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Q8WWQ8

- STAB2_HUMAN

UniProt

Q8WWQ8 - STAB2_HUMAN

Protein

Stabilin-2

Gene

STAB2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 121 (01 Oct 2014)
      Sequence version 3 (17 Apr 2007)
      Previous versions | rss
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    Functioni

    Phosphatidylserine receptor that enhances the engulfment of apoptotic cells. Hyaluronan receptor that binds to and mediates endocytosis of hyaluronic acid (HA). Acts also, in different species, as a primary systemic scavenger receptor for heparin (Hep), chondroitin sulfate (CS), dermatan sulfate (DS), nonglycosaminoglycan (GAG), acetylated low-density lipoprotein (AcLDL), pro-collagen propeptides and advanced glycation end products (AGE). May serve to maintain tissue integrity by supporting extracellular matrix turnover or it may contribute to maintaining fluidity of bodily liquids by resorption of hyaluronan. Counter receptor which plays an important role in lymphocyte recruitment in the hepatic vasculature. Binds to both Gram-positive and Gram-negative bacteria and may play a role in defense against bacterial infection. The proteolytically processed 190 kDa form also functions as an endocytosis receptor for heparin internalisation as well as HA and CS.11 Publications

    GO - Molecular functioni

    1. hyaluronic acid binding Source: UniProtKB
    2. low-density lipoprotein particle binding Source: UniProtKB
    3. low-density lipoprotein receptor activity Source: UniProtKB
    4. protein binding Source: IntAct
    5. protein disulfide oxidoreductase activity Source: UniProtKB
    6. scavenger receptor activity Source: UniProtKB

    GO - Biological processi

    1. angiogenesis Source: UniProtKB
    2. carbohydrate metabolic process Source: Reactome
    3. cell adhesion Source: UniProtKB
    4. defense response to bacterium Source: UniProtKB
    5. endocytosis Source: UniProtKB
    6. glycosaminoglycan metabolic process Source: Reactome
    7. hyaluronan catabolic process Source: Reactome
    8. hyaluronan metabolic process Source: Reactome
    9. oxidation-reduction process Source: GOC
    10. receptor-mediated endocytosis Source: UniProtKB
    11. regulation of blood coagulation Source: UniProt
    12. regulation of gene expression Source: UniProt
    13. small molecule metabolic process Source: Reactome

    Keywords - Molecular functioni

    Receptor

    Keywords - Biological processi

    Endocytosis

    Keywords - Ligandi

    Hyaluronic acid

    Enzyme and pathway databases

    ReactomeiREACT_120996. Hyaluronan uptake and degradation.
    REACT_164002. Scavenging by Class H Receptors.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Stabilin-2
    Alternative name(s):
    FAS1 EGF-like and X-link domain-containing adhesion molecule 2
    Fasciclin, EGF-like, laminin-type EGF-like and link domain-containing scavenger receptor 2
    Short name:
    FEEL-2
    Hyaluronan receptor for endocytosis
    Cleaved into the following chain:
    Alternative name(s):
    190 kDa hyaluronan receptor for endocytosis
    Gene namesi
    Name:STAB2Imported
    Synonyms:FEEL21 Publication, FELL1 Publication, FEX21 Publication, HAREImported
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:18629. STAB2.

    Subcellular locationi

    Cell membrane; Single-pass type I membrane protein. Cytoplasm
    Note: Only a small amount appears to be present at the cell surface.

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. endocytic vesicle membrane Source: Reactome
    3. external side of plasma membrane Source: UniProtKB
    4. integral component of plasma membrane Source: UniProtKB
    5. plasma membrane Source: Reactome

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA38611.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1919Sequence AnalysisAdd
    BLAST
    Chaini20 – 25512532Stabilin-2PRO_0000007712Add
    BLAST
    Chaini1136 – 25511416190 kDa form stabilin-2PRO_0000007713Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi112 ↔ 126By similarity
    Disulfide bondi120 ↔ 136By similarity
    Glycosylationi133 – 1331N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi138 ↔ 147By similarity
    Disulfide bondi160 ↔ 171By similarity
    Disulfide bondi164 ↔ 181By similarity
    Disulfide bondi183 ↔ 192By similarity
    Disulfide bondi199 ↔ 210By similarity
    Disulfide bondi204 ↔ 222By similarity
    Disulfide bondi224 ↔ 235By similarity
    Disulfide bondi241 ↔ 252By similarity
    Disulfide bondi246 ↔ 262By similarity
    Disulfide bondi264 ↔ 275By similarity
    Disulfide bondi326 ↔ 338By similarity
    Disulfide bondi332 ↔ 348By similarity
    Glycosylationi337 – 3371N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi350 ↔ 361By similarity
    Glycosylationi449 – 4491N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi619 – 6191N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi720 – 7201N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi740 ↔ 754By similarity
    Disulfide bondi748 ↔ 764By similarity
    Glycosylationi761 – 7611N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi766 ↔ 775By similarity
    Disulfide bondi830 ↔ 843By similarity
    Disulfide bondi837 ↔ 852By similarity
    Glycosylationi847 – 8471N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi854 ↔ 865By similarity
    Disulfide bondi871 ↔ 885By similarity
    Disulfide bondi879 ↔ 895By similarity
    Disulfide bondi897 ↔ 908By similarity
    Disulfide bondi914 ↔ 928By similarity
    Disulfide bondi922 ↔ 938By similarity
    Glycosylationi925 – 9251N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi940 ↔ 951By similarity
    Disulfide bondi957 ↔ 970By similarity
    Disulfide bondi964 ↔ 980By similarity
    Glycosylationi1016 – 10161N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1028 – 10281N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1100 – 11001N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1247 – 12471N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1275 – 12751N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1348 ↔ 1362By similarity
    Disulfide bondi1356 ↔ 1372By similarity
    Glycosylationi1367 – 13671N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1374 ↔ 1383By similarity
    Disulfide bondi1395 ↔ 1406By similarity
    Disulfide bondi1399 ↔ 1416By similarity
    Disulfide bondi1418 ↔ 1427By similarity
    Glycosylationi1429 – 14291N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1436 ↔ 1446By similarity
    Glycosylationi1437 – 14371N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1440 ↔ 1456By similarity
    Disulfide bondi1458 ↔ 1469By similarity
    Glycosylationi1465 – 14651N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1475 ↔ 1488By similarity
    Disulfide bondi1482 ↔ 1498By similarity
    Disulfide bondi1500 ↔ 1511By similarity
    Disulfide bondi1517 ↔ 1530By similarity
    Disulfide bondi1524 ↔ 1540By similarity
    Disulfide bondi1542 ↔ 1553By similarity
    Disulfide bondi1559 ↔ 1572By similarity
    Disulfide bondi1566 ↔ 1582By similarity
    Glycosylationi1573 – 15731N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1679 – 16791N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1743 – 17431N-linked (GlcNAc...)2 Publications
    Disulfide bondi1962 ↔ 1976By similarity
    Disulfide bondi1970 ↔ 1986By similarity
    Disulfide bondi1988 ↔ 1997By similarity
    Glycosylationi1993 – 19931N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi2009 ↔ 2020By similarity
    Disulfide bondi2014 ↔ 2030By similarity
    Disulfide bondi2032 ↔ 2041By similarity
    Disulfide bondi2051 ↔ 2061By similarity
    Disulfide bondi2055 ↔ 2067By similarity
    Glycosylationi2064 – 20641N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi2069 ↔ 2080By similarity
    Disulfide bondi2086 ↔ 2099By similarity
    Disulfide bondi2093 ↔ 2108By similarity
    Disulfide bondi2110 ↔ 2121By similarity
    Disulfide bondi2127 ↔ 2141By similarity
    Disulfide bondi2135 ↔ 2151By similarity
    Disulfide bondi2153 ↔ 2164By similarity
    Disulfide bondi2220 ↔ 2289By similarity
    Disulfide bondi2244 ↔ 2265By similarity
    Glycosylationi2280 – 22801N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi2296 – 22961N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi2336 – 23361N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi2368 – 23681N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi2382 – 23821N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi2393 – 23931N-linked (GlcNAc...)Sequence Analysis
    Modified residuei2497 – 24971PhosphoserineBy similarity

    Post-translational modificationi

    Glycosylated.2 Publications
    Proteolytically processed to yield a 190 kDa protein.1 Publication

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Phosphoprotein

    Proteomic databases

    MaxQBiQ8WWQ8.
    PaxDbiQ8WWQ8.
    PRIDEiQ8WWQ8.

