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Protein

Stabilin-2

Gene

STAB2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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

  • calcium ion binding Source: InterPro
  • hyaluronic acid binding Source: UniProtKB
  • low-density lipoprotein particle binding Source: UniProtKB
  • low-density lipoprotein receptor activity Source: UniProtKB
  • protein disulfide oxidoreductase activity Source: UniProtKB
  • scavenger receptor activity Source: UniProtKB

GO - Biological processi

  • angiogenesis Source: UniProtKB
  • cell adhesion Source: UniProtKB
  • defense response to bacterium Source: UniProtKB
  • endocytosis Source: UniProtKB
  • hyaluronan catabolic process Source: Reactome
  • receptor-mediated endocytosis Source: UniProtKB
  • regulation of blood coagulation Source: UniProtKB
  • regulation of gene expression Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Receptor

Keywords - Biological processi

Endocytosis

Keywords - Ligandi

Hyaluronic acid

Enzyme and pathway databases

BioCyciZFISH:ENSG00000136011-MONOMER.
ReactomeiR-HSA-2160916. Hyaluronan uptake and degradation.
R-HSA-3000497. 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
Proteomesi
  • UP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:18629. STAB2.

Subcellular locationi

  • Cell membrane 1 Publication; Single-pass type I membrane protein 1 Publication
  • Cytoplasm 1 Publication

  • Note: Only a small amount appears to be present at the cell surface (PubMed:17145755).

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini20 – 2458ExtracellularSequence analysisAdd BLAST2439
Transmembranei2459 – 2479HelicalSequence analysisAdd BLAST21
Topological domaini2480 – 2551CytoplasmicSequence analysisAdd BLAST72

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane

Pathology & Biotechi

Organism-specific databases

DisGeNETi55576.
OpenTargetsiENSG00000136011.
PharmGKBiPA38611.

Chemistry databases

DrugBankiDB08818. Hyaluronic acid.

Polymorphism and mutation databases

BioMutaiSTAB2.
DMDMi145559531.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 19Sequence analysisAdd BLAST19
ChainiPRO_000000771220 – 2551Stabilin-2Add BLAST2532
ChainiPRO_00000077131136 – 2551190 kDa form stabilin-2Add BLAST1416

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi112 ↔ 126By similarity
Disulfide bondi120 ↔ 136By similarity
Glycosylationi133N-linked (GlcNAc...)Sequence analysis1
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
Glycosylationi337N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi350 ↔ 361By similarity
Glycosylationi449N-linked (GlcNAc...)Sequence analysis1
Glycosylationi619N-linked (GlcNAc...)Sequence analysis1
Glycosylationi720N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi740 ↔ 754By similarity
Disulfide bondi748 ↔ 764By similarity
Glycosylationi761N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi766 ↔ 775By similarity
Disulfide bondi830 ↔ 843By similarity
Disulfide bondi837 ↔ 852By similarity
Glycosylationi847N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi854 ↔ 865By similarity
Disulfide bondi871 ↔ 885By similarity
Disulfide bondi879 ↔ 895By similarity
Disulfide bondi897 ↔ 908By similarity
Disulfide bondi914 ↔ 928By similarity
Disulfide bondi922 ↔ 938By similarity
Glycosylationi925N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi940 ↔ 951By similarity
Disulfide bondi957 ↔ 970By similarity
Disulfide bondi964 ↔ 980By similarity
Glycosylationi1016N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1028N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1100N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1247N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1275N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1348 ↔ 1362By similarity
Disulfide bondi1356 ↔ 1372By similarity
Glycosylationi1367N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1374 ↔ 1383By similarity
Disulfide bondi1395 ↔ 1406By similarity
Disulfide bondi1399 ↔ 1416By similarity
Disulfide bondi1418 ↔ 1427By similarity
Glycosylationi1429N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1436 ↔ 1446By similarity
Glycosylationi1437N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1440 ↔ 1456By similarity
Disulfide bondi1458 ↔ 1469By similarity
Glycosylationi1465N-linked (GlcNAc...)Sequence analysis1
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
Glycosylationi1573N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1679N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1743N-linked (GlcNAc...)1 Publication1
Disulfide bondi1962 ↔ 1976By similarity
Disulfide bondi1970 ↔ 1986By similarity
Disulfide bondi1988 ↔ 1997By similarity
Glycosylationi1993N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi2009 ↔ 2020By similarity
Disulfide bondi2014 ↔ 2030By similarity
Disulfide bondi2032 ↔ 2041By similarity
Disulfide bondi2051 ↔ 2061By similarity
Disulfide bondi2055 ↔ 2067By similarity
Glycosylationi2064N-linked (GlcNAc...)Sequence analysis1
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
Glycosylationi2280N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2296N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2336N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2368N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2382N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2393N-linked (GlcNAc...)Sequence analysis1
Modified residuei2497PhosphoserineCombined sources1

Post-translational modificationi

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

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiQ8WWQ8.
PeptideAtlasiQ8WWQ8.
PRIDEiQ8WWQ8.

