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Q8WWQ8 (STAB2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 116. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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:

  1. 190 kDa form stabilin-2
    Alternative name(s):
    190 kDa hyaluronan receptor for endocytosis
Gene names
Name:STAB2
Synonyms:FEEL2, FELL, FEX2, HARE
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length2551 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.2 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.14 Ref.16 Ref.17 Ref.18 Ref.19

Subunit structure

Interacts with GULP1 and heparin. Also interacts with alpha-M/beta-2 integrin (ITGAM and ITGB2) and thymosin beta 4 (TMSB4X and/or TMSB4Y). Ref.12 Ref.15 Ref.16

Subcellular location

Cell membrane; Single-pass type I membrane protein. Cytoplasm. Note: Only a small amount appears to be present at the cell surface. Ref.8 Ref.12

Tissue specificity

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. Ref.1 Ref.2 Ref.6 Ref.9 Ref.12 Ref.14

Domain

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

Post-translational modification

Glycosylated. Ref.8

Proteolytically processed to yield a 190 kDa protein. Ref.6

Sequence similarities

Contains 17 EGF-like domains.

Contains 7 FAS1 domains.

Contains 2 laminin EGF-like domains.

Contains 1 Link domain.

Sequence caution

The sequence AAF82398.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence BAD18723.1 differs from that shown. Reason: Frameshift at positions 240, 253, 588 and 1586.

Ontologies

Keywords
   Biological processEndocytosis
   Cellular componentCell membrane
Cytoplasm
Membrane
   Coding sequence diversityPolymorphism
   DomainEGF-like domain
Laminin EGF-like domain
Repeat
Signal
Transmembrane
Transmembrane helix
   LigandHyaluronic acid
   Molecular functionReceptor
   PTMDisulfide bond
Glycoprotein
Phosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processangiogenesis

Non-traceable author statement Ref.2. Source: UniProtKB

carbohydrate metabolic process

Traceable author statement. Source: Reactome

cell adhesion

Non-traceable author statement Ref.2. Source: UniProtKB

defense response to bacterium

Inferred from direct assay Ref.2. Source: UniProtKB

endocytosis

Inferred from sequence or structural similarity. Source: UniProtKB

glycosaminoglycan metabolic process

Traceable author statement. Source: Reactome

hyaluronan catabolic process

Traceable author statement. Source: Reactome

hyaluronan metabolic process

Traceable author statement. Source: Reactome

oxidation-reduction process

Non-traceable author statement Ref.2. Source: GOC

receptor-mediated endocytosis

Traceable author statement Ref.2. Source: UniProtKB

small molecule metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentcytoplasm

Inferred from direct assay. Source: HPA

endocytic vesicle membrane

Traceable author statement. Source: Reactome

external side of plasma membrane

Inferred from sequence or structural similarity. Source: UniProtKB

integral component of plasma membrane

Inferred from direct assay Ref.2. Source: UniProtKB

plasma membrane

Traceable author statement. Source: Reactome

   Molecular_functionhyaluronic acid binding

Inferred from sequence or structural similarity. Source: UniProtKB

low-density lipoprotein particle binding

Inferred from direct assay Ref.2. Source: UniProtKB

low-density lipoprotein receptor activity

Inferred from direct assay Ref.2. Source: UniProtKB

protein disulfide oxidoreductase activity

Non-traceable author statement Ref.2. Source: UniProtKB

scavenger receptor activity

Inferred from direct assay Ref.2. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Tmsb4xP200653EBI-7945957,EBI-7946048From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Potential
Chain20 – 25512532Stabilin-2
PRO_0000007712
Chain1136 – 25511416190 kDa form stabilin-2 Ref.6
PRO_0000007713

Regions

Topological domain20 – 24582439Extracellular Potential
Transmembrane2459 – 247921Helical; Potential
Topological domain2480 – 255172Cytoplasmic Potential
Domain108 – 14841EGF-like 1
Domain156 – 19338EGF-like 2
Domain195 – 23642EGF-like 3
Domain237 – 27640EGF-like 4
Domain322 – 36241EGF-like 5
Domain371 – 505135FAS1 1
Domain515 – 652138FAS1 2
Domain736 – 77641EGF-like 6
Domain826 – 86641EGF-like 7
Domain867 – 90943EGF-like 8
Domain910 – 95243EGF-like 9
Domain953 – 99240EGF-like 10
Domain994 – 1127134FAS1 3
Domain1137 – 1265129FAS1 4
Domain1343 – 140866Laminin EGF-like 1
Domain1432 – 147039EGF-like 11
Domain1471 – 151242EGF-like 12
Domain1513 – 155442EGF-like 13
Domain1555 – 159440EGF-like 14
Domain1596 – 1724129FAS1 5
Domain1740 – 1881142FAS1 6
Domain1957 – 202266Laminin EGF-like 2
Domain2047 – 208135EGF-like 15
Domain2082 – 212241EGF-like 16
Domain2123 – 216543EGF-like 17
Domain2198 – 229194Link
Domain2311 – 2446136FAS1 7
Region2504 – 251411Interaction with TMSB4X

Amino acid modifications

Modified residue24971Phosphoserine By similarity
Glycosylation1331N-linked (GlcNAc...) Potential
Glycosylation3371N-linked (GlcNAc...) Potential
Glycosylation4491N-linked (GlcNAc...) Potential
Glycosylation6191N-linked (GlcNAc...) Potential
Glycosylation7201N-linked (GlcNAc...) Potential
Glycosylation7611N-linked (GlcNAc...) Potential
Glycosylation8471N-linked (GlcNAc...) Potential
Glycosylation9251N-linked (GlcNAc...) Potential
Glycosylation10161N-linked (GlcNAc...) Potential
Glycosylation10281N-linked (GlcNAc...) Potential
Glycosylation11001N-linked (GlcNAc...) Potential
Glycosylation12471N-linked (GlcNAc...) Potential
Glycosylation12751N-linked (GlcNAc...) Potential
Glycosylation13671N-linked (GlcNAc...) Potential
Glycosylation14291N-linked (GlcNAc...) Potential
Glycosylation14371N-linked (GlcNAc...) Potential
Glycosylation14651N-linked (GlcNAc...) Potential
Glycosylation15731N-linked (GlcNAc...) Potential
Glycosylation16791N-linked (GlcNAc...) Potential
Glycosylation17431N-linked (GlcNAc...) Ref.20
Glycosylation19931N-linked (GlcNAc...) Potential
Glycosylation20641N-linked (GlcNAc...) Potential
Glycosylation22801N-linked (GlcNAc...) Potential
Glycosylation22961N-linked (GlcNAc...) Potential
Glycosylation23361N-linked (GlcNAc...) Potential
Glycosylation23681N-linked (GlcNAc...) Potential
Glycosylation23821N-linked (GlcNAc...) Potential
Glycosylation23931N-linked (GlcNAc...) Potential
Disulfide bond112 ↔ 126 By similarity
Disulfide bond120 ↔ 136 By similarity
Disulfide bond138 ↔ 147 By similarity
Disulfide bond160 ↔ 171 By similarity
Disulfide bond164 ↔ 181 By similarity
Disulfide bond183 ↔ 192 By similarity
Disulfide bond199 ↔ 210 By similarity
Disulfide bond204 ↔ 222 By similarity
Disulfide bond224 ↔ 235 By similarity
Disulfide bond241 ↔ 252 By similarity
Disulfide bond246 ↔ 262 By similarity
Disulfide bond264 ↔ 275 By similarity
Disulfide bond326 ↔ 338 By similarity
Disulfide bond332 ↔ 348 By similarity
Disulfide bond350 ↔ 361 By similarity
Disulfide bond740 ↔ 754 By similarity
Disulfide bond748 ↔ 764 By similarity
Disulfide bond766 ↔ 775 By similarity
Disulfide bond830 ↔ 843 By similarity
Disulfide bond837 ↔ 852 By similarity
Disulfide bond854 ↔ 865 By similarity
Disulfide bond871 ↔ 885 By similarity
Disulfide bond879 ↔ 895 By similarity
Disulfide bond897 ↔ 908 By similarity
Disulfide bond914 ↔ 928 By similarity
Disulfide bond922 ↔ 938 By similarity
Disulfide bond940 ↔ 951 By similarity
Disulfide bond957 ↔ 970 By similarity
Disulfide bond964 ↔ 980 By similarity
Disulfide bond1348 ↔ 1362 By similarity
Disulfide bond1356 ↔ 1372 By similarity
Disulfide bond1374 ↔ 1383 By similarity
Disulfide bond1395 ↔ 1406 By similarity
Disulfide bond1399 ↔ 1416 By similarity
Disulfide bond1418 ↔ 1427 By similarity
Disulfide bond1436 ↔ 1446 By similarity
Disulfide bond1440 ↔ 1456 By similarity
Disulfide bond1458 ↔ 1469 By similarity
Disulfide bond1475 ↔ 1488 By similarity
Disulfide bond1482 ↔ 1498 By similarity
Disulfide bond1500 ↔ 1511 By similarity
Disulfide bond1517 ↔ 1530 By similarity
Disulfide bond1524 ↔ 1540 By similarity
Disulfide bond1542 ↔ 1553 By similarity
Disulfide bond1559 ↔ 1572 By similarity
Disulfide bond1566 ↔ 1582 By similarity
Disulfide bond1962 ↔ 1976 By similarity
Disulfide bond1970 ↔ 1986 By similarity
Disulfide bond1988 ↔ 1997 By similarity
Disulfide bond2009 ↔ 2020 By similarity
Disulfide bond2014 ↔ 2030 By similarity
Disulfide bond2032 ↔ 2041 By similarity
Disulfide bond2051 ↔ 2061 By similarity
Disulfide bond2055 ↔ 2067 By similarity
Disulfide bond2069 ↔ 2080 By similarity
Disulfide bond2086 ↔ 2099 By similarity
Disulfide bond2093 ↔ 2108 By similarity
Disulfide bond2110 ↔ 2121 By similarity
Disulfide bond2127 ↔ 2141 By similarity
Disulfide bond2135 ↔ 2151 By similarity
Disulfide bond2153 ↔ 2164 By similarity
Disulfide bond2220 ↔ 2289 By similarity
Disulfide bond2244 ↔ 2265 By similarity

Natural variations

Natural variant1101I → V.
Corresponds to variant rs17034186 [ dbSNP | Ensembl ].
VAR_048995
Natural variant3061E → K.
Corresponds to variant rs12319476 [ dbSNP | Ensembl ].
VAR_048996
Natural variant5101P → H. Ref.1 Ref.2
Corresponds to variant rs1609860 [ dbSNP | Ensembl ].
VAR_019541
Natural variant7871R → Q.
Corresponds to variant rs17034336 [ dbSNP | Ensembl ].
VAR_048997
Natural variant8811R → H.
Corresponds to variant rs7973658 [ dbSNP | Ensembl ].
VAR_048998
Natural variant17361N → T.
Corresponds to variant rs17034433 [ dbSNP | Ensembl ].
VAR_048999
Natural variant20391P → T. Ref.4 Ref.5
Corresponds to variant rs7306642 [ dbSNP | Ensembl ].
VAR_049000
Natural variant24011L → V. Ref.5 Ref.7
Corresponds to variant rs2271637 [ dbSNP | Ensembl ].
VAR_049001
Natural variant25191Y → S.
Corresponds to variant rs3751197 [ dbSNP | Ensembl ].
VAR_049002

Experimental info

Sequence conflict671G → R in BAD18723. Ref.5
Sequence conflict1521D → A in BAD18723. Ref.5
Sequence conflict8871K → N in BAD18723. Ref.5
Sequence conflict11361S → L AA sequence Ref.8
Sequence conflict11511S → P in CAC82105. Ref.1
Sequence conflict12761D → A in CAC82105. Ref.1
Sequence conflict15221G → C in BAD18723. Ref.5
Sequence conflict15571N → Y in AAO39681. Ref.6
Sequence conflict1599 – 16002IY → HE in AAF82398. Ref.7
Sequence conflict18541F → S in BAD18723. Ref.5
Sequence conflict22491L → V in BAD18723. Ref.5
Sequence conflict22531R → G in BAD18723. Ref.5

Sequences

Sequence LengthMass (Da)Tools
Q8WWQ8 [UniParc].

Last modified April 17, 2007. Version 3.
Checksum: 3ACB6A6C3CB80044

FASTA2,551276,988
        10         20         30         40         50         60 
MMLQHLVIFC LGLVVQNFCS PAETTGQARR CDRKSLLTIR TECRSCALNL GVKCPDGYTM 

        70         80         90        100        110        120 
ITSGSVGVRD CRYTFEVRTY SLSLPGCRHI CRKDYLQPRC CPGRWGPDCI ECPGGAGSPC 

       130        140        150        160        170        180 
NGRGSCAEGM EGNGTCSCQE GFGGTACETC ADDNLFGPSC SSVCNCVHGV CNSGLDGDGT 

       190        200        210        220        230        240 
CECYSAYTGP KCDKPIPECA ALLCPENSRC SPSTEDENKL ECKCLPNYRG DGKYCDPINP 

       250        260        270        280        290        300 
CLRKICHPHA HCTYLGPNRH SCTCQEGYRG DGQVCLPVDP CQINFGNCPT KSTVCKYDGP 

       310        320        330        340        350        360 
GQSHCECKEH YQNFVPGVGC SMTDICKSDN PCHRNANCTT VAPGRTECIC QKGYVGDGLT 

       370        380        390        400        410        420 
CYGNIMERLR ELNTEPRGKW QGRLTSFISL LDKAYAWPLS KLGPFTVLLP TDKGLKGFNV 

       430        440        450        460        470        480 
NELLVDNKAA QYFVKLHIIA GQMNIEYMNN TDMFYTLTGK SGEIFNSDKD NQIKLKLHGG 

       490        500        510        520        530        540 
KKKVKIIQGD IIASNGLLHI LDRAMDKLEP TFESNNEQTI MTMLQPRYSK FRSLLEETNL 

       550        560        570        580        590        600 
GHALDEDGVG GPYTIFVPNN EALNNMKDGT LDYLLSPEGS RKLLELVRYH IVPFTQLEVA 

       610        620        630        640        650        660 
TLISTPHIRS MANQLIQFNT TDNGQILAND VAMEEIEITA KNGRIYTLTG VLIPPSIVPI 

       670        680        690        700        710        720 
LPHRCDETKR EMKLGTCVSC SLVYWSRCPA NSEPTALFTH RCVYSGRFGS LKSGCARYCN 

       730        740        750        760        770        780 
ATVKIPKCCK GFYGPDCNQC PGGFSNPCSG NGQCADSLGG NGTCICEEGF QGSQCQFCSD 

       790        800        810        820        830        840 
PNKYGPRCNK KCLCVHGTCN NRIDSDGACL TGTCRDGSAG RLCDKQTSAC GPYVQFCHIH 

       850        860        870        880        890        900 
ATCEYSNGTA SCICKAGYEG DGTLCSEMDP CTGLTPGGCS RNAECIKTGT GTHTCVCQQG 

       910        920        930        940        950        960 
WTGNGRDCSE INNCLLPSAG GCHDNASCLY VGPGQNECEC KKGFRGNGID CEPITSCLEQ 

       970        980        990       1000       1010       1020 
TGKCHPLASC QSTSSGVWSC VCQEGYEGDG FLCYGNAAVE LSFLSEAAIF NRWINNASLQ 

      1030       1040       1050       1060       1070       1080 
PTLSATSNLT VLVPSQQATE DMDQDEKSFW LSQSNIPALI KYHMLLGTYR VADLQTLSSS 

      1090       1100       1110       1120       1130       1140 
DMLATSLQGN FLHLAKVDGN ITIEGASIVD GDNAATNGVI HIINKVLVPQ RRLTGSLPNL 

      1150       1160       1170       1180       1190       1200 
LMRLEQMPDY SIFRGYIIQY NLANAIEAAD AYTVFAPNNN AIENYIREKK VLSLEEDVLR 

      1210       1220       1230       1240       1250       1260 
YHVVLEEKLL KNDLHNGMHR ETMLGFSYFL SFFLHNDQLY VNEAPINYTN VATDKGVIHG 

      1270       1280       1290       1300       1310       1320 
LGKVLEIQKN RCDNNDTTII RGRCRTCSSE LTCPFGTKSL GNEKRRCIYT SYFMGRRTLF 

      1330       1340       1350       1360       1370       1380 
IGCQPKCVRT VITRECCAGF FGPQCQPCPG NAQNVCFGNG ICLDGVNGTG VCECGEGFSG 

      1390       1400       1410       1420       1430       1440 
TACETCTEGK YGIHCDQACS CVHGRCNQGP LGDGSCDCDV GWRGVHCDNA TTEDNCNGTC 

      1450       1460       1470       1480       1490       1500 
HTSANCLTNS DGTASCKCAA GFQGNGTICT AINACEISNG GCSAKADCKR TTPGRRVCTC 

      1510       1520       1530       1540       1550       1560 
KAGYTGDGIV CLEINPCLEN HGGCDKNAEC TQTGPNQAAC NCLPAYTGDG KVCTLINVCL 

      1570       1580       1590       1600       1610       1620 
TKNGGCSEFA ICNHTGQVER TCTCKPNYIG DGFTCRGSIY QELPKNPKTS QYFFQLQEHF 

      1630       1640       1650       1660       1670       1680 
VKDLVGPGPF TVFAPLSAAF DEEARVKDWD KYGLMPQVLR YHVVACHQLL LENLKLISNA 

      1690       1700       1710       1720       1730       1740 
TSLQGEPIVI SVSQSTVYIN NKAKIISSDI ISTNGIVHII DKLLSPKNLL ITPKDNSGRI 

      1750       1760       1770       1780       1790       1800 
LQNLTTLATN NGYIKFSNLI QDSGLLSVIT DPIHTPVTLF WPTDQALHAL PAEQQDFLFN 

      1810       1820       1830       1840       1850       1860 
QDNKDKLKEY LKFHVIRDAK VLAVDLPTST AWKTLQGSEL SVKCGAGRDI GDLFLNGQTC 

      1870       1880       1890       1900       1910       1920 
RIVQRELLFD LGVAYGIDCL LIDPTLGGRC DTFTTFDASG ECGSCVNTPS CPRWSKPKGV 

      1930       1940       1950       1960       1970       1980 
KQKCLYNLPF KRNLEGCRER CSLVIQIPRC CKGYFGRDCQ ACPGGPDAPC NNRGVCLDQY 

      1990       2000       2010       2020       2030       2040 
SATGECKCNT GFNGTACEMC WPGRFGPDCL PCGCSDHGQC DDGITGSGQC LCETGWTGPS 

      2050       2060       2070       2080       2090       2100 
CDTQAVLPAV CTPPCSAHAT CKENNTCECN LDYEGDGITC TVVDFCKQDN GGCAKVARCS 

      2110       2120       2130       2140       2150       2160 
QKGTKVSCSC QKGYKGDGHS CTEIDPCADG LNGGCHEHAT CKMTGPGKHK CECKSHYVGD 

      2170       2180       2190       2200       2210       2220 
GLNCEPEQLP IDRCLQDNGQ CHADAKCVDL HFQDTTVGVF HLRSPLGQYK LTFDKAREAC 

      2230       2240       2250       2260       2270       2280 
ANEAATMATY NQLSYAQKAK YHLCSAGWLE TGRVAYPTAF ASQNCGSGVV GIVDYGPRPN 

      2290       2300       2310       2320       2330       2340 
KSEMWDVFCY RMKDVNCTCK VGYVGDGFSC SGNLLQVLMS FPSLTNFLTE VLAYSNSSAR 

      2350       2360       2370       2380       2390       2400 
GRAFLEHLTD LSIRGTLFVP QNSGLGENET LSGRDIEHHL ANVSMFFYND LVNGTTLQTR 

      2410       2420       2430       2440       2450       2460 
LGSKLLITAS QDPLQPTETR FVDGRAILQW DIFASNGIIH VISRPLKAPP APVTLTHTGL 

      2470       2480       2490       2500       2510       2520 
GAGIFFAIIL VTGAVALAAY SYFRINRRTI GFQHFESEED INVAALGKQQ PENISNPLYE 

      2530       2540       2550 
STTSAPPEPS YDPFTDSEER QLEGNDPLRT L 

« Hide

References

« Hide 'large scale' references
[1]"Stabilin-1 and -2 constitute a novel family of fasciclin-like hyaluronan receptor homologues."
Politz O., Gratchev A., McCourt P.A.G., Schledzewski K., Guillot P., Johansson S., Svineng G., Franke P., Kannicht C., Kzhyshkowska J., Longati P., Velten F.W., Johansson S., Goerdt S.
Biochem. J. 362:155-164(2002) [PubMed] [Europe PMC] [Abstract]
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. 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] OF 35-2551, VARIANT THR-2039.
Tissue: Spleen.
[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]"FEEL-1 and FEEL-2 are endocytic receptors for advanced glycation end products."
Tamura Y., Adachi H., Osuga J., Ohashi K., Yahagi N., Sekiya M., Okazaki H., Tomita S., Iizuka Y., Shimano H., Nagai R., Kimura S., Tsujimoto M., Ishibashi S.
J. Biol. Chem. 278:12613-12617(2003) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_060034.9. NM_017564.9.
UniGeneHs.408249.

3D structure databases

ProteinModelPortalQ8WWQ8.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid120727. 7 interactions.
IntActQ8WWQ8. 2 interactions.
MINTMINT-6542238.
STRING9606.ENSP00000373539.

PTM databases

PhosphoSiteQ8WWQ8.

Polymorphism databases

DMDM145559531.

Proteomic databases

PaxDbQ8WWQ8.
PRIDEQ8WWQ8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000388887; ENSP00000373539; ENSG00000136011.
GeneID55576.
KEGGhsa:55576.
UCSCuc001tjw.3. human.

Organism-specific databases

CTD55576.
GeneCardsGC12P103981.
HGNCHGNC:18629. STAB2.
HPAHPA026871.
MIM608561. gene.
neXtProtNX_Q8WWQ8.
PharmGKBPA38611.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG2335.
HOVERGENHBG079218.
InParanoidQ8WWQ8.
OMAIPKCCKG.
OrthoDBEOG7PS1DH.
PhylomeDBQ8WWQ8.
TreeFamTF331489.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.
REACT_116125. Disease.
REACT_160300. Binding and Uptake of Ligands by Scavenger Receptors.

Gene expression databases

ArrayExpressQ8WWQ8.
BgeeQ8WWQ8.
CleanExHS_STAB2.
GenevestigatorQ8WWQ8.

Family and domain databases

Gene3D2.30.180.10. 7 hits.
2.40.155.10. 8 hits.
3.10.100.10. 1 hit.
InterProIPR016186. 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]
PfamPF12947. EGF_3. 7 hits.
PF02469. Fasciclin. 7 hits.
PF00193. Xlink. 1 hit.
[Graphical view]
SMARTSM00181. EGF. 20 hits.
SM00554. FAS1. 7 hits.
SM00445. LINK. 1 hit.
[Graphical view]
SUPFAMSSF56436. SSF56436. 1 hit.
SSF82153. SSF82153. 7 hits.
PROSITEPS00022. 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]
ProtoNetSearch...

Other

GeneWikiSTAB2.
GenomeRNAi55576.
NextBio60076.
PROQ8WWQ8.
SOURCESearch...

Entry information

Entry nameSTAB2_HUMAN
AccessionPrimary (citable) accession number: Q8WWQ8
Secondary accession number(s): Q6ZMK2 expand/collapse secondary AC list , Q7Z5N9, Q86UR4, Q8IUG9, Q8TES1, Q9H7H7, Q9NRY3
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: April 17, 2007
Last modified: April 16, 2014
This is version 116 of the entry and version 3 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

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM