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P14151 (LYAM1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 170. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
L-selectin
Alternative name(s):
CD62 antigen-like family member L
Leukocyte adhesion molecule 1
Short name=LAM-1
Leukocyte surface antigen Leu-8
Leukocyte-endothelial cell adhesion molecule 1
Short name=LECAM1
Lymph node homing receptor
TQ1
gp90-MEL
CD_antigen=CD62L
Gene names
Name:SELL
Synonyms:LNHR, LYAM1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length372 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Cell surface adhesion protein. Mediates the adherence of lymphocytes to endothelial cells of high endothelial venules in peripheral lymph nodes. Promotes initial tethering and rolling of leukocytes in endothelia. Ref.12

Subunit structure

Interaction with PSGL1/SELPLG and PODXL2 is required for promoting recruitment and rolling of leukocytes. This interaction is dependent on the sialyl Lewis X glycan modification of PSGL1 and PODXL2, and tyrosine sulfation modifications of PSGL1. Sulfation on 'Tyr-51' of PSGL1 is important for L-selectin binding.

Subcellular location

Membrane; Single-pass type I membrane protein.

Tissue specificity

Expressed in B-cell lines and T-lymphocytes. Ref.2

Sequence similarities

Belongs to the selectin/LECAM family.

Contains 1 C-type lectin domain.

Contains 1 EGF-like domain.

Contains 2 Sushi (CCP/SCR) domains.

Sequence caution

The sequence CAA34203.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence CAB43536.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence CAB43537.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P14151-1)

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: P14151-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MGCRRTREGPSKAM
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2828
Propeptide29 – 3810
PRO_0000017475
Chain39 – 372334L-selectin
PRO_0000017476

Regions

Topological domain39 – 332294Extracellular Potential
Transmembrane333 – 35523Helical; Potential
Topological domain356 – 37217Cytoplasmic Potential
Domain55 – 155101C-type lectin
Domain156 – 19237EGF-like
Domain195 – 25662Sushi 1
Domain257 – 31862Sushi 2

Amino acid modifications

Glycosylation601N-linked (GlcNAc...) Ref.11 Ref.15
Glycosylation1041N-linked (GlcNAc...) Ref.15
Glycosylation1771N-linked (GlcNAc...) Potential
Glycosylation2321N-linked (GlcNAc...) Potential
Glycosylation2461N-linked (GlcNAc...) Potential
Glycosylation2711N-linked (GlcNAc...) Potential
Glycosylation3111N-linked (GlcNAc...) Potential
Disulfide bond57 ↔ 155 By similarity
Disulfide bond128 ↔ 147 By similarity
Disulfide bond160 ↔ 171 By similarity
Disulfide bond165 ↔ 180 By similarity
Disulfide bond182 ↔ 191 By similarity
Disulfide bond197 ↔ 241 By similarity
Disulfide bond227 ↔ 254 By similarity
Disulfide bond259 ↔ 303 By similarity
Disulfide bond289 ↔ 316 By similarity

Natural variations

Alternative sequence11M → MGCRRTREGPSKAM in isoform 2.
VSP_042650
Natural variant1931F → L. Ref.1 Ref.4 Ref.8
Corresponds to variant rs1131498 [ dbSNP | Ensembl ].
VAR_019134
Natural variant2011E → Q. Ref.8
Corresponds to variant rs2229568 [ dbSNP | Ensembl ].
VAR_019135
Natural variant2131P → S. Ref.3 Ref.8
Corresponds to variant rs2229569 [ dbSNP | Ensembl ].
VAR_019136
Natural variant3691N → D. Ref.8
Corresponds to variant rs4987382 [ dbSNP | Ensembl ].
VAR_019137

Experimental info

Sequence conflict371D → Y in CAA34203. Ref.4
Sequence conflict1781Y → H in CAA34203. Ref.4
Sequence conflict2141L → F in CAA34203. Ref.4
Sequence conflict218 – 2203SFS → NFN in CAA34275. Ref.2
Sequence conflict2421G → E in CAA34275. Ref.2

Secondary structure

................................. 372
Helix Strand Turn

Details...