PTM databases

iPTMnetiQ8WWQ8.
PhosphoSitePlusiQ8WWQ8.

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

BgeeiENSG00000136011.
CleanExiHS_STAB2.
ExpressionAtlasiQ8WWQ8. baseline and differential.
GenevisibleiQ8WWQ8. HS.

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. 5 interactors.
IntActiQ8WWQ8. 2 interactors.
MINTiMINT-6542238.
STRINGi9606.ENSP00000373539.

Structurei

3D structure databases

ProteinModelPortaliQ8WWQ8.
SMRiQ8WWQ8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini108 – 148EGF-like 1PROSITE-ProRule annotationAdd BLAST41
Domaini156 – 193EGF-like 2PROSITE-ProRule annotationAdd BLAST38
Domaini195 – 236EGF-like 3PROSITE-ProRule annotationAdd BLAST42
Domaini237 – 276EGF-like 4PROSITE-ProRule annotationAdd BLAST40
Domaini322 – 362EGF-like 5PROSITE-ProRule annotationAdd BLAST41
Domaini371 – 505FAS1 1PROSITE-ProRule annotationAdd BLAST135
Domaini515 – 652FAS1 2PROSITE-ProRule annotationAdd BLAST138
Domaini736 – 776EGF-like 6PROSITE-ProRule annotationAdd BLAST41
Domaini826 – 866EGF-like 7PROSITE-ProRule annotationAdd BLAST41
Domaini867 – 909EGF-like 8PROSITE-ProRule annotationAdd BLAST43
Domaini910 – 952EGF-like 9PROSITE-ProRule annotationAdd BLAST43
Domaini953 – 992EGF-like 10PROSITE-ProRule annotationAdd BLAST40
Domaini994 – 1127FAS1 3PROSITE-ProRule annotationAdd BLAST134
Domaini1137 – 1265FAS1 4PROSITE-ProRule annotationAdd BLAST129
Domaini1343 – 1408Laminin EGF-like 1Sequence analysisAdd BLAST66
Domaini1432 – 1470EGF-like 11PROSITE-ProRule annotationAdd BLAST39
Domaini1471 – 1512EGF-like 12PROSITE-ProRule annotationAdd BLAST42
Domaini1513 – 1554EGF-like 13PROSITE-ProRule annotationAdd BLAST42
Domaini1555 – 1594EGF-like 14PROSITE-ProRule annotationAdd BLAST40
Domaini1596 – 1724FAS1 5PROSITE-ProRule annotationAdd BLAST129
Domaini1740 – 1881FAS1 6PROSITE-ProRule annotationAdd BLAST142
Domaini1957 – 2022Laminin EGF-like 2Sequence analysisAdd BLAST66
Domaini2047 – 2081EGF-like 15PROSITE-ProRule annotationAdd BLAST35
Domaini2082 – 2122EGF-like 16PROSITE-ProRule annotationAdd BLAST41
Domaini2123 – 2165EGF-like 17PROSITE-ProRule annotationAdd BLAST43
Domaini2198 – 2291LinkPROSITE-ProRule annotationAdd BLAST94
Domaini2311 – 2446FAS1 7PROSITE-ProRule annotationAdd BLAST136

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni2504 – 2514Interaction with TMSB4X1 PublicationAdd BLAST11

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

eggNOGiENOG410IRWM. Eukaryota.
ENOG4110T5S. LUCA.
GeneTreeiENSGT00760000119025.
HOVERGENiHBG079218.
InParanoidiQ8WWQ8.
KOiK19013.
OMAiKCCKGFY.
OrthoDBiEOG091G002T.
PhylomeDBiQ8WWQ8.
TreeFamiTF331489.

Family and domain databases

Gene3Di2.30.180.10. 7 hits.
2.40.155.10. 9 hits.
3.10.100.10. 1 hit.
InterProiIPR016186. C-type_lectin-like/link.
IPR016187. CTDL_fold.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR024731. EGF_dom.
IPR000782. FAS1_domain.
IPR023413. GFP-like.
IPR002049. Laminin_EGF.
IPR000538. Link_dom.
[Graphical view]
PfamiPF12947. EGF_3. 7 hits.
PF02469. Fasciclin. 7 hits.
PF00193. Xlink. 1 hit.
[Graphical view]
SMARTiSM00181. EGF. 22 hits.
SM00179. EGF_CA. 8 hits.
SM00180. EGF_Lam. 5 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

« Hide

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

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti67G → R in BAD18723 (Ref. 5) Curated1
Sequence conflicti152D → A in BAD18723 (Ref. 5) Curated1
Sequence conflicti887K → N in BAD18723 (Ref. 5) Curated1
Sequence conflicti1136S → L AA sequence (PubMed:17145755).Curated1
Sequence conflicti1151S → P in CAC82105 (PubMed:11829752).Curated1
Sequence conflicti1276D → A in CAC82105 (PubMed:11829752).Curated1
Sequence conflicti1522G → C in BAD18723 (Ref. 5) Curated1
Sequence conflicti1557N → Y in AAO39681 (PubMed:12626425).Curated1
Sequence conflicti1599 – 1600IY → HE in AAF82398 (Ref. 7) Curated2
Sequence conflicti1854F → S in BAD18723 (Ref. 5) Curated1
Sequence conflicti2249L → V in BAD18723 (Ref. 5) Curated1
Sequence conflicti2253R → G in BAD18723 (Ref. 5) Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_048995110I → V.Corresponds to variant rs17034186dbSNPEnsembl.1
Natural variantiVAR_048996306E → K.Corresponds to variant rs12319476dbSNPEnsembl.1
Natural variantiVAR_019541510P → H.2 PublicationsCorresponds to variant rs1609860dbSNPEnsembl.1
Natural variantiVAR_048997787R → Q.Corresponds to variant rs17034336dbSNPEnsembl.1
Natural variantiVAR_048998881R → H.Corresponds to variant rs7973658dbSNPEnsembl.1
Natural variantiVAR_0489991736N → T.Corresponds to variant rs17034433dbSNPEnsembl.1
Natural variantiVAR_0490002039P → T.2 PublicationsCorresponds to variant rs7306642dbSNPEnsembl.1
Natural variantiVAR_0490012401L → V.2 PublicationsCorresponds to variant rs2271637dbSNPEnsembl.1
Natural variantiVAR_0490022519Y → S.Corresponds to variant rs3751197dbSNPEnsembl.1

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.4. human.

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.
CCDSiCCDS31888.1.
RefSeqiNP_060034.9. NM_017564.9.
UniGeneiHs.408249.

3D structure databases

ProteinModelPortaliQ8WWQ8.
SMRiQ8WWQ8.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi120727. 5 interactors.
IntActiQ8WWQ8. 2 interactors.
MINTiMINT-6542238.
STRINGi9606.ENSP00000373539.

Chemistry databases

DrugBankiDB08818. Hyaluronic acid.

PTM databases

iPTMnetiQ8WWQ8.
PhosphoSitePlusiQ8WWQ8.

Polymorphism and mutation databases

BioMutaiSTAB2.
DMDMi145559531.

Proteomic databases

PaxDbiQ8WWQ8.
PeptideAtlasiQ8WWQ8.
PRIDEiQ8WWQ8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000388887; ENSP00000373539; ENSG00000136011.
GeneIDi55576.
KEGGihsa:55576.
UCSCiuc001tjw.4. human.

Organism-specific databases

CTDi55576.
DisGeNETi55576.
GeneCardsiSTAB2.
HGNCiHGNC:18629. STAB2.
HPAiHPA026871.
MIMi608561. gene.
neXtProtiNX_Q8WWQ8.
OpenTargetsiENSG00000136011.
PharmGKBiPA38611.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IRWM. Eukaryota.
ENOG4110T5S. LUCA.
GeneTreeiENSGT00760000119025.
HOVERGENiHBG079218.
InParanoidiQ8WWQ8.
KOiK19013.
OMAiKCCKGFY.
OrthoDBiEOG091G002T.
PhylomeDBiQ8WWQ8.
TreeFamiTF331489.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000136011-MONOMER.
ReactomeiR-HSA-2160916. Hyaluronan uptake and degradation.
R-HSA-3000497. Scavenging by Class H Receptors.

Miscellaneous databases

ChiTaRSiSTAB2. human.
GeneWikiiSTAB2.
GenomeRNAii55576.
PROiQ8WWQ8.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000136011.
CleanExiHS_STAB2.
ExpressionAtlasiQ8WWQ8. baseline and differential.
GenevisibleiQ8WWQ8. HS.

Family and domain databases

Gene3Di2.30.180.10. 7 hits.
2.40.155.10. 9 hits.
3.10.100.10. 1 hit.
InterProiIPR016186. C-type_lectin-like/link.
IPR016187. CTDL_fold.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR024731. EGF_dom.
IPR000782. FAS1_domain.
IPR023413. GFP-like.
IPR002049. Laminin_EGF.
IPR000538. Link_dom.
[Graphical view]
PfamiPF12947. EGF_3. 7 hits.
PF02469. Fasciclin. 7 hits.
PF00193. Xlink. 1 hit.
[Graphical view]
SMARTiSM00181. EGF. 22 hits.
SM00179. EGF_CA. 8 hits.
SM00180. EGF_Lam. 5 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]
ProtoNetiSearch...

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 30, 2016
This is version 143 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.