    PTM databases

    PhosphoSiteiQ8WWQ8.

    Expressioni

    Tissue specificityi

    Highly expressed in sinusoidal endothelial cells of liver, spleen and lymph nodes. Also expressed in non SEC-cells such as HMDMs (monocyte-derivedmacrophages), HAMs (T-cell leukemia virus type 1-associated myelopathy), and several macrophage cell line.6 Publications

    Gene expression databases

    ArrayExpressiQ8WWQ8.
    BgeeiQ8WWQ8.
    CleanExiHS_STAB2.
    GenevestigatoriQ8WWQ8.

    Organism-specific databases

    HPAiHPA026871.

    Interactioni

    Subunit structurei

    Interacts with GULP1 and heparin. Also interacts with alpha-M/beta-2 integrin (ITGAM and ITGB2) and thymosin beta 4 (TMSB4X and/or TMSB4Y).3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Tmsb4xP200653EBI-7945957,EBI-7946048From a different organism.

    Protein-protein interaction databases

    BioGridi120727. 7 interactions.
    IntActiQ8WWQ8. 2 interactions.
    MINTiMINT-6542238.
    STRINGi9606.ENSP00000373539.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8WWQ8.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini20 – 24582439ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini2480 – 255172CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei2459 – 247921HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini108 – 14841EGF-like 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini156 – 19338EGF-like 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini195 – 23642EGF-like 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini237 – 27640EGF-like 4PROSITE-ProRule annotationAdd
    BLAST
    Domaini322 – 36241EGF-like 5PROSITE-ProRule annotationAdd
    BLAST
    Domaini371 – 505135FAS1 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini515 – 652138FAS1 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini736 – 77641EGF-like 6PROSITE-ProRule annotationAdd
    BLAST
    Domaini826 – 86641EGF-like 7PROSITE-ProRule annotationAdd
    BLAST
    Domaini867 – 90943EGF-like 8PROSITE-ProRule annotationAdd
    BLAST
    Domaini910 – 95243EGF-like 9PROSITE-ProRule annotationAdd
    BLAST
    Domaini953 – 99240EGF-like 10PROSITE-ProRule annotationAdd
    BLAST
    Domaini994 – 1127134FAS1 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini1137 – 1265129FAS1 4PROSITE-ProRule annotationAdd
    BLAST
    Domaini1343 – 140866Laminin EGF-like 1Sequence AnalysisAdd
    BLAST
    Domaini1432 – 147039EGF-like 11PROSITE-ProRule annotationAdd
    BLAST
    Domaini1471 – 151242EGF-like 12PROSITE-ProRule annotationAdd
    BLAST
    Domaini1513 – 155442EGF-like 13PROSITE-ProRule annotationAdd
    BLAST
    Domaini1555 – 159440EGF-like 14PROSITE-ProRule annotationAdd
    BLAST
    Domaini1596 – 1724129FAS1 5PROSITE-ProRule annotationAdd
    BLAST
    Domaini1740 – 1881142FAS1 6PROSITE-ProRule annotationAdd
    BLAST
    Domaini1957 – 202266Laminin EGF-like 2Sequence AnalysisAdd
    BLAST
    Domaini2047 – 208135EGF-like 15PROSITE-ProRule annotationAdd
    BLAST
    Domaini2082 – 212241EGF-like 16PROSITE-ProRule annotationAdd
    BLAST
    Domaini2123 – 216543EGF-like 17PROSITE-ProRule annotationAdd
    BLAST
    Domaini2198 – 229194LinkPROSITE-ProRule annotationAdd
    BLAST
    Domaini2311 – 2446136FAS1 7PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni2504 – 251411Interaction with TMSB4XAdd
    BLAST

    Domaini

    Recognizes phosphatidyl serine via its epidermal growth factor-like domains.

    Sequence similaritiesi

    Contains 17 EGF-like domains.PROSITE-ProRule annotation
    Contains 7 FAS1 domains.PROSITE-ProRule annotation
    Contains 2 laminin EGF-like domains.Sequence Analysis
    Contains 1 Link domain.PROSITE-ProRule annotation

    Keywords - Domaini

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

    Phylogenomic databases

    eggNOGiCOG2335.
    HOVERGENiHBG079218.
    InParanoidiQ8WWQ8.
    OMAiIPKCCKG.
    OrthoDBiEOG7PS1DH.
    PhylomeDBiQ8WWQ8.
    TreeFamiTF331489.

    Family and domain databases

    Gene3Di2.30.180.10. 7 hits.
    2.40.155.10. 8 hits.
    3.10.100.10. 1 hit.
    InterProiIPR016186. C-type_lectin-like.
    IPR016187. C-type_lectin_fold.
    IPR000742. EG-like_dom.
    IPR013032. EGF-like_CS.
    IPR024731. EGF_dom_MSP1-like.
    IPR002049. EGF_laminin.
    IPR000782. FAS1_domain.
    IPR023413. GFP_like.
    IPR000538. Link.
    [Graphical view]
    PfamiPF12947. EGF_3. 7 hits.
    PF02469. Fasciclin. 7 hits.
    PF00193. Xlink. 1 hit.
    [Graphical view]
    SMARTiSM00181. EGF. 20 hits.
    SM00554. FAS1. 7 hits.
    SM00445. LINK. 1 hit.
    [Graphical view]
    SUPFAMiSSF56436. SSF56436. 1 hit.
    SSF82153. SSF82153. 7 hits.
    PROSITEiPS00022. EGF_1. 7 hits.
    PS01186. EGF_2. 16 hits.
    PS50026. EGF_3. 21 hits.
    PS01248. EGF_LAM_1. 2 hits.
    PS50213. FAS1. 7 hits.
    PS01241. LINK_1. 1 hit.
    PS50963. LINK_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q8WWQ8-1 [UniParc]FASTAAdd to Basket

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    MMLQHLVIFC LGLVVQNFCS PAETTGQARR CDRKSLLTIR TECRSCALNL     50
    GVKCPDGYTM ITSGSVGVRD CRYTFEVRTY SLSLPGCRHI CRKDYLQPRC 100
    CPGRWGPDCI ECPGGAGSPC NGRGSCAEGM EGNGTCSCQE GFGGTACETC 150
    ADDNLFGPSC SSVCNCVHGV CNSGLDGDGT CECYSAYTGP KCDKPIPECA 200
    ALLCPENSRC SPSTEDENKL ECKCLPNYRG DGKYCDPINP CLRKICHPHA 250
    HCTYLGPNRH SCTCQEGYRG DGQVCLPVDP CQINFGNCPT KSTVCKYDGP 300
    GQSHCECKEH YQNFVPGVGC SMTDICKSDN PCHRNANCTT VAPGRTECIC 350
    QKGYVGDGLT CYGNIMERLR ELNTEPRGKW QGRLTSFISL LDKAYAWPLS 400
    KLGPFTVLLP TDKGLKGFNV NELLVDNKAA QYFVKLHIIA GQMNIEYMNN 450
    TDMFYTLTGK SGEIFNSDKD NQIKLKLHGG KKKVKIIQGD IIASNGLLHI 500
    LDRAMDKLEP TFESNNEQTI MTMLQPRYSK FRSLLEETNL GHALDEDGVG 550
    GPYTIFVPNN EALNNMKDGT LDYLLSPEGS RKLLELVRYH IVPFTQLEVA 600
    TLISTPHIRS MANQLIQFNT TDNGQILAND VAMEEIEITA KNGRIYTLTG 650
    VLIPPSIVPI LPHRCDETKR EMKLGTCVSC SLVYWSRCPA NSEPTALFTH 700
    RCVYSGRFGS LKSGCARYCN ATVKIPKCCK GFYGPDCNQC PGGFSNPCSG 750
    NGQCADSLGG NGTCICEEGF QGSQCQFCSD PNKYGPRCNK KCLCVHGTCN 800
    NRIDSDGACL TGTCRDGSAG RLCDKQTSAC GPYVQFCHIH ATCEYSNGTA 850
    SCICKAGYEG DGTLCSEMDP CTGLTPGGCS RNAECIKTGT GTHTCVCQQG 900
    WTGNGRDCSE INNCLLPSAG GCHDNASCLY VGPGQNECEC KKGFRGNGID 950
    CEPITSCLEQ TGKCHPLASC QSTSSGVWSC VCQEGYEGDG FLCYGNAAVE 1000
    LSFLSEAAIF NRWINNASLQ PTLSATSNLT VLVPSQQATE DMDQDEKSFW 1050
    LSQSNIPALI KYHMLLGTYR VADLQTLSSS DMLATSLQGN FLHLAKVDGN 1100
    ITIEGASIVD GDNAATNGVI HIINKVLVPQ RRLTGSLPNL LMRLEQMPDY 1150
    SIFRGYIIQY NLANAIEAAD AYTVFAPNNN AIENYIREKK VLSLEEDVLR 1200
    YHVVLEEKLL KNDLHNGMHR ETMLGFSYFL SFFLHNDQLY VNEAPINYTN 1250
    VATDKGVIHG LGKVLEIQKN RCDNNDTTII RGRCRTCSSE LTCPFGTKSL 1300
    GNEKRRCIYT SYFMGRRTLF IGCQPKCVRT VITRECCAGF FGPQCQPCPG 1350
    NAQNVCFGNG ICLDGVNGTG VCECGEGFSG TACETCTEGK YGIHCDQACS 1400
    CVHGRCNQGP LGDGSCDCDV GWRGVHCDNA TTEDNCNGTC HTSANCLTNS 1450
    DGTASCKCAA GFQGNGTICT AINACEISNG GCSAKADCKR TTPGRRVCTC 1500
    KAGYTGDGIV CLEINPCLEN HGGCDKNAEC TQTGPNQAAC NCLPAYTGDG 1550
    KVCTLINVCL TKNGGCSEFA ICNHTGQVER TCTCKPNYIG DGFTCRGSIY 1600
    QELPKNPKTS QYFFQLQEHF VKDLVGPGPF TVFAPLSAAF DEEARVKDWD 1650
    KYGLMPQVLR YHVVACHQLL LENLKLISNA TSLQGEPIVI SVSQSTVYIN 1700
    NKAKIISSDI ISTNGIVHII DKLLSPKNLL ITPKDNSGRI LQNLTTLATN 1750
    NGYIKFSNLI QDSGLLSVIT DPIHTPVTLF WPTDQALHAL PAEQQDFLFN 1800
    QDNKDKLKEY LKFHVIRDAK VLAVDLPTST AWKTLQGSEL SVKCGAGRDI 1850
    GDLFLNGQTC RIVQRELLFD LGVAYGIDCL LIDPTLGGRC DTFTTFDASG 1900
    ECGSCVNTPS CPRWSKPKGV KQKCLYNLPF KRNLEGCRER CSLVIQIPRC 1950
    CKGYFGRDCQ ACPGGPDAPC NNRGVCLDQY SATGECKCNT GFNGTACEMC 2000
    WPGRFGPDCL PCGCSDHGQC DDGITGSGQC LCETGWTGPS CDTQAVLPAV 2050
    CTPPCSAHAT CKENNTCECN LDYEGDGITC TVVDFCKQDN GGCAKVARCS 2100
    QKGTKVSCSC QKGYKGDGHS CTEIDPCADG LNGGCHEHAT CKMTGPGKHK 2150
    CECKSHYVGD GLNCEPEQLP IDRCLQDNGQ CHADAKCVDL HFQDTTVGVF 2200
    HLRSPLGQYK LTFDKAREAC ANEAATMATY NQLSYAQKAK YHLCSAGWLE 2250
    TGRVAYPTAF ASQNCGSGVV GIVDYGPRPN KSEMWDVFCY RMKDVNCTCK 2300
    VGYVGDGFSC SGNLLQVLMS FPSLTNFLTE VLAYSNSSAR GRAFLEHLTD 2350
    LSIRGTLFVP QNSGLGENET LSGRDIEHHL ANVSMFFYND LVNGTTLQTR 2400
    LGSKLLITAS QDPLQPTETR FVDGRAILQW DIFASNGIIH VISRPLKAPP 2450
    APVTLTHTGL GAGIFFAIIL VTGAVALAAY SYFRINRRTI GFQHFESEED 2500
    INVAALGKQQ PENISNPLYE STTSAPPEPS YDPFTDSEER QLEGNDPLRT 2550
    L 2551
    Length:2,551
    Mass (Da):276,988
    Last modified:April 17, 2007 - v3
    Checksum:i3ACB6A6C3CB80044
    GO

    Sequence cautioni

    The sequence BAD18723.1 differs from that shown. Reason: Frameshift at positions 240, 253, 588 and 1586.
    The sequence AAF82398.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti67 – 671G → R in BAD18723. 1 PublicationCurated
    Sequence conflicti152 – 1521D → A in BAD18723. 1 PublicationCurated
    Sequence conflicti887 – 8871K → N in BAD18723. 1 PublicationCurated
    Sequence conflicti1136 – 11361S → L AA sequence (PubMed:17145755)Curated
    Sequence conflicti1151 – 11511S → P in CAC82105. (PubMed:11829752)Curated
    Sequence conflicti1276 – 12761D → A in CAC82105. (PubMed:11829752)Curated
    Sequence conflicti1522 – 15221G → C in BAD18723. 1 PublicationCurated
    Sequence conflicti1557 – 15571N → Y in AAO39681. (PubMed:12626425)Curated
    Sequence conflicti1599 – 16002IY → HE in AAF82398. 1 PublicationCurated
    Sequence conflicti1854 – 18541F → S in BAD18723. 1 PublicationCurated
    Sequence conflicti2249 – 22491L → V in BAD18723. 1 PublicationCurated
    Sequence conflicti2253 – 22531R → G in BAD18723. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti110 – 1101I → V.
    Corresponds to variant rs17034186 [ dbSNP | Ensembl ].
    VAR_048995
    Natural varianti306 – 3061E → K.
    Corresponds to variant rs12319476 [ dbSNP | Ensembl ].
    VAR_048996
    Natural varianti510 – 5101P → H.2 Publications
    Corresponds to variant rs1609860 [ dbSNP | Ensembl ].
    VAR_019541
    Natural varianti787 – 7871R → Q.
    Corresponds to variant rs17034336 [ dbSNP | Ensembl ].
    VAR_048997
    Natural varianti881 – 8811R → H.
    Corresponds to variant rs7973658 [ dbSNP | Ensembl ].
    VAR_048998
    Natural varianti1736 – 17361N → T.
    Corresponds to variant rs17034433 [ dbSNP | Ensembl ].
    VAR_048999
    Natural varianti2039 – 20391P → T.2 Publications
    Corresponds to variant rs7306642 [ dbSNP | Ensembl ].
    VAR_049000
    Natural varianti2401 – 24011L → V.2 Publications
    Corresponds to variant rs2271637 [ dbSNP | Ensembl ].
    VAR_049001
    Natural varianti2519 – 25191Y → S.
    Corresponds to variant rs3751197 [ dbSNP | Ensembl ].
    VAR_049002

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ295695 mRNA. Translation: CAC82105.1.
    AB052958 mRNA. Translation: BAC15608.1.
    AY311388 mRNA. Translation: AAP74958.1.
    AK024503 mRNA. Translation: BAB15793.1.
    AK074051 mRNA. Translation: BAB84877.1.
    AK160380 mRNA. Translation: BAD18723.1. Frameshift.
    AY227444 mRNA. Translation: AAO39681.1.
    AF160476 mRNA. Translation: AAF82398.1. Different initiation.
    CCDSiCCDS31888.1.
    RefSeqiNP_060034.9. NM_017564.9.
    UniGeneiHs.408249.

    Genome annotation databases

    EnsembliENST00000388887; ENSP00000373539; ENSG00000136011.
    GeneIDi55576.
    KEGGihsa:55576.
    UCSCiuc001tjw.3. human.

    Polymorphism databases

    DMDMi145559531.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ295695 mRNA. Translation: CAC82105.1 .
    AB052958 mRNA. Translation: BAC15608.1 .
    AY311388 mRNA. Translation: AAP74958.1 .
    AK024503 mRNA. Translation: BAB15793.1 .
    AK074051 mRNA. Translation: BAB84877.1 .
    AK160380 mRNA. Translation: BAD18723.1 . Frameshift.
    AY227444 mRNA. Translation: AAO39681.1 .
    AF160476 mRNA. Translation: AAF82398.1 . Different initiation.
    CCDSi CCDS31888.1.
    RefSeqi NP_060034.9. NM_017564.9.
    UniGenei Hs.408249.

    3D structure databases

    ProteinModelPortali Q8WWQ8.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 120727. 7 interactions.
    IntActi Q8WWQ8. 2 interactions.
    MINTi MINT-6542238.
    STRINGi 9606.ENSP00000373539.

    PTM databases

    PhosphoSitei Q8WWQ8.

    Polymorphism databases

    DMDMi 145559531.

    Proteomic databases

    MaxQBi Q8WWQ8.
    PaxDbi Q8WWQ8.
    PRIDEi Q8WWQ8.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000388887 ; ENSP00000373539 ; ENSG00000136011 .
    GeneIDi 55576.
    KEGGi hsa:55576.
    UCSCi uc001tjw.3. human.

    Organism-specific databases

    CTDi 55576.
    GeneCardsi GC12P103981.
    HGNCi HGNC:18629. STAB2.
    HPAi HPA026871.
    MIMi 608561. gene.
    neXtProti NX_Q8WWQ8.
    PharmGKBi PA38611.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG2335.
    HOVERGENi HBG079218.
    InParanoidi Q8WWQ8.
    OMAi IPKCCKG.
    OrthoDBi EOG7PS1DH.
    PhylomeDBi Q8WWQ8.
    TreeFami TF331489.

    Enzyme and pathway databases

    Reactomei REACT_120996. Hyaluronan uptake and degradation.
    REACT_164002. Scavenging by Class H Receptors.

    Miscellaneous databases

    GeneWikii STAB2.
    GenomeRNAii 55576.
    NextBioi 60076.
    PROi Q8WWQ8.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q8WWQ8.
    Bgeei Q8WWQ8.
    CleanExi HS_STAB2.
    Genevestigatori Q8WWQ8.

    Family and domain databases

    Gene3Di 2.30.180.10. 7 hits.
    2.40.155.10. 8 hits.
    3.10.100.10. 1 hit.
    InterProi IPR016186. C-type_lectin-like.
    IPR016187. C-type_lectin_fold.
    IPR000742. EG-like_dom.
    IPR013032. EGF-like_CS.
    IPR024731. EGF_dom_MSP1-like.
    IPR002049. EGF_laminin.
    IPR000782. FAS1_domain.
    IPR023413. GFP_like.
    IPR000538. Link.
    [Graphical view ]
    Pfami PF12947. EGF_3. 7 hits.
    PF02469. Fasciclin. 7 hits.
    PF00193. Xlink. 1 hit.
    [Graphical view ]
    SMARTi SM00181. EGF. 20 hits.
    SM00554. FAS1. 7 hits.
    SM00445. LINK. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56436. SSF56436. 1 hit.
    SSF82153. SSF82153. 7 hits.
    PROSITEi PS00022. EGF_1. 7 hits.
    PS01186. EGF_2. 16 hits.
    PS50026. EGF_3. 21 hits.
    PS01248. EGF_LAM_1. 2 hits.
    PS50213. FAS1. 7 hits.
    PS01241. LINK_1. 1 hit.
    PS50963. LINK_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, VARIANT HIS-510.
    2. "FEEL-1, a novel scavenger receptor with in vitro bacteria-binding and angiogenesis-modulating activities."
      Adachi H., Tsujimoto M.
      J. Biol. Chem. 277:34264-34270(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, VARIANT HIS-510.
    3. "FEX2, a novel cell adhesion molecule of Fas-1 superfamily mediates cell-cell interaction."
      Park S.-Y., Kim I.-S.
      Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    4. "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] OF 35-2551, VARIANT THR-2039.
      Tissue: SpleenImported.
    5. "The nucleotide sequence of a long cDNA clone isolated from human spleen."
      Jikuya H., Takano J., Nomura N., Kikuno R., Nagase T., Ohara O.
      Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 35-2551, VARIANTS THR-2039 AND VAL-2401.
      Tissue: Spleen.
    6. "Purification and molecular identification of the human hyaluronan receptor for endocytosis."
      Zhou B., McGary C.T., Weigel J.A., Saxena A., Weigel P.H.
      Glycobiology 13:339-349(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1136-2551, PROTEIN SEQUENCE OF 1136-1144; 1257-1269; 1597-1605; 1623-1645; 1652-1660; 1813-1817; 1834-1843; 1914-1918; 1953-1957; 2204-2217; 2211-2215 AND 2355-2367, TISSUE SPECIFICITY.
    7. "Molecular cloning and characterization of human FELL sharing homology with CD44."
      Tao Q., Zhang W., Cao X.
      Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1599-2551, VARIANT VAL-2401.
    8. "Expression, processing, and glycosaminoglycan binding activity of the recombinant human 315-kDa hyaluronic acid receptor for endocytosis (HARE)."
      Harris E.N., Kyosseva S.V., Weigel J.A., Weigel P.H.
      J. Biol. Chem. 282:2785-2797(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1136-1144, GLYCOSYLATION, SUBCELLULAR LOCATION, FUNCTION.
    9. Cited for: FUNCTION, TISSUE SPECIFICITY.
    10. "Endocytic function, glycosaminoglycan specificity, and antibody sensitivity of the recombinant human 190-kDa hyaluronan receptor for endocytosis (HARE)."
      Harris E.N., Weigel J.A., Weigel P.H.
      J. Biol. Chem. 279:36201-36209(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    11. "Stabilin-1 and stabilin-2 are both directed into the early endocytic pathway in hepatic sinusoidal endothelium via interactions with clathrin/AP-2, independent of ligand binding."
      Hansen B., Longati P., Elvevold K., Nedredal G.-I., Schledzewski K., Olsen R., Falkowski M., Kzhyshkowska J., Carlsson F., Johansson S., Smedsroed B., Goerdt S., Johansson S., McCourt P.
      Exp. Cell Res. 303:160-173(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    12. "Stabilin-2 is involved in lymphocyte adhesion to the hepatic sinusoidal endothelium via the interaction with alphaMbeta2 integrin."
      Jung M.Y., Park S.Y., Kim I.S.
      J. Leukoc. Biol. 82:1156-1165(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, FUNCTION, TISSUE SPECIFICITY, INTERACTION WITH ALPHA-M/BETA-2 [ITGAM/ITGB2] INTEGRIN.
    13. Erratum
      Jung M.Y., Park S.Y., Kim I.S.
      J. Leukoc. Biol. 83:438-438(2008)
    14. "Rapid cell corpse clearance by stabilin-2, a membrane phosphatidylserine receptor."
      Park S.Y., Jung M.Y., Kim H.J., Lee S.J., Kim S.Y., Lee B.H., Kwon T.H., Park R.W., Kim I.S.
      Cell Death Differ. 15:192-201(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TISSUE SPECIFICITY.
    15. "Thymosin beta4 is involved in stabilin-2-mediated apoptotic cell engulfment."
      Lee S.J., So I.S., Park S.Y., Kim I.S.
      FEBS Lett. 582:2161-2166(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TMSB4X.
    16. "Requirement of adaptor protein GULP during stabilin-2-mediated cell corpse engulfment."
      Park S.Y., Kang K.B., Thapa N., Kim S.Y., Lee S.J., Kim I.S.
      J. Biol. Chem. 283:10593-10600(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH GULP1.
    17. "The human hyaluronan receptor for endocytosis (HARE/Stabilin-2) is a systemic clearance receptor for heparin."
      Harris E.N., Weigel J.A., Weigel P.H.
      J. Biol. Chem. 283:17341-17350(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    18. "Epidermal growth factor-like domain repeat of stabilin-2 recognizes phosphatidylserine during cell corpse clearance."
      Park S.-Y., Kim S.-Y., Jung M.-Y., Bae D.-J., Kim I.-S.
      Mol. Cell. Biol. 28:5288-5298(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    19. "Rat and human HARE/stabilin-2 are clearance receptors for high- and low-molecular-weight heparins."
      Harris E.N., Baggenstoss B.A., Weigel P.H.
      Am. J. Physiol. 296:G1191-G1199(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    20. "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
      Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
      J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1743.
      Tissue: Liver.

    Entry informationi

    Entry nameiSTAB2_HUMAN
    AccessioniPrimary (citable) accession number: Q8WWQ8
    Secondary accession number(s): Q6ZMK2
    , Q7Z5N9, Q86UR4, Q8IUG9, Q8TES1, Q9H7H7, Q9NRY3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 19, 2004
    Last sequence update: April 17, 2007
    Last modified: October 1, 2014
    This is version 121 of the entry and version 3 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

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 12
      Human chromosome 12: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3