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Protein

P-selectin glycoprotein ligand 1

Gene

SELPLG

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

Functioni

A SLe(x)-type proteoglycan, which through high affinity, calcium-dependent interactions with E-, P- and L-selectins, mediates rapid rolling of leukocytes over vascular surfaces during the initial steps in inflammation. Critical for the initial leukocyte capture.2 Publications

GO - Molecular functioni

  • receptor binding Source: ProtInc

GO - Biological processi

  • blood coagulation Source: Reactome
  • cell adhesion Source: ProtInc
  • cellular response to interleukin-6 Source: MGI
  • leukocyte adhesive activation Source: UniProtKB
  • leukocyte migration Source: Reactome
  • leukocyte tethering or rolling Source: Ensembl
Complete GO annotation...

Keywords - Biological processi

Cell adhesion

Keywords - Ligandi

Sialic acid

Enzyme and pathway databases

ReactomeiREACT_12051. Cell surface interactions at the vascular wall.

Names & Taxonomyi

Protein namesi
Recommended name:
P-selectin glycoprotein ligand 1
Short name:
PSGL-1
Alternative name(s):
Selectin P ligand
CD_antigen: CD162
Gene namesi
Name:SELPLG
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:10722. SELPLG.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini18 – 320303ExtracellularSequence AnalysisAdd
BLAST
Transmembranei321 – 34121HelicalSequence AnalysisAdd
BLAST
Topological domaini342 – 41271CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  • integral component of membrane Source: ProtInc
  • integral component of plasma membrane Source: ProtInc
  • membrane Source: ProtInc
  • plasma membrane Source: UniProtKB
  • uropod Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi44 – 441T → A: No effect on L-selectin binding nor neutrophil rolling. 1 Publication
Mutagenesisi46 – 527YEYLDYD → FEFLDFE: No sulfation. Almost complete loss of P-selectin binding. No effect on E-selectin binding. 1 Publication
Mutagenesisi46 – 516YEYLDY → FEFLDF: No sulfation. Almost complete loss of P-selectin binding. No effect on E-selectin binding.
Mutagenesisi46 – 461Y → F: Binding L-selectin reduced by 20%, neutrophil recruitment reduced by 30%, and lymphocyte rolling reduced by 32%; when associated with F-48. Binding L-selectin reduced by 86%, neutrophil recruitment reduced by 75%, and lymphocyte rolling reduced by 69%; when associated with F-51. Binding L-selectin reduced by 89%, and neutrophil recruitment reduced by 90%; when associated with F-48 and F-51. Binding of L-selectin reduced by 91%; when associated with F-48; F-51 and A-57. 1 Publication
Mutagenesisi48 – 481Y → F: Binding L-selectin reduced by 20%, neutrophil recruitment reduced by 30%, and lymphocyte rolling reduced by 32%; when associated with F-46. Binding L-lectin reduced by 31%, neutrophil recruitment reduced by 52%, and lymphocyte rolling reduced by 52%; when associated with F-51. Binding L-selectin reduced by 89%, and neutrophil recruitment reduced by 90%; when associated with F-46 and F-51. Binding of L-selectin reduced by 91%; when associated with F-46; F-51 and A-57. 2 Publications
Mutagenesisi51 – 511Y → F: Binding L-selectin reduced by 86%, neutrophil recruitment reduced by 75% and, lymphocyte rolling reduced by 69%; when associated with F-46. Binding L-selectin reduced by 31%, neutrophil recruitment reduced by 52%, and lymphocyte rolling reduced by 52%; when associated with F-48; Binding L-selectin reduced by 89%, and neutrophil recruitment reduced by 90%; when associated with F-46 and F-48. Binding of L-selectin reduced by 91%; when associated with F-46; F-48 and A-57. 2 Publications
Mutagenesisi57 – 571T → A: No E- nor P-selectin binding, and very little neutrophil rolling. Binding of L-selectin reduced by 91%; when associated with F-46; F-48 and F-51. 2 Publications
Mutagenesisi320 – 3201C → A or S: No dimer formation. No effect on P-selectin binding. 1 Publication

Organism-specific databases

PharmGKBiPA35644.

