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Protein

L-selectin

Gene

SELL

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

Functioni

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.1 Publication

GO - Molecular functioni

  • carbohydrate binding Source: ProtInc
  • glycosphingolipid binding Source: BHF-UCL
  • heparin binding Source: BHF-UCL
  • protease binding Source: BHF-UCL

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Cell adhesion

Keywords - Ligandi

Lectin

Enzyme and pathway databases

ReactomeiREACT_11152. Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
REACT_12051. Cell surface interactions at the vascular wall.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:SELL
Synonyms:LNHR, LYAM1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:10720. SELL.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini39 – 332294ExtracellularSequence AnalysisAdd
BLAST
Transmembranei333 – 35523HelicalSequence AnalysisAdd
BLAST
Topological domaini356 – 37217CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  • external side of plasma membrane Source: Ensembl
  • integral component of plasma membrane Source: ProtInc
  • plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Organism-specific databases

Orphaneti34145. Berger disease.
PharmGKBiPA35642.

Polymorphism and mutation databases

BioMutaiSELL.
DMDMi126178.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2828Add
BLAST
Propeptidei29 – 3810PRO_0000017475
Chaini39 – 372334L-selectinPRO_0000017476Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi57 ↔ 155By similarity
Glycosylationi60 – 601N-linked (GlcNAc...)2 Publications
Glycosylationi104 – 1041N-linked (GlcNAc...)1 Publication
Disulfide bondi128 ↔ 147By similarity
Disulfide bondi160 ↔ 171By similarity
Disulfide bondi165 ↔ 180By similarity
Glycosylationi177 – 1771N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi182 ↔ 191By similarity
Disulfide bondi197 ↔ 241By similarity
Disulfide bondi227 ↔ 254By similarity
Glycosylationi232 – 2321N-linked (GlcNAc...)Sequence Analysis
Glycosylationi246 – 2461N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi259 ↔ 303By similarity
Glycosylationi271 – 2711N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi289 ↔ 316By similarity
Glycosylationi311 – 3111N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiP14151.
PaxDbiP14151.
PRIDEiP14151.

PTM databases

PhosphoSiteiP14151.
UniCarbKBiP14151.

Miscellaneous databases

PMAP-CutDBP14151.

Expressioni

Tissue specificityi

Expressed in B-cell lines and T-lymphocytes.1 Publication

Gene expression databases

BgeeiP14151.
CleanExiHS_SELL.
ExpressionAtlasiP14151. baseline and differential.
GenevisibleiP14151. HS.

Organism-specific databases

HPAiCAB002144.

Interactioni

Subunit structurei

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.

Protein-protein interaction databases

BioGridi112302. 13 interactions.
STRINGi9606.ENSP00000236147.

Structurei

Secondary structure

1
372
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi40 – 489Combined sources
Helixi50 – 6011Combined sources
Beta strandi61 – 644Combined sources
Helixi70 – 7910Combined sources
Beta strandi87 – 948Combined sources
Beta strandi97 – 1004Combined sources
Turni101 – 1033Combined sources
Turni109 – 1113Combined sources
Helixi122 – 1243Combined sources
Beta strandi128 – 1314Combined sources
Beta strandi136 – 1383Combined sources
Beta strandi142 – 1454Combined sources
Beta strandi151 – 1577Combined sources
Beta strandi167 – 1748Combined sources
Beta strandi177 – 1826Combined sources
Beta strandi187 – 1915Combined sources
Helixi350 – 36213Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1KJBmodel-A39-158[»]
2LGFNMR-B349-363[»]
3CFWX-ray2.20A39-194[»]
ProteinModelPortaliP14151.
SMRiP14151. Positions 39-317.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP14151.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini55 – 155101C-type lectinPROSITE-ProRule annotationAdd
BLAST
Domaini156 – 19237EGF-likePROSITE-ProRule annotationAdd
BLAST
Domaini195 – 25662Sushi 1PROSITE-ProRule annotationAdd
BLAST
Domaini257 – 31862Sushi 2PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the selectin/LECAM family.Curated
Contains 1 C-type lectin domain.PROSITE-ProRule annotation
Contains 1 EGF-like domain.PROSITE-ProRule annotation
Contains 2 Sushi (CCP/SCR) domains.PROSITE-ProRule annotation

