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Q9NY15

- STAB1_HUMAN

UniProt

Q9NY15 - STAB1_HUMAN

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Protein

Stabilin-1

Gene

STAB1

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

Functioni

Acts as a scavenger receptor for acetylated low density lipoprotein. Binds to both Gram-positive and Gram-negative bacteria and may play a role in defense against bacterial infection. When inhibited in endothelial tube formation assays, there is a marked decrease in cell-cell interactions, suggesting a role in angiogenesis. Involved in the delivery of newly synthesized CHID1/SI-CLP from the biosynthetic compartment to the endosomal/lysosomal system.2 Publications

GO - Molecular functioni

  1. hyaluronic acid binding Source: InterPro
  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. cell adhesion Source: UniProtKB
  2. cell-cell signaling Source: UniProtKB
  3. defense response to bacterium Source: UniProtKB
  4. inflammatory response Source: UniProtKB-KW
  5. negative regulation of angiogenesis Source: UniProtKB
  6. oxidation-reduction process Source: GOC
  7. receptor-mediated endocytosis Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Receptor

Keywords - Biological processi

Inflammatory response

Enzyme and pathway databases

ReactomeiREACT_164002. Scavenging by Class H Receptors.

Names & Taxonomyi

Protein namesi
Recommended name:
Stabilin-1
Alternative name(s):
Fasciclin, EGF-like, laminin-type EGF-like and link domain-containing scavenger receptor 1
Short name:
FEEL-1
MS-1 antigen
Gene namesi
Name:STAB1
Synonyms:FEEL1, KIAA0246
OrganismiHomo sapiens (Human)Imported
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 3

Organism-specific databases

HGNCiHGNC:18628. STAB1.

