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P14151

- LYAM1_HUMAN

UniProt

P14151 - LYAM1_HUMAN

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Protein
L-selectin
Gene
SELL, LNHR, LYAM1
Organism
Homo sapiens (Human)
Status
Reviewed - 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

  1. carbohydrate binding Source: ProtInc
  2. glycosphingolipid binding Source: BHF-UCL
  3. heparin binding Source: BHF-UCL
  4. protease binding Source: BHF-UCL
  5. protein binding Source: UniProtKB

GO - Biological processi

  1. blood coagulation Source: Reactome
  2. cell adhesion Source: ProtInc
  3. leukocyte migration Source: Reactome
  4. regulation of immune response Source: Reactome
  5. response to ATP Source: Ensembl
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: Chromosome 1

Organism-specific databases

HGNCiHGNC:10720. SELL.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini39 – 332294Extracellular Reviewed prediction
Add
BLAST
Transmembranei333 – 35523Helical; Reviewed prediction
Add
BLAST
Topological domaini356 – 37217Cytoplasmic Reviewed prediction
Add
BLAST

GO - Cellular componenti

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

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Organism-specific databases

Orphaneti34145. Berger disease.
PharmGKBiPA35642.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2828
Add
BLAST
Propeptidei29 – 3810
PRO_0000017475
Chaini39 – 372334L-selectin
PRO_0000017476Add
BLAST

Amino acid modifications

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

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

ArrayExpressiP14151.
BgeeiP14151.
CleanExiHS_SELL.
GenevestigatoriP14151.

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. 14 interactions.
STRINGi9606.ENSP00000236147.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1KJBmodel-A39-158[»]
2LGFNMR-B349-363[»]
3CFWX-ray2.20A39-194[»]
ProteinModelPortaliP14151.
SMRiP14151. Positions 39-319.

Miscellaneous databases

EvolutionaryTraceiP14151.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini55 – 155101C-type lectin
Add
BLAST
Domaini156 – 19237EGF-like
Add
BLAST
Domaini195 – 25662Sushi 1
Add
BLAST
Domaini257 – 31862Sushi 2
Add
BLAST

Sequence similaritiesi

Belongs to the selectin/LECAM family.
Contains 1 EGF-like domain.

Keywords - Domaini

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

Phylogenomic databases

eggNOGiNOG258998.
HOGENOMiHOG000236254.
HOVERGENiHBG052375.
InParanoidiP14151.
KOiK06495.
OMAiVAIQNKG.
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.
[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. Align

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

MIFPWKCQST QRDLWNIFKL WGWTMLCCDF LAHHGTDCWT YHYSEKPMNW    50
QRARRFCRDN YTDLVAIQNK AEIEYLEKTL PFSRSYYWIG IRKIGGIWTW 100
VGTNKSLTEE AENWGDGEPN NKKNKEDCVE IYIKRNKDAG KWNDDACHKL 150
KAALCYTASC QPWSCSGHGE CVEIINNYTC NCDVGYYGPQ CQFVIQCEPL 200
EAPELGTMDC THPLGNFSFS SQCAFSCSEG TNLTGIEETT CGPFGNWSSP 250
EPTCQVIQCE PLSAPDLGIM NCSHPLASFS FTSACTFICS EGTELIGKKK 300
TICESSGIWS NPSPICQKLD KSFSMIKEGD YNPLFIPVAV MVTAFSGLAF 350
IIWLARRLKK GKKSKRSMND PY 372
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.
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.

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.
VSP_042650

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti37 – 371D → Y in CAA34203. 1 Publication
Sequence conflicti178 – 1781Y → H in CAA34203. 1 Publication
Sequence conflicti214 – 2141L → F in CAA34203. 1 Publication
Sequence conflicti218 – 2203SFS → NFN in CAA34275. 1 Publication
Sequence conflicti242 – 2421G → E in CAA34275. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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. [P14151-2]
GeneIDi6402.
KEGGihsa:6402.
UCSCiuc001ggk.3. human. [P14151-2]
uc010pls.2. human. [P14151-1]

Polymorphism databases

DMDMi126178.

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:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS53427.1. [P14151-2 ]
RefSeqi NP_000646.2. NM_000655.4. [P14151-2 ]
UniGenei Hs.728756.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1KJB model - A 39-158 [» ]
2LGF NMR - B 349-363 [» ]
3CFW X-ray 2.20 A 39-194 [» ]
ProteinModelPortali P14151.
SMRi P14151. Positions 39-319.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 112302. 14 interactions.
STRINGi 9606.ENSP00000236147.

Chemistry

BindingDBi P14151.
ChEMBLi CHEMBL3161.

PTM databases

PhosphoSitei P14151.
UniCarbKBi P14151.

Polymorphism databases

DMDMi 126178.

Proteomic databases

MaxQBi P14151.
PaxDbi P14151.
PRIDEi P14151.

Protocols and materials databases

DNASUi 6402.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000236147 ; ENSP00000236147 ; ENSG00000188404 . [P14151-2 ]
GeneIDi 6402.
KEGGi hsa:6402.
UCSCi uc001ggk.3. human. [P14151-2 ]
uc010pls.2. human. [P14151-1 ]

Organism-specific databases

CTDi 6402.
GeneCardsi GC01M169659.
HGNCi HGNC:10720. SELL.
HPAi CAB002144.
MIMi 153240. gene.
neXtProti NX_P14151.
Orphaneti 34145. Berger disease.
PharmGKBi PA35642.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG258998.
HOGENOMi HOG000236254.
HOVERGENi HBG052375.
InParanoidi P14151.
KOi K06495.
OMAi VAIQNKG.
OrthoDBi EOG7DZ8J9.
PhylomeDBi P14151.
TreeFami TF326910.

Enzyme and pathway databases

Reactomei REACT_11152. Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
REACT_12051. Cell surface interactions at the vascular wall.

Miscellaneous databases

EvolutionaryTracei P14151.
GeneWikii L-selectin.
GenomeRNAii 6402.
NextBioi 24874.
PMAP-CutDB P14151.
PROi P14151.
SOURCEi Search...

Gene expression databases

ArrayExpressi P14151.
Bgeei P14151.
CleanExi HS_SELL.
Genevestigatori P14151.

Family and domain databases

Gene3Di 3.10.100.10. 1 hit.
InterProi IPR001304. 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 ]
Pfami PF00008. EGF. 1 hit.
PF00059. Lectin_C. 1 hit.
PF00084. Sushi. 2 hits.
[Graphical view ]
PIRSFi PIRSF002421. L-selectin. 1 hit.
PRINTSi PR00343. SELECTIN.
SMARTi SM00032. CCP. 2 hits.
SM00034. CLECT. 1 hit.
SM00181. EGF. 1 hit.
[Graphical view ]
SUPFAMi SSF56436. SSF56436. 1 hit.
SSF57535. SSF57535. 2 hits.
PROSITEi PS00615. 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 ]
ProtoNeti Search...

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: September 3, 2014
This is version 171 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

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