Sequences

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

Last modified February 1, 1991. Version 2.
Checksum: 6EA9918ECA2D3643

FASTA37242,187
        10         20         30         40         50         60 
MIFPWKCQST QRDLWNIFKL WGWTMLCCDF LAHHGTDCWT YHYSEKPMNW QRARRFCRDN 

        70         80         90        100        110        120 
YTDLVAIQNK AEIEYLEKTL PFSRSYYWIG IRKIGGIWTW VGTNKSLTEE AENWGDGEPN 

       130        140        150        160        170        180 
NKKNKEDCVE IYIKRNKDAG KWNDDACHKL KAALCYTASC QPWSCSGHGE CVEIINNYTC 

       190        200        210        220        230        240 
NCDVGYYGPQ CQFVIQCEPL EAPELGTMDC THPLGNFSFS SQCAFSCSEG TNLTGIEETT 

       250        260        270        280        290        300 
CGPFGNWSSP EPTCQVIQCE PLSAPDLGIM NCSHPLASFS FTSACTFICS EGTELIGKKK 

       310        320        330        340        350        360 
TICESSGIWS NPSPICQKLD KSFSMIKEGD YNPLFIPVAV MVTAFSGLAF IIWLARRLKK 

       370 
GKKSKRSMND PY 

« Hide

Isoform 2 [UniParc].

Checksum: 1205F691BA638EF1
Show »

FASTA38543,618

References

« Hide 'large scale' references
[1]"Human homologue of mouse lymph node homing receptor: evolutionary conservation at tandem cell interaction domains."
Siegelman M.H., Weissman I.L.
Proc. Natl. Acad. Sci. U.S.A. 86:5562-5566(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT LEU-193.
Tissue: Lymphocyte.
[2]"Isolation and chromosomal localization of cDNAs encoding a novel human lymphocyte cell surface molecule, LAM-1. Homology with the mouse lymphocyte homing receptor and other human adhesion proteins."
Tedder T.F., Isaacs C.M., Ernst T.J., Demetri G.D., Adler D.A., Disteche C.M.
J. Exp. Med. 170:123-133(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
Tissue: Tonsil.
[3]"Leu-8/TQ1 is the human equivalent of the Mel-14 lymph node homing receptor."
Camerini D., James S.P., Stamenkovic I., Seed B.
Nature 342:78-82(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT SER-213.
Tissue: Lymphocyte.
[4]"Characterization of a human homologue of the murine peripheral lymph node homing receptor."
Bowen B.R., Nguyen T., Lasky L.A.
J. Cell Biol. 109:421-427(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT LEU-193.
Tissue: Lymphocyte.
[5]"Structure of the gene encoding the human leukocyte adhesion molecule-1 (TQ1, Leu-8) of lymphocytes and neutrophils."
Ord D.C., Ernst T.J., Zhou L.J., Rambaldi A., Spertini O., Griffin J., Tedder T.F.
J. Biol. Chem. 265:7760-7767(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[6]Fieger C.B.
Thesis (1998), Freie Universtiaet Berlin, Germany
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Tissue: Hematopoietic.
[7]"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] (ISOFORM 1).
[8]SeattleSNPs variation discovery resource
Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS LEU-193; GLN-201; SER-213 AND ASP-369.
[9]"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].
[10]Mural R.J., Istrail S., Sutton 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[11]"Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-60.
Tissue: Plasma.
[12]"Molecular basis of leukocyte rolling on PSGL-1. Predominant role of core-2 O-glycans and of tyrosine sulfate residue 51."
Bernimoulin M.P., Zeng X.-L., Abbal C., Giraud S., Martinez M., Michielin O., Schapira M., Spertini O.
J. Biol. Chem. 278:37-47(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SELPLG, FUNCTION.
[13]"Model glycosulfopeptides from P-selectin glycoprotein ligand-1 require tyrosine sulfation and a core 2-branched O-glycan to bind to L-selectin."
Leppaenen A., Yago T., Otto V.I., McEver R.P., Cummings R.D.
J. Biol. Chem. 278:26391-26400(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SELPLG.
[14]"Endoglycan, a member of the CD34 family of sialomucins, is a ligand for the vascular selectins."
Kerr S.C., Fieger C.B., Snapp K.R., Rosen S.D.
J. Immunol. 181:1480-1490(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PODXL2.
[15]"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-60 AND ASN-104.
Tissue: Leukemic T-cell.
[16]"A template for generation and comparison of three-dimensional selectin models."
Bajorath J., Aruffo A.
Biochem. Biophys. Res. Commun. 216:1018-1023(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: 3D-STRUCTURE MODELING.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M25280 mRNA. Translation: AAC63053.1.
X16150 mRNA. Translation: CAA34275.1.
X17519 mRNA. Translation: CAB43536.1. Different initiation.
X17519 mRNA. Translation: CAB43537.1. Different initiation.
X16070 mRNA. Translation: CAA34203.1. Different initiation.
M32414 expand/collapse EMBL AC list , M32406, M32407, M32408, M32409, M32410, M32411, M32412, M32413 Genomic DNA. Translation: AAB60700.1.
AJ246000 mRNA. Translation: CAB55488.1.
AK312673 mRNA. Translation: BAG35555.1.
AY233976 Genomic DNA. Translation: AAO48272.1.
AL021940 Genomic DNA. Translation: CAI19356.1.
CH471067 Genomic DNA. Translation: EAW90856.1.
CCDSCCDS53427.1. [P14151-2]
RefSeqNP_000646.2. NM_000655.4. [P14151-2]
UniGeneHs.728756.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1KJBmodel-A39-158[»]
2LGFNMR-B349-363[»]
3CFWX-ray2.20A39-194[»]
ProteinModelPortalP14151.
SMRP14151. Positions 39-319.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112302. 14 interactions.
STRING9606.ENSP00000236147.

