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Q14242 (SELPL_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 131. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
P-selectin glycoprotein ligand 1

Short name=PSGL-1
Alternative name(s):
Selectin P ligand
CD_antigen=CD162
Gene names
Name:SELPLG
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length412 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.13 Ref.15

Subunit structure

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. Ref.7 Ref.8 Ref.9 Ref.10 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17

Subcellular location

Membrane; Single-pass type I membrane protein.

Tissue specificity

Expressed on neutrophils, monocytes and most lymphocytes.

Post-translational modification

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.

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.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

SNX20Q7Z6145EBI-1030190,EBI-744896

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q14242-1)

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: Q14242-2)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1717 Potential
Propeptide18 – 4124
PRO_0000022302
Chain42 – 412371P-selectin glycoprotein ligand 1
PRO_0000022303

Regions

Topological domain18 – 320303Extracellular Potential
Transmembrane321 – 34121Helical; Potential
Topological domain342 – 41271Cytoplasmic Potential
Repeat122 – 131101
Repeat132 – 141102
Repeat142 – 151103
Repeat162 – 171104
Repeat182 – 191105
Repeat192 – 201106
Repeat202 – 211107
Repeat212 – 221108
Repeat222 – 231109
Repeat232 – 2411010
Repeat242 – 2511011
Repeat252 – 2611012
Region122 – 26114012 X 10 AA tandem repeats

Amino acid modifications

Modified residue421Pyrrolidone carboxylic acid
Modified residue461Sulfotyrosine Ref.19
Modified residue481Sulfotyrosine Ref.19
Modified residue511Sulfotyrosine Ref.19
Glycosylation571O-linked (GalNAc...) Ref.19
Glycosylation651N-linked (GlcNAc...) Potential
Glycosylation1111N-linked (GlcNAc...) Potential
Glycosylation3021N-linked (GlcNAc...) Potential
Disulfide bond320Interchain Ref.12

Natural variations

Alternative sequence11M → MAVGASGLEGDKMAGAM in isoform 2.
VSP_044827
Natural variant621M → I. Ref.3 Ref.4
Corresponds to variant rs2228315 [ dbSNP | Ensembl ].
VAR_019156
Natural variant132 – 14110Missing in short form; not an alternative splicing.
Corresponds to variant rs63748999 [ dbSNP | Ensembl ].
VAR_005611
Natural variant2461P → S. Ref.4
Corresponds to variant rs8179142 [ dbSNP | Ensembl ].
VAR_019157

Experimental info

Mutagenesis441T → A: No effect on L-selectin binding nor neutrophil rolling. Ref.15
Mutagenesis46 – 527YEYLDYD → FEFLDFE: No sulfation. Almost complete loss of P-selectin binding. No effect on E-selectin binding. Ref.8 Ref.9
Mutagenesis46 – 516YEYLDY → FEFLDF: No sulfation. Almost complete loss of P-selectin binding. No effect on E-selectin binding. Ref.9 Ref.15
Mutagenesis461Y → 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. Ref.9
Mutagenesis481Y → 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. Ref.9 Ref.15
Mutagenesis511Y → 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. Ref.9 Ref.15
Mutagenesis571T → 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. Ref.9 Ref.15
Mutagenesis3201C → A or S: No dimer formation. No effect on P-selectin binding. Ref.12
Sequence conflict23 – 3917Missing in BAC05283. Ref.3
Sequence conflict501D → E in BAC05283. Ref.3
Sequence conflict2191M → T in BAC05283. Ref.3
Sequence conflict2221Q → R in BAH12863. Ref.3
Sequence conflict3961P → A in BAC05283. Ref.3

Secondary structure

... 412
Helix Strand Turn

Details...

Sequences

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

Last modified November 1, 1996. Version 1.
Checksum: A92A2A902DC9963A

FASTA41243,201
        10         20         30         40         50         60 
MPLQLLLLLI LLGPGNSLQL WDTWADEAEK ALGPLLARDR RQATEYEYLD YDFLPETEPP 

        70         80         90        100        110        120 
EMLRNSTDTT PLTGPGTPES TTVEPAARRS TGLDAGGAVT ELTTELANMG NLSTDSAAME 

       130        140        150        160        170        180 
IQTTQPAATE AQTTQPVPTE AQTTPLAATE AQTTRLTATE AQTTPLAATE AQTTPPAATE 

       190        200        210        220        230        240 
AQTTQPTGLE AQTTAPAAME AQTTAPAAME AQTTPPAAME AQTTQTTAME AQTTAPEATE 

       250        260        270        280        290        300 
AQTTQPTATE AQTTPLAAME ALSTEPSATE ALSMEPTTKR GLFIPFSVSS VTHKGIPMAA 

       310        320        330        340        350        360 
SNLSVNYPVG APDHISVKQC LLAILILALV ATIFFVCTVV LAVRLSRKGH MYPVRNYSPT 

       370        380        390        400        410 
EMVCISSLLP DGGEGPSATA NGGLSKAKSP GLTPEPREDR EGDDLTLHSF LP 

« Hide

Isoform 2 [UniParc].

Checksum: FDB7B0A35F5C4CCC
Show »

FASTA42844,648

References

« Hide 'large scale' references
[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]"Expression cloning of a functional glycoprotein ligand for P-selectin."
Sako D., Chang X.J., Barone K.M., Vachino G., White H.M., Shaw G., Veldman G.M., Bean K.M., Ahern T.J., Furie B., Cumming D.A., Larsen G.R.
Cell 75:1179-1186(1993) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), 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. expand/collapse author list , 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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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)
+Additional computationally mapped references.

Web resources

Wikipedia

P-selectin glycoprotein ligand 1 entry

SeattleSNPs

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS31895.2. [Q14242-1]
CCDS55881.1. [Q14242-2]
PIRA57468.
RefSeqNP_001193538.1. NM_001206609.1. [Q14242-2]
NP_002997.2. NM_003006.4. [Q14242-1]
XP_005269133.1. XM_005269076.1.
UniGeneHs.591014.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1G1SX-ray1.90C/D42-60[»]
ProteinModelPortalQ14242.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112304. 5 interactions.
DIPDIP-37668N.
IntActQ14242. 6 interactions.
STRING9606.ENSP00000373614.

Chemistry

BindingDBQ14242.
ChEMBLCHEMBL4183.

PTM databases

PhosphoSiteQ14242.
UniCarbKBQ14242.

Polymorphism databases

DMDM2498904.

Proteomic databases

MaxQBQ14242.
PaxDbQ14242.
PRIDEQ14242.

Protocols and materials databases

DNASU6404.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000228463; ENSP00000228463; ENSG00000110876. [Q14242-2]
ENST00000388962; ENSP00000373614; ENSG00000110876.
ENST00000550948; ENSP00000447752; ENSG00000110876. [Q14242-1]
GeneID6404.
KEGGhsa:6404.
UCSCuc001tni.3. human. [Q14242-1]

Organism-specific databases

CTD6404.
GeneCardsGC12M109015.
H-InvDBHIX0010969.
HGNCHGNC:10722. SELPLG.
HPACAB002431.
MIM600738. gene.
neXtProtNX_Q14242.
PharmGKBPA35644.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG300903.
HOGENOMHOG000013048.
HOVERGENHBG061628.
InParanoidQ14242.
KOK06544.
OMANYSPTEM.
OrthoDBEOG7CVPZ8.
PhylomeDBQ14242.
TreeFamTF337792.

Enzyme and pathway databases

ReactomeREACT_604. Hemostasis.

Gene expression databases

ArrayExpressQ14242.
BgeeQ14242.
CleanExHS_SELPLG.
GenevestigatorQ14242.

Family and domain databases

InterProIPR026195. PSGL-1.
[Graphical view]
PANTHERPTHR17384. PTHR17384. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceQ14242.
GeneWikiP-selectin_glycoprotein_ligand-1.
GenomeRNAi6404.
NextBio24882.
PMAP-CutDBA8K2Y0.
PROQ14242.
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Entry information

Entry nameSELPL_HUMAN
AccessionPrimary (citable) accession number: Q14242
Secondary accession number(s): A8K2Y0 expand/collapse secondary AC list , B4DQC3, B7Z5C7, J3KMX6, Q12775, Q6GTW7, Q8N7J7
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: July 9, 2014
This is version 131 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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