Q14242 (SELPL_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
P-selectin glycoprotein ligand 1
Short name=PSGL-1

Alternative name(s):
Selectin P ligand
CD_antigen=CD162

Gene names

Name:

SELPLG

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	412 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	A SLe(x)-type glycan, 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. PSGL1 is 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.

Ontologies

Keywords
Biological process	Cell adhesion
Cellular component	Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Repeat Signal Transmembrane Transmembrane helix
Ligand	Sialic acid
PTM	Cleavage on pair of basic residues Disulfide bond Glycoprotein Pyrrolidone carboxylic acid Sulfation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	blood coagulation Traceable author statement. Source: Reactome cell adhesion Traceable author statement Ref.2. Source: ProtInc cellular response to interleukin-6 Inferred from direct assay PubMed 9486531. Source: MGI leukocyte adhesive activation Inferred from sequence or structural similarity. Source: UniProtKB leukocyte tethering or rolling Inferred from electronic annotation. Source: InterPro
Cellular_component	integral to plasma membrane Traceable author statement Ref.2. Source: ProtInc
Molecular_function	bacterial cell surface binding Traceable author statement PubMed 10834846. Source: ProtInc receptor binding Non-traceable author statement Ref.2. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
SNX20	Q7Z614	5	EBI-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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 17

17

Potential

Propeptide

18 – 41

24

PRO_0000022302

Chain

42 – 412

371

P-selectin glycoprotein ligand 1

PRO_0000022303

Regions

Topological domain

18 – 320

303

Extracellular Potential

Transmembrane

321 – 341

21

Helical; Potential

Topological domain

342 – 412

71

Cytoplasmic Potential

Repeat

122 – 131

10

1

Repeat

132 – 141

10

2

Repeat

142 – 151

10

3

Repeat

162 – 171

10

4

Repeat

182 – 191

10

5

Repeat

192 – 201

10

6

Repeat

202 – 211

10

7

Repeat

212 – 221

10

8

Repeat

222 – 231

10

9

Repeat

232 – 241

10

10

Repeat

242 – 251

10

11

Repeat

252 – 261

10

12

Region

122 – 261

140

12 X 10 AA tandem repeats

Amino acid modifications

Modified residue

42

1

Pyrrolidone carboxylic acid

Modified residue

46

1

Sulfotyrosine Ref.19

Modified residue

48

1

Sulfotyrosine Ref.19

Modified residue

51

1

Sulfotyrosine Ref.19

Glycosylation

57

1

O-linked (GalNAc...) Ref.19

Glycosylation

65

1

N-linked (GlcNAc...) Potential

Glycosylation

111

1

N-linked (GlcNAc...) Potential

Glycosylation

302

1

N-linked (GlcNAc...) Potential

Disulfide bond

320

Interchain Ref.12

Natural variations

Alternative sequence

1

1

M → MAVGASGLEGDKMAGAM in isoform 2.

VSP_044827

Natural variant

62

1

M → I. Ref.3 Ref.4
Corresponds to variant rs2228315 [ dbSNP | Ensembl ].

VAR_019156

Natural variant

132 – 141

10

Missing in short form; not an alternative splicing.
Corresponds to variant rs63748999 [ dbSNP | Ensembl ].

VAR_005611

Natural variant

246

1

P → S. Ref.4
Corresponds to variant rs8179142 [ dbSNP | Ensembl ].

VAR_019157

Experimental info

Mutagenesis

44

1

T → A: No effect on L-selectin binding nor neutrophil rolling. Ref.15

Mutagenesis

46 – 52

7

YEYLDYD → FEFLDFE: No sulfation. Almost complete loss of P-selectin binding. No effect on E-selectin binding. Ref.8 Ref.9

Mutagenesis

46 – 51

6

YEYLDY → FEFLDF: No sulfation. Almost complete loss of P-selectin binding. No effect on E-selectin binding. Ref.9 Ref.15

Mutagenesis

46

1

Y → 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

Mutagenesis

48

1

Y → 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

Mutagenesis

51

1

Y → 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

Mutagenesis

57

1

T → 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

Mutagenesis

320

1

C → A or S: No dimer formation. No effect on P-selectin binding. Ref.12

Sequence conflict

23 – 39

17

Missing in BAC05283. Ref.3

Sequence conflict

50

1

D → E in BAC05283. Ref.3

Sequence conflict

219

1

M → T in BAC05283. Ref.3

Sequence conflict

222

1

Q → R in BAH12863. Ref.3

Sequence conflict

396

1

P → A in BAC05283. Ref.3

Secondary structure

1

.

.

.

412

Helix Strand Turn

Details...

Turn

51 – 53

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: A92A2A902DC9963A	FASTA	412	43,201
	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
	Isoform 2 [UniParc]. Checksum: FDB7B0A35F5C4CCC	FASTA	428	44,648
	10 20 30 40 50 60 MAVGASGLEG DKMAGAMPLQ LLLLLILLGP GNSLQLWDTW ADEAEKALGP LLARDRRQAT 70 80 90 100 110 120 EYEYLDYDFL PETEPPEMLR NSTDTTPLTG PGTPESTTVE PAARRSTGLD AGGAVTELTT 130 140 150 160 170 180 ELANMGNLST DSAAMEIQTT QPAATEAQTT QPVPTEAQTT PLAATEAQTT RLTATEAQTT 190 200 210 220 230 240 PLAATEAQTT PPAATEAQTT QPTGLEAQTT APAAMEAQTT APAAMEAQTT PPAAMEAQTT 250 260 270 280 290 300 QTTAMEAQTT APEATEAQTT QPTATEAQTT PLAAMEALST EPSATEALSM EPTTKRGLFI 310 320 330 340 350 360 PFSVSSVTHK GIPMAASNLS VNYPVGAPDH ISVKQCLLAI LILALVATIF FVCTVVLAVR 370 380 390 400 410 420 LSRKGHMYPV RNYSPTEMVC ISSLLPDGGE GPSATANGGL SKAKSPGLTP EPREDREGDD LTLHSFLP

References

	« Hide 'large scale' referencesShow '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. , 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]	"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.

IPI

IPI00029591.
IPI01018057.

PIR

A57468.

RefSeq

NP_001193538.1. NM_001206609.1.
NP_002997.2. NM_003006.4.

UniGene

Hs.591014.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1G1S	X-ray	1.90	C/D	42-60	[»]

ProteinModelPortal

Q14242.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-37668N.

IntAct

Q14242. 6 interactions.

STRING

9606.ENSP00000373614.

PTM databases

GlycoSuiteDB

Q14242.

PhosphoSite

Q14242.

Polymorphism databases

DMDM

2498904.

Proteomic databases

PaxDb

Q14242.

PRIDE

Q14242.

Protocols and materials databases

DNASU

6404.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000228463; ENSP00000228463; ENSG00000110876.
ENST00000388962; ENSP00000373614; ENSG00000110876.
ENST00000550948; ENSP00000447752; ENSG00000110876.

GeneID

6404.

KEGG

hsa:6404.

UCSC

uc001tni.3. human.

Organism-specific databases

CTD

6404.

GeneCards

GC12M109015.

H-InvDB

HIX0010969.

HGNC

HGNC:10722. SELPLG.

HPA

CAB002431.

MIM

600738. gene.

neXtProt

NX_Q14242.

PharmGKB

PA35644.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG300903.

HOGENOM

HOG000013048.

HOVERGEN

HBG061628.

InParanoid

Q14242.

KO

K06544.

OMA

NYSPTEM.

OrthoDB

EOG4GMTZH.

Enzyme and pathway databases

Pathway_Interaction_DB

amb2_neutrophils_pathway. amb2 Integrin signaling.

Reactome

REACT_604. Hemostasis.

Gene expression databases

ArrayExpress

Q14242.

Bgee

Q14242.

CleanEx

HS_SELPLG.

Genevestigator

Q14242.

GermOnline

ENSG00000110876. Homo sapiens.

Family and domain databases

InterPro

IPR026195. PSGL-1.
[Graphical view]

PANTHER

PTHR17384. PTHR17384. 1 hit.

ProtoNet

Search...

Other

BindingDB

Q14242.

ChEMBL

CHEMBL4183.

EvolutionaryTrace

Q14242.

GenomeRNAi

6404.

NextBio

24882.

PMAP-CutDB

A8K2Y0.

SOURCE

Search...

Entry information

Entry name

SELPL_HUMAN

Accession

Primary (citable) accession number: Q14242
Secondary accession number(s): A8K2Y0 , B4DQC3, B7Z5C7, J3KMX6, Q12775, Q6GTW7, Q8N7J7

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1996
Last modified:	April 3, 2013
This is version 118 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.