Chemistry

BindingDBP14151.
ChEMBLCHEMBL3161.

PTM databases

PhosphoSiteP14151.
UniCarbKBP14151.

Polymorphism databases

DMDM126178.

Proteomic databases

MaxQBP14151.
PaxDbP14151.
PRIDEP14151.

Protocols and materials databases

DNASU6402.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000236147; ENSP00000236147; ENSG00000188404. [P14151-2]
GeneID6402.
KEGGhsa:6402.
UCSCuc001ggk.3. human. [P14151-2]
uc010pls.2. human. [P14151-1]

Organism-specific databases

CTD6402.
GeneCardsGC01M169659.
HGNCHGNC:10720. SELL.
HPACAB002144.
MIM153240. gene.
neXtProtNX_P14151.
Orphanet34145. Berger disease.
PharmGKBPA35642.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG258998.
HOGENOMHOG000236254.
HOVERGENHBG052375.
InParanoidP14151.
KOK06495.
OMAVAIQNKG.
OrthoDBEOG7DZ8J9.
PhylomeDBP14151.
TreeFamTF326910.

Enzyme and pathway databases

ReactomeREACT_604. Hemostasis.
REACT_6900. Immune System.

Gene expression databases

ArrayExpressP14151.
BgeeP14151.
CleanExHS_SELL.
GenevestigatorP14151.

Family and domain databases

Gene3D3.10.100.10. 1 hit.
InterProIPR001304. C-type_lectin.
IPR016186. C-type_lectin-like.
IPR018378. C-type_lectin_CS.
IPR016187. C-type_lectin_fold.
IPR000742. EG-like_dom.
IPR013032. EGF-like_CS.
IPR016348. L-selectin.
IPR002396. Selectin_superfamily.
IPR000436. Sushi_SCR_CCP.
[Graphical view]
PfamPF00008. EGF. 1 hit.
PF00059. Lectin_C. 1 hit.
PF00084. Sushi. 2 hits.
[Graphical view]
PIRSFPIRSF002421. L-selectin. 1 hit.
PRINTSPR00343. SELECTIN.
SMARTSM00032. CCP. 2 hits.
SM00034. CLECT. 1 hit.
SM00181. EGF. 1 hit.
[Graphical view]
SUPFAMSSF56436. SSF56436. 1 hit.
SSF57535. SSF57535. 2 hits.
PROSITEPS00615. C_TYPE_LECTIN_1. 1 hit.
PS50041. C_TYPE_LECTIN_2. 1 hit.
PS00022. EGF_1. 1 hit.
PS01186. EGF_2. 1 hit.
PS50026. EGF_3. 1 hit.
PS50923. SUSHI. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP14151.
GeneWikiL-selectin.
GenomeRNAi6402.
NextBio24874.
PMAP-CutDBP14151.
PROP14151.
SOURCESearch...

Entry information

Entry nameLYAM1_HUMAN
AccessionPrimary (citable) accession number: P14151
Secondary accession number(s): B2R6Q8, P15023, Q9UJ43
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: February 1, 1991
Last modified: July 9, 2014
This is version 170 of the entry and version 2 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

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

Human cell differentiation molecules

CD nomenclature of surface proteins of human leucocytes and list of entries