidylcholine (LPC) symporter, which plays an essential role for blood-brain barrier formation and function. Specifically expressed in endothelium of the blood-brain barrier of micro-vessels and transports LPC into the brain. Transport of LPC is essential because it constitutes the major mechanism by which docosahexaenoic acid (DHA), an omega-3 fatty acid that is essential for normal brain growth and cognitive function, enters the brain. Transports LPC carrying long-chain fatty acids such LPC oleate and LPC palmitate with a minimum acyl chain length of 14 carbons. Does not transport docosahexaenoic acid in unesterified fatty acid. Specifically required for blood-brain barrier formation and function, probably by mediating lipid transport. Not required for central nervous system vascular morphogenesis By similarity. Acts as a transporter for tunicamycin, an inhibitor of asparagine-linked glycosylation. In placenta, acts as a receptor for ERVFRD-1/syncytin-2 and is required for trophoblast fusion (Ref.10). Ref.10 Ref.11 Ref.12

Subunit structure

Interacts with ERVFRD-1/syncytin-2. Ref.10

Subcellular location

Cell membrane; Multi-pass membrane protein. Endoplasmic reticulum membrane By similarity; Multi-pass membrane protein Potential. Note: Cytoplasmic punctae that may represent vesicles shuttling between the endoplasmic reticulum and the plasma membrane (Ref.11). Ref.10 Ref.11

Tissue specificity

In placenta, associated with trophoblast cells. Ref.10

Post-translational modification

N-glycosylated. Ref.11

Sequence similarities

Belongs to the major facilitator superfamily.

Ontologies

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8NA29-1)

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: Q8NA29-2)

The sequence of this isoform differs from the canonical sequence as follows:
     77-89: Missing.
Isoform 3 (identifier: Q8NA29-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-186: MAKGEGAESG...PYSALTMFIS → MWLRWALSLP...PTRLSPCSSA
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 543543Sodium-dependent lysophosphatidylcholine symporter 1
PRO_0000273387

Regions

Topological domain1 – 4646Extracellular Potential
Transmembrane47 – 6721Helical; Potential
Topological domain68 – 8013Cytoplasmic Potential
Transmembrane81 – 10121Helical; Potential
Topological domain102 – 12827Extracellular Potential
Transmembrane129 – 14921Helical; Potential
Topological domain150 – 16011Cytoplasmic Potential
Transmembrane161 – 18121Helical; Potential
Topological domain182 – 25675Extracellular Potential
Transmembrane257 – 27721Helical; Potential
Topological domain278 – 31033Cytoplasmic Potential
Transmembrane311 – 33121Helical; Potential
Topological domain332 – 34413Extracellular Potential
Transmembrane345 – 36521Helical; Potential
Topological domain366 – 3705Cytoplasmic Potential
Transmembrane371 – 39121Helical; Potential
Topological domain392 – 3932Extracellular Potential
Transmembrane394 – 41421Helical; Potential
Topological domain415 – 43723Cytoplasmic Potential
Transmembrane438 – 45821Helical; Potential
Topological domain459 – 48022Extracellular Potential
Transmembrane481 – 50121Helical; Potential
Topological domain502 – 54342Cytoplasmic Potential
Compositional bias35 – 384Poly-Lys

Amino acid modifications

Glycosylation2301N-linked (GlcNAc...) Probable
Glycosylation2401N-linked (GlcNAc...) Probable

Natural variations

Alternative sequence1 – 186186MAKGE…TMFIS → MWLRWALSLPPSSCLWAEPG MPSQTPWWASASANPPGPAW VALCPGSSSPRPWPSLPTSS SGSCPTSHTARPIGTCFSIA SLKQWSRVSMFPTRLSPCSS A in isoform 3.
VSP_022540
Alternative sequence77 – 8913Missing in isoform 2.
VSP_022539

Experimental info

Mutagenesis1031R → A: No effect on cell sensitivity toward tunicamycin. Ref.11
Mutagenesis1061D → A: No effect on cell sensitivity toward tunicamycin. Ref.11
Mutagenesis1101D → A: Drastic loss of cell sensitivity toward tunicamycin. Ref.11
Mutagenesis2301N → Q: Loss of glycosylation; when associated with Q-240. Ref.11
Mutagenesis2401N → Q: Loss of glycosylation; when associated with Q-230. Ref.11
Mutagenesis4491K → A: Loss of plasma membrane localization. Loss of cell sensitivity toward tunicamycin. Ref.11
Sequence conflict2291L → F in AAQ88999. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: C9933B79335BFBDE