Subcellular locationi

GO - Cellular componenti

  1. endocytic vesicle membrane Source: Reactome
  2. integral component of plasma membrane Source: UniProtKB
  3. plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA38610.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2525Sequence AnalysisAdd
BLAST
Chaini26 – 25702545Stabilin-1PRO_0000007710Add
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 ↔ 217By similarity
Disulfide bondi236 ↔ 247By similarity
Disulfide bondi241 ↔ 257By similarity
Disulfide bondi259 ↔ 270By similarity
Glycosylationi286 – 2861N-linked (GlcNAc...)Sequence Analysis
Glycosylationi312 – 3121N-linked (GlcNAc...)Sequence Analysis
Glycosylationi413 – 4131N-linked (GlcNAc...)Sequence Analysis
Glycosylationi606 – 6061N-linked (GlcNAc...)Sequence Analysis
Glycosylationi673 – 6731N-linked (GlcNAc...)Sequence Analysis
Glycosylationi712 – 7121N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi732 ↔ 746By similarity
Disulfide bondi740 ↔ 756By similarity
Glycosylationi745 – 7451N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi758 ↔ 767By similarity
Glycosylationi816 – 8161N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi822 ↔ 837By similarity
Disulfide bondi831 ↔ 846By similarity
Disulfide bondi865 ↔ 879By similarity
Disulfide bondi873 ↔ 889By similarity
Disulfide bondi891 ↔ 902By similarity
Disulfide bondi908 ↔ 922By similarity
Disulfide bondi916 ↔ 932By similarity
Disulfide bondi934 ↔ 945By similarity
Disulfide bondi951 ↔ 964By similarity
Disulfide bondi958 ↔ 974By similarity
Glycosylationi1087 – 10871N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1096 – 10961N-linked (GlcNAc...)1 Publication
Glycosylationi1170 – 11701N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1178 – 11781N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1222 – 12221N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1274 – 12741N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi1332 ↔ 1346By similarity
Disulfide bondi1340 ↔ 1356By similarity
Disulfide bondi1358 ↔ 1367By similarity
Glycosylationi1378 – 13781N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi1379 ↔ 1390By similarity
Disulfide bondi1383 ↔ 1400By similarity
Disulfide bondi1402 ↔ 1411By similarity
Disulfide bondi1420 ↔ 1430By similarity
Disulfide bondi1424 ↔ 1440By similarity
Disulfide bondi1442 ↔ 1453By similarity
Disulfide bondi1459 ↔ 1472By similarity
Disulfide bondi1466 ↔ 1482By similarity
Glycosylationi1471 – 14711N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi1484 ↔ 1495By similarity
Disulfide bondi1501 ↔ 1514By similarity
Disulfide bondi1508 ↔ 1524By similarity
Disulfide bondi1526 ↔ 1538By similarity
Disulfide bondi1544 ↔ 1557By similarity
Disulfide bondi1551 ↔ 1567By similarity
Disulfide bondi1569 ↔ 1581By similarity
Glycosylationi1626 – 16261N-linked (GlcNAc...)1 Publication
Glycosylationi1727 – 17271N-linked (GlcNAc...)1 Publication
Disulfide bondi1971 ↔ 1985By similarity
Disulfide bondi1979 ↔ 1995By similarity
Disulfide bondi1997 ↔ 2006By similarity
Disulfide bondi2018 ↔ 2029By similarity
Disulfide bondi2023 ↔ 2039By similarity
Disulfide bondi2041 ↔ 2050By similarity
Disulfide bondi2060 ↔ 2070By similarity
Disulfide bondi2064 ↔ 2076By similarity
Disulfide bondi2078 ↔ 2089By similarity
Disulfide bondi2095 ↔ 2108By similarity
Disulfide bondi2102 ↔ 2117By similarity
Glycosylationi2107 – 21071N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi2119 ↔ 2130By similarity
Disulfide bondi2136 ↔ 2150By similarity
Disulfide bondi2144 ↔ 2160By similarity
Disulfide bondi2162 ↔ 2173By similarity
Glycosylationi2222 – 22221N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi2230 ↔ 2299By similarity
Disulfide bondi2254 ↔ 2275By similarity
Glycosylationi2261 – 22611N-linked (GlcNAc...)Sequence Analysis
Glycosylationi2290 – 22901N-linked (GlcNAc...)Sequence Analysis
Glycosylationi2334 – 23341N-linked (GlcNAc...)Sequence Analysis
Glycosylationi2347 – 23471N-linked (GlcNAc...)1 Publication
Glycosylationi2379 – 23791N-linked (GlcNAc...)Sequence Analysis
Glycosylationi2393 – 23931N-linked (GlcNAc...)Sequence Analysis
Glycosylationi2400 – 24001N-linked (GlcNAc...)Sequence Analysis
Glycosylationi2424 – 24241N-linked (GlcNAc...)1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ9NY15.
PRIDEiQ9NY15.

PTM databases

PhosphoSiteiQ9NY15.

Expressioni

Tissue specificityi

High levels found in spleen, lymph node, liver and placenta. Also expressed in endothelial cells.2 Publications

Gene expression databases

BgeeiQ9NY15.
CleanExiHS_STAB1.
GenevestigatoriQ9NY15.

Organism-specific databases

HPAiHPA005434.

Interactioni

Subunit structurei

Interacts with CHID1.1 Publication

Protein-protein interaction databases

BioGridi116778. 5 interactions.
IntActiQ9NY15. 71 interactions.
MINTiMINT-4831401.
STRINGi9606.ENSP00000312946.

Structurei

3D structure databases

ProteinModelPortaliQ9NY15.
SMRiQ9NY15. Positions 29-350, 518-643, 736-983, 1340-1575, 1939-2300.
ModBaseiSearch...
MobiDBiSearch...

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini26 – 24782453ExtracellularSequence AnalysisAdd
BLAST
Topological domaini2500 – 257071CytoplasmicSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei2479 – 249921HelicalSequence AnalysisAdd
BLAST

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini110 – 14839EGF-like 1CuratedPROSITE-ProRule annotationAdd
BLAST
Domaini156 – 19338EGF-like 2CuratedPROSITE-ProRule annotationAdd
BLAST
Domaini195 – 22935EGF-like 3CuratedPROSITE-ProRule annotationAdd
BLAST
Domaini232 – 27140EGF-like 4CuratedPROSITE-ProRule annotationAdd
BLAST
Domaini356 – 494139FAS1 1CuratedPROSITE-ProRule annotationAdd
BLAST
Domaini506 – 641136FAS1 2CuratedPROSITE-ProRule annotationAdd
BLAST
Domaini728 – 76841EGF-like 5CuratedPROSITE-ProRule annotationAdd
BLAST
Domaini818 – 85841EGF-like 6CuratedPROSITE-ProRule annotationAdd
BLAST
Domaini861 – 90343EGF-like 7CuratedPROSITE-ProRule annotationAdd
BLAST
Domaini904 – 94643EGF-like 8CuratedPROSITE-ProRule annotationAdd
BLAST
Domaini947 – 98640EGF-like 9CuratedPROSITE-ProRule annotationAdd
BLAST
Domaini988 – 1118131FAS1 3CuratedPROSITE-ProRule annotationAdd
BLAST
Domaini1128 – 1253126FAS1 4CuratedPROSITE-ProRule annotationAdd
BLAST
Domaini1327 – 139266Laminin EGF-like 1CuratedAdd
BLAST
Domaini1416 – 145439EGF-like 10CuratedPROSITE-ProRule annotationAdd
BLAST
Domaini1455 – 149642EGF-like 11CuratedPROSITE-ProRule annotationAdd
BLAST
Domaini1497 – 153943EGF-like 12CuratedPROSITE-ProRule annotationAdd
BLAST
Domaini1540 – 158243EGF-like 13CuratedPROSITE-ProRule annotationAdd
BLAST
Domaini1582 – 1708127FAS1 5CuratedPROSITE-ProRule annotationAdd
BLAST
Domaini1724 – 1864141FAS1 6CuratedPROSITE-ProRule annotationAdd
BLAST
Domaini1966 – 203166Laminin EGF-like 2CuratedAdd
BLAST
Domaini2056 – 209035EGF-like 14CuratedPROSITE-ProRule annotationAdd
BLAST
Domaini2091 – 213141EGF-like 15CuratedPROSITE-ProRule annotationAdd
BLAST
Domaini2132 – 217443EGF-like 16CuratedPROSITE-ProRule annotationAdd
BLAST
Domaini2206 – 230196LinkCuratedPROSITE-ProRule annotationAdd
BLAST
Domaini2322 – 2459138FAS1 7CuratedPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 16 EGF-like domains.CuratedPROSITE-ProRule annotation
Contains 7 FAS1 domains.CuratedPROSITE-ProRule annotation
Contains 2 laminin EGF-like domains.Curated
Contains 1 Link domain.CuratedPROSITE-ProRule annotation

Keywords - Domaini

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

Phylogenomic databases

eggNOGiCOG2335.
GeneTreeiENSGT00730000110695.
HOGENOMiHOG000154436.
HOVERGENiHBG079218.
InParanoidiQ9NY15.
OMAiGNCSDGI.
OrthoDBiEOG7PS1DH.
PhylomeDBiQ9NY15.
TreeFamiTF331489.

Family and domain databases

Gene3Di2.30.180.10. 7 hits.
2.40.155.10. 3 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. 5 hits.
PF02469. Fasciclin. 6 hits.
PF00193. Xlink. 1 hit.
[Graphical view]
SMARTiSM00181. EGF. 17 hits.
SM00180. EGF_Lam. 1 hit.
SM00554. FAS1. 7 hits.
SM00445. LINK. 1 hit.
[Graphical view]
SUPFAMiSSF56436. SSF56436. 1 hit.
SSF82153. SSF82153. 8 hits.
PROSITEiPS00022. EGF_1. 7 hits.
PS01186. EGF_2. 16 hits.
PS50026. EGF_3. 20 hits.
PS01248. EGF_LAM_1. 2 hits.
PS50213. FAS1. 7 hits.
PS01241. LINK_1. 1 hit.
PS50963. LINK_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 11 Publication (identifier: Q9NY15-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAGPRGLLPL CLLAFCLAGF SFVRGQVLFK GCDVKTTFVT HVPCTSCAAI
60 70 80 90 100
KKQTCPSGWL RELPDQITQD CRYEVQLGGS MVSMSGCRRK CRKQVVQKAC
110 120 130 140 150
CPGYWGSRCH ECPGGAETPC NGHGTCLDGM DRNGTCVCQE NFRGSACQEC
160 170 180 190 200
QDPNRFGPDC QSVCSCVHGV CNHGPRGDGS CLCFAGYTGP HCDQELPVCQ
210 220 230 240 250
ELRCPQNTQC SAEAPSCRCL PGYTQQGSEC RAPNPCWPSP CSLLAQCSVS
260 270 280 290 300
PKGQAQCHCP ENYHGDGMVC LPKDPCTDNL GGCPSNSTLC VYQKPGQAFC
310 320 330 340 350
TCRPGLVSIN SNASAGCFAF CSPFSCDRSA TCQVTADGKT SCVCRESEVG
360 370 380 390 400
DGRACYGHLL HEVQKATQTG RVFLQLRVAV AMMDQGCREI LTTAGPFTVL
410 420 430 440 450
VPSVSSFSSR TMNASLAQQL CRQHIIAGQH ILEDTRTQQT RRWWTLAGQE
460 470 480 490 500
ITVTFNQFTK YSYKYKDQPQ QTFNIYKANN IAANGVFHVV TGLRWQAPSG
510 520 530 540 550
TPGDPKRTIG QILASTEAFS RFETILENCG LPSILDGPGP FTVFAPSNEA
560 570 580 590 600
VDSLRDGRLI YLFTAGLSKL QELVRYHIYN HGQLTVEKLI SKGRILTMAN
610 620 630 640 650
QVLAVNISEE GRILLGPEGV PLQRVDVMAA NGVIHMLDGI LLPPTILPIL
660 670 680 690 700
PKHCSEEQHK IVAGSCVDCQ ALNTSTCPPN SVKLDIFPKE CVYIHDPTGL
710 720 730 740 750
NVLKKGCASY CNQTIMEQGC CKGFFGPDCT QCPGGFSNPC YGKGNCSDGI
760 770 780 790 800
QGNGACLCFP DYKGIACHIC SNPNKHGEQC QEDCGCVHGL CDNRPGSGGV
810 820 830 840 850
CQQGTCAPGF SGRFCNESMG DCGPTGLAQH CHLHARCVSQ EGVARCRCLD
860 870 880 890 900
GFEGDGFSCT PSNPCSHPDR GGCSENAECV PGSLGTHHCT CHKGWSGDGR
910 920 930 940 950
VCVAIDECEL DMRGGCHTDA LCSYVGPGQS RCTCKLGFAG DGYQCSPIDP
960 970 980 990 1000
CRAGNGGCHG LATCRAVGGG QRVCTCPPGF GGDGFSCYGD IFRELEANAH
1010 1020 1030 1040 1050
FSIFYQWLKS AGITLPADRR VTALVPSEAA VRQLSPEDRA FWLQPRTLPN
1060 1070 1080 1090 1100
LVRAHFLQGA LFEEELARLG GQEVATLNPT TRWEIRNISG RVWVQNASVD
1110 1120 1130 1140 1150
VADLLATNGV LHILSQVLLP PRGDVPGGQG LLQQLDLVPA FSLFRELLQH
1160 1170 1180 1190 1200
HGLVPQIEAA TAYTIFVPTN RSLEAQGNSS HLDADTVRHH VVLGEALSME
1210 1220 1230 1240 1250
TLRKGGHRNS LLGPAHWIVF YNHSGQPEVN HVPLEGPMLE APGRSLIGLS
1260 1270 1280 1290 1300
GVLTVGSSRC LHSHAEALRE KCVNCTRRFR CTQGFQLQDT PRKSCVYRSG
1310 1320 1330 1340 1350
FSFSRGCSYT CAKKIQVPDC CPGFFGTLCE PCPGGLGGVC SGHGQCQDRF
1360 1370 1380 1390 1400
LGSGECHCHE GFHGTACEVC ELGRYGPNCT GVCDCAHGLC QEGLQGDGSC
1410 1420 1430 1440 1450
VCNVGWQGLR CDQKITSPQC PRKCDPNANC VQDSAGASTC ACAAGYSGNG
1460 1470 1480 1490 1500
IFCSEVDPCA HGHGGCSPHA NCTKVAPGQR TCTCQDGYMG DGELCQEINS
1510 1520 1530 1540 1550
CLIHHGGCHI HAECIPTGPQ QVSCSCREGY SGDGIRTCEL LDPCSKNNGG
1560 1570 1580 1590 1600
CSPYATCKST GDGQRTCTCD TAHTVGDGLT CRARVGLELL RDKHASFFSL
1610 1620 1630 1640 1650
RLLEYKELKG DGPFTIFVPH ADLMSNLSQD ELARIRAHRQ LVFRYHVVGC
1660 1670 1680 1690 1700
RRLRSEDLLE QGYATALSGH PLRFSEREGS IYLNDFARVV SSDHEAVNGI
1710 1720 1730 1740 1750
LHFIDRVLLP PEALHWEPDD APIPRRNVTA AAQGFGYKIF SGLLKVAGLL
1760 1770 1780 1790 1800
PLLREASHRP FTMLWPTDAA FRALPPDRQA WLYHEDHRDK LAAILRGHMI
1810 1820 1830 1840 1850
RNVEALASDL PNLGPLRTMH GTPISFSCSR TRAGELMVGE DDARIVQRHL
1860 1870 1880 1890 1900
PFEGGLAYGI DQLLEPPGLG ARCDHFETRP LRLNTCSICG LEPPCPEGSQ
1910 1920 1930 1940 1950
EQGSPEACWR FYPKFWTSPP LHSLGLRSVW VHPSLWGRPQ GLGRGCHRNC
1960 1970 1980 1990 2000
VTTTWKPSCC PGHYGSECQA CPGGPSSPCS DRGVCMDGMS GSGQCLCRSG
2010 2020 2030 2040 2050
FAGTACELCA PGAFGPHCQA CRCTVHGRCD EGLGGSGSCF CDEGWTGPRC
2060 2070 2080 2090 2100
EVQLELQPVC TPPCAPEAVC RAGNSCECSL GYEGDGRVCT VADLCQDGHG
2110 2120 2130 2140 2150
GCSEHANCSQ VGTMVTCTCL PDYEGDGWSC RARNPCTDGH RGGCSEHANC
2160 2170 2180 2190 2200
LSTGLNTRRC ECHAGYVGDG LQCLEESEPP VDRCLGQPPP CHSDAMCTDL
2210 2220 2230 2240 2250
HFQEKRAGVF HLQATSGPYG LNFSEAEAAC EAQGAVLASF PQLSAAQQLG
2260 2270 2280 2290 2300
FHLCLMGWLA NGSTAHPVVF PVADCGNGRV GIVSLGARKN LSERWDAYCF
2310 2320 2330 2340 2350
RVQDVACRCR NGFVGDGIST CNGKLLDVLA ATANFSTFYG MLLGYANATQ
2360 2370 2380 2390 2400
RGLDFLDFLD DELTYKTLFV PVNEGFVDNM TLSGPDLELH ASNATLLSAN
2410 2420 2430 2440 2450
ASQGKLLPAH SGLSLIISDA GPDNSSWAPV APGTVVVSRI IVWDIMAFNG
2460 2470 2480 2490 2500
IIHALASPLL APPQPQAVLA PEAPPVAAGV GAVLAAGALL GLVAGALYLR
2510 2520 2530 2540 2550
ARGKPMGFGF SAFQAEDDAD DDFSPWQEGT NPTLVSVPNP VFGSDTFCEP
2560 2570
FDDSLLEEDF PDTQRILTVK
Length:2,570
Mass (Da):275,482
Last modified:May 18, 2010 - v3
Checksum:iFA55D191D9D30FAD
GO
Isoform 21 Publication (identifier: Q9NY15-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     746-803: CSDGIQGNGA...RPGSGGVCQQ → VSPILSWGEV...IISHILIKNN
     804-2570: Missing.

Show »
Length:803
Mass (Da):87,026
Checksum:i1A833922D0F223FB
GO

Sequence cautioni

The sequence BAA13377.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti913 – 9131R → G in CAB61827. (PubMed:11829752)Curated
Sequence conflicti2200 – 22001L → Q in CAB61827. (PubMed:11829752)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti672 – 6721L → M.
Corresponds to variant rs12636502 [ dbSNP | Ensembl ].
VAR_060338
Natural varianti912 – 9121M → V.4 Publications
Corresponds to variant rs9835659 [ dbSNP | Ensembl ].
VAR_060339
Natural varianti1127 – 11271G → R.
Corresponds to variant rs2286786 [ dbSNP | Ensembl ].
VAR_055774
Natural varianti1833 – 18331A → P.3 Publications
Corresponds to variant rs7630214 [ dbSNP | Ensembl ].
VAR_060340
Natural varianti2282 – 22821I → V.1 Publication
Corresponds to variant rs4434138 [ dbSNP | Ensembl ].
VAR_055775
Natural varianti2506 – 25061M → T.
Corresponds to variant rs13303 [ dbSNP | Ensembl ].
VAR_019078

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei746 – 80358CSDGI…GVCQQ → VSPILSWGEVWGTQGLLHRL ASDWLCVWAKPATLALGFSY LCSGKLDQIISHILIKNN in isoform 2. 1 PublicationVSP_050764Add
BLAST
Alternative sequencei804 – 25701767Missing in isoform 2. 1 PublicationVSP_050765Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ275213 mRNA. Translation: CAB61827.1.
AB052956 mRNA. Translation: BAC15606.1.
AB052957 mRNA. Translation: BAC15607.1.
D87433 mRNA. Translation: BAA13377.2. Different initiation.
AC006208 Genomic DNA. No translation available.
AC112215 Genomic DNA. No translation available.
BC150250 mRNA. Translation: AAI50251.1.
CCDSiCCDS33768.1. [Q9NY15-1]
RefSeqiNP_055951.2. NM_015136.2. [Q9NY15-1]
UniGeneiHs.301989.

Genome annotation databases

GeneIDi23166.
KEGGihsa:23166.
UCSCiuc003dei.1. human. [Q9NY15-2]
uc003dej.3. human. [Q9NY15-1]

Polymorphism databases

DMDMi296452949.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ275213 mRNA. Translation: CAB61827.1 .
AB052956 mRNA. Translation: BAC15606.1 .
AB052957 mRNA. Translation: BAC15607.1 .
D87433 mRNA. Translation: BAA13377.2 . Different initiation.
AC006208 Genomic DNA. No translation available.
AC112215 Genomic DNA. No translation available.
BC150250 mRNA. Translation: AAI50251.1 .
CCDSi CCDS33768.1. [Q9NY15-1 ]
RefSeqi NP_055951.2. NM_015136.2. [Q9NY15-1 ]
UniGenei Hs.301989.

3D structure databases

ProteinModelPortali Q9NY15.
SMRi Q9NY15. Positions 29-350, 518-643, 736-983, 1340-1575, 1939-2300.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 116778. 5 interactions.
IntActi Q9NY15. 71 interactions.
MINTi MINT-4831401.
STRINGi 9606.ENSP00000312946.

PTM databases

PhosphoSitei Q9NY15.

Polymorphism databases

DMDMi 296452949.

Proteomic databases

PaxDbi Q9NY15.
PRIDEi Q9NY15.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 23166.
KEGGi hsa:23166.
UCSCi uc003dei.1. human. [Q9NY15-2 ]
uc003dej.3. human. [Q9NY15-1 ]

Organism-specific databases

CTDi 23166.
GeneCardsi GC03P052529.
H-InvDB HIX0003360.
HGNCi HGNC:18628. STAB1.
HPAi HPA005434.
MIMi 608560. gene.
neXtProti NX_Q9NY15.
PharmGKBi PA38610.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG2335.
GeneTreei ENSGT00730000110695.
HOGENOMi HOG000154436.
HOVERGENi HBG079218.
InParanoidi Q9NY15.
OMAi GNCSDGI.
OrthoDBi EOG7PS1DH.
PhylomeDBi Q9NY15.
TreeFami TF331489.

Enzyme and pathway databases

Reactomei REACT_164002. Scavenging by Class H Receptors.

Miscellaneous databases

ChiTaRSi STAB1. human.
GeneWikii STAB1.
GenomeRNAii 23166.
NextBioi 44560.
PROi Q9NY15.
SOURCEi Search...

Gene expression databases

Bgeei Q9NY15.
CleanExi HS_STAB1.
Genevestigatori Q9NY15.

Family and domain databases

Gene3Di 2.30.180.10. 7 hits.
2.40.155.10. 3 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. 5 hits.
PF02469. Fasciclin. 6 hits.
PF00193. Xlink. 1 hit.
[Graphical view ]
SMARTi SM00181. EGF. 17 hits.
SM00180. EGF_Lam. 1 hit.
SM00554. FAS1. 7 hits.
SM00445. LINK. 1 hit.
[Graphical view ]
SUPFAMi SSF56436. SSF56436. 1 hit.
SSF82153. SSF82153. 8 hits.
PROSITEi PS00022. EGF_1. 7 hits.
PS01186. EGF_2. 16 hits.
PS50026. EGF_3. 20 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] (ISOFORM 1), TISSUE SPECIFICITY, VARIANTS VARIANTS VAL-912; PRO-1833 AND VAL-2282.
  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] (ISOFORMS 1 AND 2), FUNCTION, TISSUE SPECIFICITY, VARIANT VAL-912.
  3. "Prediction of the coding sequences of unidentified human genes. VI. The coding sequences of 80 new genes (KIAA0201-KIAA0280) deduced by analysis of cDNA clones from cell line KG-1 and brain."
    Nagase T., Seki N., Ishikawa K., Ohira M., Kawarabayasi Y., Ohara O., Tanaka A., Kotani H., Miyajima N., Nomura N.
    DNA Res. 3:321-329(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANTS VAL-912 AND PRO-1833.
    Tissue: BrainImported.
  4. "Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
    Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
    DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SEQUENCE REVISION.
  5. "The DNA sequence, annotation and analysis of human chromosome 3."
    Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
    , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
    Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANTS VAL-912 AND PRO-1833.
  7. "Novel stabilin-1 interacting chitinase-like protein (SI-CLP) is up-regulated in alternatively activated macrophages and secreted via lysosomal pathway."
    Kzhyshkowska J., Mamidi S., Gratchev A., Kremmer E., Schmuttermaier C., Krusell L., Haus G., Utikal J., Schledzewski K., Scholtze J., Goerdt S.
    Blood 107:3221-3228(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH CHID1.
  8. "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-1096; ASN-1626; ASN-1727; ASN-2347 AND ASN-2424.
    Tissue: Liver.

Entry informationi

Entry nameiSTAB1_HUMAN
AccessioniPrimary (citable) accession number: Q9NY15
Secondary accession number(s): A7E297
, Q8IUH0, Q8IUH1, Q93072
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 5, 2004
Last sequence update: May 18, 2010
Last modified: October 29, 2014
This is version 125 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, Reference proteome

Documents

  1. Human chromosome 3
    Human chromosome 3: 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