Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q14242

- SELPL_HUMAN

UniProt

Q14242 - SELPL_HUMAN

Protein

P-selectin glycoprotein ligand 1

Gene

SELPLG

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 133 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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

    1. protein binding Source: IntAct
    2. receptor binding Source: ProtInc

    GO - Biological processi

    1. blood coagulation Source: Reactome
    2. cell adhesion Source: ProtInc
    3. cellular response to interleukin-6 Source: MGI
    4. leukocyte adhesive activation Source: UniProtKB
    5. leukocyte migration Source: Reactome
    6. leukocyte tethering or rolling Source: Ensembl

    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: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:10722. SELPLG.

    Subcellular locationi

    GO - Cellular componenti

    1. integral component of membrane Source: ProtInc
    2. integral component of plasma membrane Source: ProtInc
    3. membrane Source: ProtInc
    4. plasma membrane Source: Reactome

    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. 2 Publications
    Mutagenesisi46 – 527YEYLDYD → FEFLDFE: No sulfation. Almost complete loss of P-selectin binding. No effect on E-selectin binding. 2 Publications
    Mutagenesisi46 – 516YEYLDY → FEFLDF: No sulfation. Almost complete loss of P-selectin binding. No effect on E-selectin binding. 2 Publications
    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. 2 Publications
    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. 3 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. 3 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. 3 Publications
    Mutagenesisi320 – 3201C → A or S: No dimer formation. No effect on P-selectin binding. 2 Publications

    Organism-specific databases

    PharmGKBiPA35644.

    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...)2 Publications
    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

    ArrayExpressiQ14242.
    BgeeiQ14242.
    CleanExiHS_SELPLG.
    GenevestigatoriQ14242.

    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. 5 interactions.
    DIPiDIP-37668N.
    IntActiQ14242. 6 interactions.
    STRINGi9606.ENSP00000373614.

    Structurei

    Secondary structure

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

    3D structure databases

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

    Miscellaneous databases

    EvolutionaryTraceiQ14242.

    Topological domain

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

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei321 – 34121HelicalSequence AnalysisAdd
    BLAST

    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.
    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. Align

    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

    MPLQLLLLLI LLGPGNSLQL WDTWADEAEK ALGPLLARDR RQATEYEYLD    50
    YDFLPETEPP EMLRNSTDTT PLTGPGTPES TTVEPAARRS TGLDAGGAVT 100
    ELTTELANMG NLSTDSAAME IQTTQPAATE AQTTQPVPTE AQTTPLAATE 150
    AQTTRLTATE AQTTPLAATE AQTTPPAATE AQTTQPTGLE AQTTAPAAME 200
    AQTTAPAAME AQTTPPAAME AQTTQTTAME AQTTAPEATE AQTTQPTATE 250
    AQTTPLAAME ALSTEPSATE ALSMEPTTKR GLFIPFSVSS VTHKGIPMAA 300
    SNLSVNYPVG APDHISVKQC LLAILILALV ATIFFVCTVV LAVRLSRKGH 350
    MYPVRNYSPT EMVCISSLLP DGGEGPSATA NGGLSKAKSP GLTPEPREDR 400
    EGDDLTLHSF LP 412
    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. 2 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:
    EMBL
    GenBank
    DDBJ
    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_005269076.1.
    UniGeneiHs.591014.

    Genome annotation databases

    EnsembliENST00000228463; ENSP00000228463; ENSG00000110876. [Q14242-2]
    ENST00000388962; ENSP00000373614; ENSG00000110876.
    ENST00000550948; ENSP00000447752; ENSG00000110876. [Q14242-1]
    GeneIDi6404.
    KEGGihsa:6404.
    UCSCiuc001tni.3. human. [Q14242-1]

    Polymorphism databases

    DMDMi2498904.

    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:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS31895.2. [Q14242-1 ]
    CCDS55881.1. [Q14242-2 ]
    PIRi A57468.
    RefSeqi NP_001193538.1. NM_001206609.1. [Q14242-2 ]
    NP_002997.2. NM_003006.4. [Q14242-1 ]
    XP_005269133.1. XM_005269076.1.
    UniGenei Hs.591014.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1G1S X-ray 1.90 C/D 42-60 [» ]
    ProteinModelPortali Q14242.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112304. 5 interactions.
    DIPi DIP-37668N.
    IntActi Q14242. 6 interactions.
    STRINGi 9606.ENSP00000373614.

    Chemistry

    BindingDBi Q14242.
    ChEMBLi CHEMBL4183.

    PTM databases

    PhosphoSitei Q14242.
    UniCarbKBi Q14242.

    Polymorphism databases

    DMDMi 2498904.

    Proteomic databases

    MaxQBi Q14242.
    PaxDbi Q14242.
    PRIDEi Q14242.

    Protocols and materials databases

    DNASUi 6404.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000228463 ; ENSP00000228463 ; ENSG00000110876 . [Q14242-2 ]
    ENST00000388962 ; ENSP00000373614 ; ENSG00000110876 .
    ENST00000550948 ; ENSP00000447752 ; ENSG00000110876 . [Q14242-1 ]
    GeneIDi 6404.
    KEGGi hsa:6404.
    UCSCi uc001tni.3. human. [Q14242-1 ]

    Organism-specific databases

    CTDi 6404.
    GeneCardsi GC12M109015.
    H-InvDB HIX0010969.
    HGNCi HGNC:10722. SELPLG.
    HPAi CAB002431.
    MIMi 600738. gene.
    neXtProti NX_Q14242.
    PharmGKBi PA35644.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG300903.
    HOGENOMi HOG000013048.
    HOVERGENi HBG061628.
    InParanoidi Q14242.
    KOi K06544.
    OMAi NYSPTEM.
    OrthoDBi EOG7CVPZ8.
    PhylomeDBi Q14242.
    TreeFami TF337792.

    Enzyme and pathway databases

    Reactomei REACT_12051. Cell surface interactions at the vascular wall.

    Miscellaneous databases

    EvolutionaryTracei Q14242.
    GeneWikii P-selectin_glycoprotein_ligand-1.
    GenomeRNAii 6404.
    NextBioi 24882.
    PMAP-CutDB A8K2Y0.
    PROi Q14242.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q14242.
    Bgeei Q14242.
    CleanExi HS_SELPLG.
    Genevestigatori Q14242.

    Family and domain databases

    InterProi IPR026195. PSGL-1.
    [Graphical view ]
    PANTHERi PTHR17384. PTHR17384. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 133 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