FASTA54360,170
        10         20         30         40         50         60 
MAKGEGAESG SAAGLLPTSI LQSTERPAQV KKEPKKKKQQ LSVCNKLCYA LGGAPYQVTG 

        70         80         90        100        110        120 
CALGFFLQIY LLDVAQKDEE VVFCFSSFQV GPFSASIILF VGRAWDAITD PLVGLCISKS 

       130        140        150        160        170        180 
PWTCLGRLMP WIIFSTPLAV IAYFLIWFVP DFPHGQTYWY LLFYCLFETM VTCFHVPYSA 

       190        200        210        220        230        240 
LTMFISTEQT ERDSATAYRM TVEVLGTVLG TAIQGQIVGQ ADTPCFQDLN SSTVASQSAN 

       250        260        270        280        290        300 
HTHGTTSHRE TQKAYLLAAG VIVCIYIICA VILILGVREQ REPYEAQQSE PIAYFRGLRL 

       310        320        330        340        350        360 
VMSHGPYIKL ITGFLFTSLA FMLVEGNFVL FCTYTLGFRN EFQNLLLAIM LSATLTIPIW 

       370        380        390        400        410        420 
QWFLTRFGKK TAVYVGISSA VPFLILVALM ESNLIITYAV AVAAGISVAA AFLLPWSMLP 

       430        440        450        460        470        480 
DVIDDFHLKQ PHFHGTEPIF FSFYVFFTKF ASGVSLGIST LSLDFAGYQT RGCSQPERVK 

       490        500        510        520        530        540 
FTLNMLVTMA PIVLILLGLL LFKMYPIDEE RRRQNKKALQ ALRDEASSSG CSETDSTELA 


SIL 

« Hide

Isoform 2 [UniParc].

Checksum: 3B6978F4EA92C763
Show »

FASTA53058,624
Isoform 3 [UniParc].

Checksum: 4C470B6380870E38
Show »

FASTA45850,230

References

« Hide 'large scale' references
[1]"The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment."
Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E. expand/collapse author list , Heldens S., Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.
Genome Res. 13:2265-2270(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
[2]"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. expand/collapse author list , 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 2).
Tissue: Placenta and Testis.
[3]"Expression profiling and differential screening between hepatoblastomas and the corresponding normal livers: identification of high expression of the PLK1 oncogene as a poor-prognostic indicator of hepatoblastomas."
Yamada S., Ohira M., Horie H., Ando K., Takayasu H., Suzuki Y., Sugano S., Hirata T., Goto T., Matsunaga T., Hiyama E., Hayashi Y., Ando H., Suita S., Kaneko M., Sasaki F., Hashizume K., Ohnuma N., Nakagawara A.
Oncogene 23:5901-5911(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Hepatoblastoma.
[4]"Large-scale cDNA transfection screening for genes related to cancer development and progression."
Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X., Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X. expand/collapse author list , Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.
Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
[5]"Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries."
Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J., Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S., Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y. expand/collapse author list , Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S., Isogai T.
DNA Res. 12:117-126(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
[6]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]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. expand/collapse author list , 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].
[8]"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] (ISOFORM 2).
Tissue: Eye, Muscle and Testis.
[9]"Mfsd2a encodes a novel major facilitator superfamily domain-containing protein highly induced in brown adipose tissue during fasting and adaptive thermogenesis."
Angers M., Uldry M., Kong D., Gimble J.M., Jetten A.M.
Biochem. J. 416:347-355(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION.
[10]"A placenta-specific receptor for the fusogenic, endogenous retrovirus-derived, human syncytin-2."
Esnault C., Priet S., Ribet D., Vernochet C., Bruls T., Lavialle C., Weissenbach J., Heidmann T.
Proc. Natl. Acad. Sci. U.S.A. 105:17532-17537(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, TISSUE SPECIFICITY, INTERACTION WITH ERVFRD-1.
[11]"A haploid genetic screen identifies the major facilitator domain containing 2A (MFSD2A) transporter as a key mediator in the response to tunicamycin."
Reiling J.H., Clish C.B., Carette J.E., Varadarajan M., Brummelkamp T.R., Sabatini D.M.
Proc. Natl. Acad. Sci. U.S.A. 108:11756-11765(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, GLYCOSYLATION AT ASN-230 AND ASN-240, MUTAGENESIS OF ARG-103; ASP-106; ASP-110; ASN-230; ASN-240 AND LYS-449.
[12]"MFSD2a, the Syncytin-2 receptor, is important for trophoblast fusion."
Toufaily C., Vargas A., Lemire M., Lafond J., Rassart E., Barbeau B.
Placenta 34:85-88(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY358636 mRNA. Translation: AAQ88999.1.
AK093223 mRNA. Translation: BAC04100.1.
AB073383 mRNA. Translation: BAD38634.1.
AF289609 mRNA. Translation: AAL55793.1.
AK075183 mRNA. Translation: BAC11456.1.
AK291540 mRNA. Translation: BAF84229.1.
AL663070 Genomic DNA. Translation: CAI20268.1.
AL663070 Genomic DNA. Translation: CAI20269.1.
CH471059 Genomic DNA. Translation: EAX07248.1.
BC006353 mRNA. Translation: AAH06353.2.
BC011587 mRNA. Translation: AAH11587.1.
BC092414 mRNA. Translation: AAH92414.1.
CCDSCCDS44118.1. [Q8NA29-1]
CCDS446.1. [Q8NA29-2]
RefSeqNP_001129965.1. NM_001136493.2. [Q8NA29-1]
NP_001274737.1. NM_001287808.1.
NP_001274738.1. NM_001287809.1.
NP_116182.2. NM_032793.4. [Q8NA29-2]
UniGeneHs.655177.

3D structure databases

ProteinModelPortalQ8NA29.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-47306N.
STRING9606.ENSP00000361895.

Protein family/group databases

TCDB2.A.2.3.8. the glycoside-pentoside-hexuronide (gph):cation symporter family.

PTM databases

PhosphoSiteQ8NA29.

Polymorphism databases

DMDM74751132.

Proteomic databases

PaxDbQ8NA29.
PRIDEQ8NA29.

Protocols and materials databases

DNASU84879.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000372809; ENSP00000361895; ENSG00000168389. [Q8NA29-1]
ENST00000372811; ENSP00000361898; ENSG00000168389. [Q8NA29-2]
GeneID84879.
KEGGhsa:84879.
UCSCuc001ceu.3. human. [Q8NA29-2]
uc001cev.3. human. [Q8NA29-1]

Organism-specific databases

CTD84879.
GeneCardsGC01P040421.
HGNCHGNC:25897. MFSD2A.
HPAHPA043107.
MIM614397. gene.
neXtProtNX_Q8NA29.
PharmGKBPA165751549.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG2211.
HOGENOMHOG000294186.
HOVERGENHBG080097.
InParanoidQ8NA29.
OMARGCSQPK.
OrthoDBEOG7QRQTT.
PhylomeDBQ8NA29.
TreeFamTF331194.

Gene expression databases

ArrayExpressQ8NA29.
BgeeQ8NA29.
CleanExHS_MFSD2.
GenevestigatorQ8NA29.

Family and domain databases

InterProIPR016196. MFS_dom_general_subst_transpt.
[Graphical view]
SUPFAMSSF103473. SSF103473. 2 hits.
ProtoNetSearch...

Other

ChiTaRSmfsd2a. human.
GeneWikiMFSD2.
GenomeRNAi84879.
NextBio75189.
PROQ8NA29.
SOURCESearch...

Entry information

Entry nameNLS1_HUMAN
AccessionPrimary (citable) accession number: Q8NA29
Secondary accession number(s): A8K675 expand/collapse secondary AC list , Q6UWU5, Q96F59, Q9BRC8
Entry history
Integrated into UniProtKB/Swiss-Prot: January 23, 2007
Last sequence update: October 1, 2002
Last modified: July 9, 2014
This is version 90 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM