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Q8WWQ8

- STAB2_HUMAN

UniProt

Q8WWQ8 - STAB2_HUMAN

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Protein

Stabilin-2

Gene

STAB2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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 disulfide oxidoreductase activity Source: UniProtKB
  5. 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
Complete GO annotation...

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.

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini20 – 24582439ExtracellularSequence AnalysisAdd
BLAST
Transmembranei2459 – 247921HelicalSequence AnalysisAdd
BLAST
Topological domaini2480 – 255172CytoplasmicSequence AnalysisAdd
BLAST

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
Complete GO annotation...

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...)1 Publication
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

BgeeiQ8WWQ8.
CleanExiHS_STAB2.
ExpressionAtlasiQ8WWQ8. baseline and differential.
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...

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.
GeneTreeiENSGT00730000110695.
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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        10         20         30         40         50
MMLQHLVIFC LGLVVQNFCS PAETTGQARR CDRKSLLTIR TECRSCALNL
60 70 80 90 100
GVKCPDGYTM ITSGSVGVRD CRYTFEVRTY SLSLPGCRHI CRKDYLQPRC
110 120 130 140 150
CPGRWGPDCI ECPGGAGSPC NGRGSCAEGM EGNGTCSCQE GFGGTACETC
160 170 180 190 200
ADDNLFGPSC SSVCNCVHGV CNSGLDGDGT CECYSAYTGP KCDKPIPECA
210 220 230 240 250
ALLCPENSRC SPSTEDENKL ECKCLPNYRG DGKYCDPINP CLRKICHPHA
260 270 280 290 300
HCTYLGPNRH SCTCQEGYRG DGQVCLPVDP CQINFGNCPT KSTVCKYDGP
310 320 330 340 350
GQSHCECKEH YQNFVPGVGC SMTDICKSDN PCHRNANCTT VAPGRTECIC
360 370 380 390 400
QKGYVGDGLT CYGNIMERLR ELNTEPRGKW QGRLTSFISL LDKAYAWPLS
410 420 430 440 450
KLGPFTVLLP TDKGLKGFNV NELLVDNKAA QYFVKLHIIA GQMNIEYMNN
460 470 480 490 500
TDMFYTLTGK SGEIFNSDKD NQIKLKLHGG KKKVKIIQGD IIASNGLLHI
510 520 530 540 550
LDRAMDKLEP TFESNNEQTI MTMLQPRYSK FRSLLEETNL GHALDEDGVG
560 570 580 590 600
GPYTIFVPNN EALNNMKDGT LDYLLSPEGS RKLLELVRYH IVPFTQLEVA
610 620 630 640 650
TLISTPHIRS MANQLIQFNT TDNGQILAND VAMEEIEITA KNGRIYTLTG
660 670 680 690 700
VLIPPSIVPI LPHRCDETKR EMKLGTCVSC SLVYWSRCPA NSEPTALFTH
710 720 730 740 750
RCVYSGRFGS LKSGCARYCN ATVKIPKCCK GFYGPDCNQC PGGFSNPCSG
760 770 780 790 800
NGQCADSLGG NGTCICEEGF QGSQCQFCSD PNKYGPRCNK KCLCVHGTCN
810 820 830 840 850
NRIDSDGACL TGTCRDGSAG RLCDKQTSAC GPYVQFCHIH ATCEYSNGTA
860 870 880 890 900
SCICKAGYEG DGTLCSEMDP CTGLTPGGCS RNAECIKTGT GTHTCVCQQG
910 920 930 940 950
WTGNGRDCSE INNCLLPSAG GCHDNASCLY VGPGQNECEC KKGFRGNGID
960 970 980 990 1000
CEPITSCLEQ TGKCHPLASC QSTSSGVWSC VCQEGYEGDG FLCYGNAAVE
1010 1020 1030 1040 1050
LSFLSEAAIF NRWINNASLQ PTLSATSNLT VLVPSQQATE DMDQDEKSFW
1060 1070 1080 1090 1100
LSQSNIPALI KYHMLLGTYR VADLQTLSSS DMLATSLQGN FLHLAKVDGN
1110 1120 1130 1140 1150
ITIEGASIVD GDNAATNGVI HIINKVLVPQ RRLTGSLPNL LMRLEQMPDY
1160 1170 1180 1190 1200
SIFRGYIIQY NLANAIEAAD AYTVFAPNNN AIENYIREKK VLSLEEDVLR
1210 1220 1230 1240 1250
YHVVLEEKLL KNDLHNGMHR ETMLGFSYFL SFFLHNDQLY VNEAPINYTN
1260 1270 1280 1290 1300
VATDKGVIHG LGKVLEIQKN RCDNNDTTII RGRCRTCSSE LTCPFGTKSL
1310 1320 1330 1340 1350
GNEKRRCIYT SYFMGRRTLF IGCQPKCVRT VITRECCAGF FGPQCQPCPG
1360 1370 1380 1390 1400
NAQNVCFGNG ICLDGVNGTG VCECGEGFSG TACETCTEGK YGIHCDQACS
1410 1420 1430 1440 1450
CVHGRCNQGP LGDGSCDCDV GWRGVHCDNA TTEDNCNGTC HTSANCLTNS
1460 1470 1480 1490 1500
DGTASCKCAA GFQGNGTICT AINACEISNG GCSAKADCKR TTPGRRVCTC
1510 1520 1530 1540 1550
KAGYTGDGIV CLEINPCLEN HGGCDKNAEC TQTGPNQAAC NCLPAYTGDG
1560 1570 1580 1590 1600
KVCTLINVCL TKNGGCSEFA ICNHTGQVER TCTCKPNYIG DGFTCRGSIY
1610 1620 1630 1640 1650
QELPKNPKTS QYFFQLQEHF VKDLVGPGPF TVFAPLSAAF DEEARVKDWD
1660 1670 1680 1690 1700
KYGLMPQVLR YHVVACHQLL LENLKLISNA TSLQGEPIVI SVSQSTVYIN
1710 1720 1730 1740 1750
NKAKIISSDI ISTNGIVHII DKLLSPKNLL ITPKDNSGRI LQNLTTLATN
1760 1770 1780 1790 1800
NGYIKFSNLI QDSGLLSVIT DPIHTPVTLF WPTDQALHAL PAEQQDFLFN
1810 1820 1830 1840 1850
QDNKDKLKEY LKFHVIRDAK VLAVDLPTST AWKTLQGSEL SVKCGAGRDI
1860 1870 1880 1890 1900
GDLFLNGQTC RIVQRELLFD LGVAYGIDCL LIDPTLGGRC DTFTTFDASG
1910 1920 1930 1940 1950
ECGSCVNTPS CPRWSKPKGV KQKCLYNLPF KRNLEGCRER CSLVIQIPRC
1960 1970 1980 1990 2000
CKGYFGRDCQ ACPGGPDAPC NNRGVCLDQY SATGECKCNT GFNGTACEMC
2010 2020 2030 2040 2050
WPGRFGPDCL PCGCSDHGQC DDGITGSGQC LCETGWTGPS CDTQAVLPAV
2060 2070 2080 2090 2100
CTPPCSAHAT CKENNTCECN LDYEGDGITC TVVDFCKQDN GGCAKVARCS
2110 2120 2130 2140 2150
QKGTKVSCSC QKGYKGDGHS CTEIDPCADG LNGGCHEHAT CKMTGPGKHK
2160 2170 2180 2190 2200
CECKSHYVGD GLNCEPEQLP IDRCLQDNGQ CHADAKCVDL HFQDTTVGVF
2210 2220 2230 2240 2250
HLRSPLGQYK LTFDKAREAC ANEAATMATY NQLSYAQKAK YHLCSAGWLE
2260 2270 2280 2290 2300
TGRVAYPTAF ASQNCGSGVV GIVDYGPRPN KSEMWDVFCY RMKDVNCTCK
2310 2320 2330 2340 2350
VGYVGDGFSC SGNLLQVLMS FPSLTNFLTE VLAYSNSSAR GRAFLEHLTD
2360 2370 2380 2390 2400
LSIRGTLFVP QNSGLGENET LSGRDIEHHL ANVSMFFYND LVNGTTLQTR
2410 2420 2430 2440 2450
LGSKLLITAS QDPLQPTETR FVDGRAILQW DIFASNGIIH VISRPLKAPP
2460 2470 2480 2490 2500
APVTLTHTGL GAGIFFAIIL VTGAVALAAY SYFRINRRTI GFQHFESEED
2510 2520 2530 2540 2550
INVAALGKQQ PENISNPLYE STTSAPPEPS YDPFTDSEER QLEGNDPLRT

L
Length:2,551
Mass (Da):276,988
Last modified:April 17, 2007 - v3
Checksum:i3ACB6A6C3CB80044
GO

Sequence cautioni

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

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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

Chemistry

DrugBanki DB08818. Hyaluronan.

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.
GeneTreei ENSGT00730000110695.
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

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

Gene expression databases

Bgeei Q8WWQ8.
CleanExi HS_STAB2.
ExpressionAtlasi Q8WWQ8. baseline and differential.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 123 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