Polymorphism and mutation databases

BioMutaiSELPLG.
DMDMi2498904.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1717Sequence AnalysisAdd
BLAST
Propeptidei18 – 4124PRO_0000022302Add
BLAST
Chaini42 – 412371P-selectin glycoprotein ligand 1PRO_0000022303Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei42 – 421Pyrrolidone carboxylic acid1 Publication
Modified residuei46 – 461Sulfotyrosine1 Publication
Modified residuei48 – 481Sulfotyrosine1 Publication
Modified residuei51 – 511Sulfotyrosine1 Publication
Glycosylationi57 – 571O-linked (GalNAc...)1 Publication
Glycosylationi65 – 651N-linked (GlcNAc...)Sequence Analysis
Glycosylationi111 – 1111N-linked (GlcNAc...)Sequence Analysis
Glycosylationi302 – 3021N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi320 – 320Interchain1 Publication

Post-translational modificationi

Displays complex, core-2, sialylated and fucosylated O-linked oligosaccharides, at least some of which appear to contain poly-N-acetyllactosamine with varying degrees of substitution. Mainly disialylated or neutral forms of the core-2 tetrasaccharide, Galbeta1-->4GlcNAcbeta1-->6(Galbeta1-->3)GalNAcOH. The GlcN:GalN ratio is approximately 2:1 and the Man:Fuc ratio 3:5. Contains about 14% fucose with alpha-1,3 linkage present in two forms: One species is a disialylated, monofucosylated glycan, and the other, a monosialylated, trifucosylated glycan with a polylactosamine backbone. The fucosylated forms carry the Lewis antigen and are important for interaction with selectins and for functioning in leukocyte rolling. The modification containing the sialyl Lewis X glycan is on Thr-57. No sulfated O-glycans. Some N-glycosylation.2 Publications
Sulfation, in conjunction with the SLe(x)-containing glycan, is necessary for P- and L-selectin binding. High affinity P-selectin binding has a preferred requirement for the isomer sulfated on both Tyr-48 and Tyr-51, whereas L-selectin binding requires predominantly sulfation on Tyr-51 with sulfation on Tyr-48 playing only a minor role. These sulfations play an important role in L- and P-selectin-mediated neutrophil recruitment, and leukocyte rolling.1 Publication

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, Pyrrolidone carboxylic acid, Sulfation

Proteomic databases

MaxQBiQ14242.
PaxDbiQ14242.
PRIDEiQ14242.

PTM databases

PhosphoSiteiQ14242.
UniCarbKBiQ14242.

Miscellaneous databases

PMAP-CutDBA8K2Y0.

Expressioni

Tissue specificityi

Expressed on neutrophils, monocytes and most lymphocytes.

Gene expression databases

BgeeiQ14242.
CleanExiHS_SELPLG.
GenevisibleiQ14242. HS.

Organism-specific databases

HPAiCAB002431.

Interactioni

Subunit structurei

Homodimer; disulfide-linked. Interaction with P-, E- and L-selectins, through their lectin/EGF domains, is required for promoting recruitment and rolling of leukocytes. These interactions require sialyl Lewis X glycan modification but there is a differing dependence for tyrosine sulfations. Sulfation on Tyr-51 of PSGL1 is most important for high affinity L-selectin/SELL binding while P-selectin/SELP requires sulfation on Tyr-48. E-selectin/SELE binds with much lower affinity and requires the sLe(x) epitope, but apparantly not tyrosine sulfation. Dimerization appears not to be required for P-selectin/SELP binding. Interacts with SNX20. Interacts with MSN and SYK; mediates the activation of SYK by SELPLG.11 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
SNX20Q7Z6145EBI-1030190,EBI-744896

Protein-protein interaction databases

BioGridi112304. 6 interactions.
DIPiDIP-37668N.
IntActiQ14242. 7 interactions.
STRINGi9606.ENSP00000228463.

Structurei

Secondary structure

1
412
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni51 – 533Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1G1SX-ray1.90C/D42-60[»]
ProteinModelPortaliQ14242.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ14242.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati122 – 131101
Repeati132 – 141102
Repeati142 – 151103
Repeati162 – 171104
Repeati182 – 191105
Repeati192 – 201106
Repeati202 – 211107
Repeati212 – 221108
Repeati222 – 231109
Repeati232 – 2411010
Repeati242 – 2511011
Repeati252 – 2611012

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni122 – 26114012 X 10 AA tandem repeatsAdd
BLAST

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG300903.
GeneTreeiENSGT00440000039754.
HOGENOMiHOG000013048.
HOVERGENiHBG061628.
InParanoidiQ14242.
KOiK06544.
OMAiNYSPTEM.
OrthoDBiEOG7CVPZ8.
PhylomeDBiQ14242.
TreeFamiTF337792.

Family and domain databases

InterProiIPR026195. PSGL-1.
[Graphical view]
PANTHERiPTHR17384. PTHR17384. 1 hit.

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: Q14242-1) [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
MPLQLLLLLI LLGPGNSLQL WDTWADEAEK ALGPLLARDR RQATEYEYLD
60 70 80 90 100
YDFLPETEPP EMLRNSTDTT PLTGPGTPES TTVEPAARRS TGLDAGGAVT
110 120 130 140 150
ELTTELANMG NLSTDSAAME IQTTQPAATE AQTTQPVPTE AQTTPLAATE
160 170 180 190 200
AQTTRLTATE AQTTPLAATE AQTTPPAATE AQTTQPTGLE AQTTAPAAME
210 220 230 240 250
AQTTAPAAME AQTTPPAAME AQTTQTTAME AQTTAPEATE AQTTQPTATE
260 270 280 290 300
AQTTPLAAME ALSTEPSATE ALSMEPTTKR GLFIPFSVSS VTHKGIPMAA
310 320 330 340 350
SNLSVNYPVG APDHISVKQC LLAILILALV ATIFFVCTVV LAVRLSRKGH
360 370 380 390 400
MYPVRNYSPT EMVCISSLLP DGGEGPSATA NGGLSKAKSP GLTPEPREDR
410
EGDDLTLHSF LP
Length:412
Mass (Da):43,201
Last modified:November 1, 1996 - v1
Checksum:iA92A2A902DC9963A
GO
Isoform 2 (identifier: Q14242-2) [UniParc]FASTAAdd to basket

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

Note: No experimental confirmation available.
Show »
Length:428
Mass (Da):44,648
Checksum:iFDB7B0A35F5C4CCC
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti23 – 3917Missing in BAC05283 (PubMed:14702039).CuratedAdd
BLAST
Sequence conflicti50 – 501D → E in BAC05283 (PubMed:14702039).Curated
Sequence conflicti219 – 2191M → T in BAC05283 (PubMed:14702039).Curated
Sequence conflicti222 – 2221Q → R in BAH12863 (PubMed:14702039).Curated
Sequence conflicti396 – 3961P → A in BAC05283 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti62 – 621M → I.2 Publications
Corresponds to variant rs2228315 [ dbSNP | Ensembl ].
VAR_019156
Natural varianti132 – 14110Missing in short form; not an alternative splicing. 3 Publications
Corresponds to variant rs63748999 [ dbSNP | Ensembl ].
VAR_005611
Natural varianti246 – 2461P → S.1 Publication
Corresponds to variant rs8179142 [ dbSNP | Ensembl ].
VAR_019157

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 11M → MAVGASGLEGDKMAGAM in isoform 2. 1 PublicationVSP_044827

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U25956 Genomic DNA. Translation: AAA74577.1.
U02297 mRNA. Translation: AAC50061.1.
AK098315 mRNA. Translation: BAC05283.1.
AK290395 mRNA. Translation: BAF83084.1.
AK298738 mRNA. Translation: BAG60885.1.
AK298742 mRNA. Translation: BAH12863.1.
AY331789 Genomic DNA. Translation: AAP81163.1.
AC007569 Genomic DNA. No translation available.
AC008119 Genomic DNA. No translation available.
BC029782 mRNA. Translation: AAH29782.1.
CCDSiCCDS31895.2. [Q14242-1]
CCDS55881.1. [Q14242-2]
PIRiA57468.
RefSeqiNP_001193538.1. NM_001206609.1. [Q14242-2]
NP_002997.2. NM_003006.4. [Q14242-1]
XP_005269133.1. XM_005269076.2.
UniGeneiHs.591014.

Genome annotation databases

EnsembliENST00000228463; ENSP00000228463; ENSG00000110876. [Q14242-2]
ENST00000550948; ENSP00000447752; ENSG00000110876.
GeneIDi6404.
KEGGihsa:6404.
UCSCiuc001tni.3. human. [Q14242-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Wikipedia

P-selectin glycoprotein ligand 1 entry

SeattleSNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U25956 Genomic DNA. Translation: AAA74577.1.
U02297 mRNA. Translation: AAC50061.1.
AK098315 mRNA. Translation: BAC05283.1.
AK290395 mRNA. Translation: BAF83084.1.
AK298738 mRNA. Translation: BAG60885.1.
AK298742 mRNA. Translation: BAH12863.1.
AY331789 Genomic DNA. Translation: AAP81163.1.
AC007569 Genomic DNA. No translation available.
AC008119 Genomic DNA. No translation available.
BC029782 mRNA. Translation: AAH29782.1.
CCDSiCCDS31895.2. [Q14242-1]
CCDS55881.1. [Q14242-2]
PIRiA57468.
RefSeqiNP_001193538.1. NM_001206609.1. [Q14242-2]
NP_002997.2. NM_003006.4. [Q14242-1]
XP_005269133.1. XM_005269076.2.
UniGeneiHs.591014.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1G1SX-ray1.90C/D42-60[»]
ProteinModelPortaliQ14242.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112304. 6 interactions.
DIPiDIP-37668N.
IntActiQ14242. 7 interactions.
STRINGi9606.ENSP00000228463.

Chemistry

BindingDBiQ14242.
ChEMBLiCHEMBL3301394.

PTM databases

PhosphoSiteiQ14242.
UniCarbKBiQ14242.

Polymorphism and mutation databases

BioMutaiSELPLG.
DMDMi2498904.

Proteomic databases

MaxQBiQ14242.
PaxDbiQ14242.
PRIDEiQ14242.

Protocols and materials databases

DNASUi6404.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000228463; ENSP00000228463; ENSG00000110876. [Q14242-2]
ENST00000550948; ENSP00000447752; ENSG00000110876.
GeneIDi6404.
KEGGihsa:6404.
UCSCiuc001tni.3. human. [Q14242-1]

Organism-specific databases

CTDi6404.
GeneCardsiGC12M109015.
H-InvDBHIX0010969.
HGNCiHGNC:10722. SELPLG.
HPAiCAB002431.
MIMi600738. gene.
neXtProtiNX_Q14242.
PharmGKBiPA35644.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG300903.
GeneTreeiENSGT00440000039754.
HOGENOMiHOG000013048.
HOVERGENiHBG061628.
InParanoidiQ14242.
KOiK06544.
OMAiNYSPTEM.
OrthoDBiEOG7CVPZ8.
PhylomeDBiQ14242.
TreeFamiTF337792.

Enzyme and pathway databases

ReactomeiREACT_12051. Cell surface interactions at the vascular wall.

Miscellaneous databases

ChiTaRSiSELPLG. human.
EvolutionaryTraceiQ14242.
GeneWikiiP-selectin_glycoprotein_ligand-1.
GenomeRNAii6404.
NextBioi24882.
PMAP-CutDBA8K2Y0.
PROiQ14242.
SOURCEiSearch...

Gene expression databases

BgeeiQ14242.
CleanExiHS_SELPLG.
GenevisibleiQ14242. HS.

Family and domain databases

InterProiIPR026195. PSGL-1.
[Graphical view]
PANTHERiPTHR17384. PTHR17384. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Genomic organization and chromosomal localization of the gene encoding human P-selectin glycoprotein ligand."
    Veldman G.M., Bean K.M., Cumming D.A., Eddy R.L., Sait S.N.J., Shows T.B.
    J. Biol. Chem. 270:16470-16475(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Tissue: Placenta.
  2. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT 132-GLN--ALA-141 DEL.
  3. "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 2), VARIANTS ILE-62 AND 132-GLN--ALA-141 DEL.
    Tissue: Uterus.
  4. SeattleSNPs variation discovery resource
    Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ILE-62 AND SER-246.
  5. "The finished DNA sequence of human chromosome 12."
    Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
    , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
    Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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 1), VARIANT 132-GLN--ALA-141 DEL.
    Tissue: Brain.
  7. "The P-selectin glycoprotein ligand from human neutrophils displays sialylated, fucosylated, O-linked poly-N-acetyllactosamine."
    Moore K.L., Eaton S.F., Lyons D.E., Lichenstein H.S., Cummings R.D., McEver R.P.
    J. Biol. Chem. 269:23318-23327(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 350-355 AND 390-396, INTERACTION WITH SELP AND SELE, STRUCTURE OF CARBOHYDRATE, SUBUNIT, SIALIC ACID CONTENT.
    Tissue: Neutrophil.
  8. "A sulfated peptide segment at the amino terminus of PSGL-1 is critical for P-selectin binding."
    Sako D., Comess K.M., Barone K.M., Camphausen R.T., Cumming D.A., Shaw G.D.
    Cell 83:323-331(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: SULFATION, INTERACTION WITH SELP, MUTAGENESIS OF 46-TYR--ASP-52.
  9. "PSGL-1 recognition of P-selectin is controlled by a tyrosine sulfation consensus at the PSGL-1 amino terminus."
    Pouyani T., Seed B.
    Cell 83:333-343(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: SULFATION, INTERACTION WITH SELP, MUTAGENESIS OF TYR-46; TYR-48; TYR-51 AND THR-57.
  10. "Tyrosine sulfation of P-selectin glycoprotein ligand-1 is required for high affinity binding to P-selectin."
    Wilkins P.P., Moore K.L., McEver R.P., Cummings R.D.
    J. Biol. Chem. 270:22677-22680(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: SULFATION, INTERACTION WITH SELP.
  11. "Structures of the O-glycans on P-selectin glycoprotein ligand-1 from HL-60 cells."
    Wilkins P.P., McEver R.P., Cummings R.D.
    J. Biol. Chem. 271:18732-18742(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE OF O-LINKED CARBOHYDRATES.
  12. "Noncovalent association of P-selectin glycoprotein ligand-1 and minimal determinants for binding to P-selectin."
    Epperson T.K., Patel K.D., McEver R.P., Cummings R.D.
    J. Biol. Chem. 275:7839-7853(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SELP, DISULFIDE BOND AT CYS-320, MUTAGENESIS OF CYS-320.
  13. "Tyrosine sulfation enhances but is not required for PSGL-1 rolling adhesion on P-selectin."
    Rodgers S.D., Camphausen R.T., Hammer D.A.
    Biophys. J. 81:2001-2009(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SELE AND SELP, SULFATION, FUNCTION.
  14. "ITAM-based interaction of ERM proteins with Syk mediates signaling by the leukocyte adhesion receptor PSGL-1."
    Urzainqui A., Serrador J.M., Viedma F., Yanez-Mo M., Rodriguez A., Corbi A.L., Alonso-Lebrero J.L., Luque A., Deckert M., Vazquez J., Sanchez-Madrid F.
    Immunity 17:401-412(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MSN AND SYK.
  15. "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 SELL, FUNCTION, MUTAGENESIS OF THR-44; TYR-48; TYR-51 AND THR-57.
  16. "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 SELL, SULFATION, GLYCOSYLATION.
  17. "SLIC-1/sorting nexin 20: a novel sorting nexin that directs subcellular distribution of PSGL-1."
    Schaff U.Y., Shih H.H., Lorenz M., Sako D., Kriz R., Milarski K., Bates B., Tchernychev B., Shaw G.D., Simon S.I.
    Eur. J. Immunol. 38:550-564(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SNX20.
  18. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  19. "Insights into the molecular basis of leukocyte tethering and rolling revealed by structures of P- and E-selectin bound to SLe(X) and PSGL-1."
    Somers W.S., Tang J., Shaw G.D., Camphausen R.T.
    Cell 103:467-479(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 42-68 IN COMPLEX WITH SELE AND SELP LECTIN/EGF DOMAINS, SULFATION AT TYR-46; TYR-48 AND TYR-51, GLYCOSYLATION AT THR-57, PYROGLUTAMATE FORMATION AT GLN-42.
  20. Erratum
    Somers W.S., Tang J., Shaw G.D., Camphausen R.T.
    Cell 105:971-971(2001)

Entry informationi

Entry nameiSELPL_HUMAN
AccessioniPrimary (citable) accession number: Q14242
Secondary accession number(s): A8K2Y0
, B4DQC3, B7Z5C7, J3KMX6, Q12775, Q6GTW7, Q8N7J7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: July 22, 2015
This is version 143 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

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human cell differentiation molecules
    CD nomenclature of surface proteins of human leucocytes and list of entries
  2. Human chromosome 12
    Human chromosome 12: 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

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.