Keywords - Domaini

EGF-like domain, Repeat, Signal, Sushi, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG258998.
HOGENOMiHOG000236254.
HOVERGENiHBG052375.
InParanoidiP14151.
KOiK06495.
OMAiEAENWGD.
OrthoDBiEOG7DZ8J9.
PhylomeDBiP14151.
TreeFamiTF326910.

Family and domain databases

Gene3Di3.10.100.10. 1 hit.
InterProiIPR001304. 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_dom.
[Graphical view]
PfamiPF00008. EGF. 1 hit.
PF00059. Lectin_C. 1 hit.
PF00084. Sushi. 2 hits.
[Graphical view]
PIRSFiPIRSF002421. L-selectin. 1 hit.
PRINTSiPR00343. SELECTIN.
SMARTiSM00032. CCP. 2 hits.
SM00034. CLECT. 1 hit.
SM00181. EGF. 1 hit.
[Graphical view]
SUPFAMiSSF56436. SSF56436. 1 hit.
SSF57535. SSF57535. 2 hits.
PROSITEiPS00615. 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]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P14151-1) [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
MIFPWKCQST QRDLWNIFKL WGWTMLCCDF LAHHGTDCWT YHYSEKPMNW
60 70 80 90 100
QRARRFCRDN YTDLVAIQNK AEIEYLEKTL PFSRSYYWIG IRKIGGIWTW
110 120 130 140 150
VGTNKSLTEE AENWGDGEPN NKKNKEDCVE IYIKRNKDAG KWNDDACHKL
160 170 180 190 200
KAALCYTASC QPWSCSGHGE CVEIINNYTC NCDVGYYGPQ CQFVIQCEPL
210 220 230 240 250
EAPELGTMDC THPLGNFSFS SQCAFSCSEG TNLTGIEETT CGPFGNWSSP
260 270 280 290 300
EPTCQVIQCE PLSAPDLGIM NCSHPLASFS FTSACTFICS EGTELIGKKK
310 320 330 340 350
TICESSGIWS NPSPICQKLD KSFSMIKEGD YNPLFIPVAV MVTAFSGLAF
360 370
IIWLARRLKK GKKSKRSMND PY
Length:372
Mass (Da):42,187
Last modified:February 1, 1991 - v2
Checksum:i6EA9918ECA2D3643
GO
Isoform 2 (identifier: P14151-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MGCRRTREGPSKAM

Note: No experimental confirmation available.
Show »
Length:385
Mass (Da):43,618
Checksum:i1205F691BA638EF1
GO

Sequence cautioni

The sequence CAA34203.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence CAB43536.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence CAB43537.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti37 – 371D → Y in CAA34203 (PubMed:2663882).Curated
Sequence conflicti178 – 1781Y → H in CAA34203 (PubMed:2663882).Curated
Sequence conflicti214 – 2141L → F in CAA34203 (PubMed:2663882).Curated
Sequence conflicti218 – 2203SFS → NFN in CAA34275 (PubMed:2473156).Curated
Sequence conflicti242 – 2421G → E in CAA34275 (PubMed:2473156).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti193 – 1931F → L.3 Publications
Corresponds to variant rs1131498 [ dbSNP | Ensembl ].
VAR_019134
Natural varianti201 – 2011E → Q.1 Publication
Corresponds to variant rs2229568 [ dbSNP | Ensembl ].
VAR_019135
Natural varianti213 – 2131P → S.2 Publications
Corresponds to variant rs2229569 [ dbSNP | Ensembl ].
VAR_019136
Natural varianti369 – 3691N → D.1 Publication
Corresponds to variant rs4987382 [ dbSNP | Ensembl ].
VAR_019137

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 11M → MGCRRTREGPSKAM in isoform 2. 1 PublicationVSP_042650

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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
, 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.
CCDSiCCDS53427.1. [P14151-2]
RefSeqiNP_000646.2. NM_000655.4. [P14151-2]
UniGeneiHs.728756.

Genome annotation databases

EnsembliENST00000236147; ENSP00000236147; ENSG00000188404.
GeneIDi6402.
KEGGihsa:6402.
UCSCiuc001ggk.3. human. [P14151-2]
uc010pls.2. human. [P14151-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

SeattleSNPs
Functional Glycomics Gateway - Glycan Binding

L-selectin

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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
, 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.
CCDSiCCDS53427.1. [P14151-2]
RefSeqiNP_000646.2. NM_000655.4. [P14151-2]
UniGeneiHs.728756.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1KJBmodel-A39-158[»]
2LGFNMR-B349-363[»]
3CFWX-ray2.20A39-194[»]
ProteinModelPortaliP14151.
SMRiP14151. Positions 39-317.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112302. 13 interactions.
STRINGi9606.ENSP00000236147.

Chemistry

BindingDBiP14151.
ChEMBLiCHEMBL3161.

PTM databases

PhosphoSiteiP14151.
UniCarbKBiP14151.

Polymorphism and mutation databases

BioMutaiSELL.
DMDMi126178.

Proteomic databases

MaxQBiP14151.
PaxDbiP14151.
PRIDEiP14151.

Protocols and materials databases

DNASUi6402.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000236147; ENSP00000236147; ENSG00000188404.
GeneIDi6402.
KEGGihsa:6402.
UCSCiuc001ggk.3. human. [P14151-2]
uc010pls.2. human. [P14151-1]

Organism-specific databases

CTDi6402.
GeneCardsiGC01M169659.
HGNCiHGNC:10720. SELL.
HPAiCAB002144.
MIMi153240. gene.
neXtProtiNX_P14151.
Orphaneti34145. Berger disease.
PharmGKBiPA35642.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG258998.
HOGENOMiHOG000236254.
HOVERGENiHBG052375.
InParanoidiP14151.
KOiK06495.
OMAiEAENWGD.
OrthoDBiEOG7DZ8J9.
PhylomeDBiP14151.
TreeFamiTF326910.

Enzyme and pathway databases

ReactomeiREACT_11152. Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
REACT_12051. Cell surface interactions at the vascular wall.

Miscellaneous databases

EvolutionaryTraceiP14151.
GeneWikiiL-selectin.
GenomeRNAii6402.
NextBioi24874.
PMAP-CutDBP14151.
PROiP14151.
SOURCEiSearch...

Gene expression databases

BgeeiP14151.
CleanExiHS_SELL.
ExpressionAtlasiP14151. baseline and differential.
GenevisibleiP14151. HS.

Family and domain databases

Gene3Di3.10.100.10. 1 hit.
InterProiIPR001304. 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_dom.
[Graphical view]
PfamiPF00008. EGF. 1 hit.
PF00059. Lectin_C. 1 hit.
PF00084. Sushi. 2 hits.
[Graphical view]
PIRSFiPIRSF002421. L-selectin. 1 hit.
PRINTSiPR00343. SELECTIN.
SMARTiSM00032. CCP. 2 hits.
SM00034. CLECT. 1 hit.
SM00181. EGF. 1 hit.
[Graphical view]
SUPFAMiSSF56436. SSF56436. 1 hit.
SSF57535. SSF57535. 2 hits.
PROSITEiPS00615. 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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.
    , 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. 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.

Entry informationi

Entry nameiLYAM1_HUMAN
AccessioniPrimary (citable) accession number: P14151
Secondary accession number(s): B2R6Q8, P15023, Q9UJ43
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: February 1, 1991
Last modified: July 22, 2015
This is version 180 of the entry and version 2 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human cell differentiation molecules
    CD nomenclature of surface proteins of human leucocytes and list of entries
  2. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  3. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. 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.