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Q4LDE5

- SVEP1_HUMAN

UniProt

Q4LDE5 - SVEP1_HUMAN

Protein

Sushi, von Willebrand factor type A, EGF and pentraxin domain-containing protein 1

Gene

SVEP1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 94 (01 Oct 2014)
      Sequence version 3 (18 May 2010)
      Previous versions | rss
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    Functioni

    May play a role in the cell attachment process.By similarity

    GO - Molecular functioni

    1. calcium ion binding Source: InterPro
    2. chromatin binding Source: Ensembl

    GO - Biological processi

    1. cell adhesion Source: UniProtKB-KW

    Keywords - Biological processi

    Cell adhesion

    Keywords - Ligandi

    Calcium

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Sushi, von Willebrand factor type A, EGF and pentraxin domain-containing protein 1
    Alternative name(s):
    CCP module-containing protein 22
    Polydom
    Selectin-like osteoblast-derived protein
    Short name:
    SEL-OB
    Serologically defined breast cancer antigen NY-BR-38
    Gene namesi
    Name:SVEP1
    Synonyms:C9orf13, CCP22, SELOB
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 9

    Organism-specific databases

    HGNCiHGNC:15985. SVEP1.

    Subcellular locationi

    Secreted Curated. Cytoplasm 1 Publication. Membrane 1 Publication; Peripheral membrane protein 1 Publication

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. extracellular region Source: UniProtKB-SubCell
    3. membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Membrane, Secreted

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA25971.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1717Sequence AnalysisAdd
    BLAST
    Chaini18 – 35713554Sushi, von Willebrand factor type A, EGF and pentraxin domain-containing protein 1PRO_0000320179Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi186 – 1861N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi378 ↔ 420By similarity
    Disulfide bondi406 ↔ 433By similarity
    Disulfide bondi438 ↔ 480By similarity
    Disulfide bondi466 ↔ 493By similarity
    Disulfide bondi498 ↔ 544By similarity
    Disulfide bondi529 ↔ 559By similarity
    Disulfide bondi727 ↔ 769By similarity
    Disulfide bondi753 ↔ 787By similarity
    Glycosylationi847 – 8471N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1102 – 11021N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1197 ↔ 1208By similarity
    Disulfide bondi1202 ↔ 1217By similarity
    Disulfide bondi1219 ↔ 1228By similarity
    Disulfide bondi1235 ↔ 1246By similarity
    Disulfide bondi1240 ↔ 1255By similarity
    Disulfide bondi1257 ↔ 1266By similarity
    Disulfide bondi1273 ↔ 1284By similarity
    Disulfide bondi1278 ↔ 1293By similarity
    Disulfide bondi1295 ↔ 1304By similarity
    Disulfide bondi1311 ↔ 1322By similarity
    Disulfide bondi1316 ↔ 1331By similarity
    Disulfide bondi1333 ↔ 1342By similarity
    Disulfide bondi1349 ↔ 1360By similarity
    Disulfide bondi1354 ↔ 1369By similarity
    Disulfide bondi1371 ↔ 1380By similarity
    Disulfide bondi1387 ↔ 1398By similarity
    Disulfide bondi1392 ↔ 1407By similarity
    Disulfide bondi1409 ↔ 1418By similarity
    Disulfide bondi1631 ↔ 1672By similarity
    Disulfide bondi1658 ↔ 1685By similarity
    Disulfide bondi1690 ↔ 1730By similarity
    Disulfide bondi1716 ↔ 1743By similarity
    Disulfide bondi1749 ↔ 1761By similarity
    Disulfide bondi1755 ↔ 1770By similarity
    Disulfide bondi1772 ↔ 1783By similarity
    Disulfide bondi1789 ↔ 1829By similarity
    Disulfide bondi1815 ↔ 1842By similarity
    Disulfide bondi1847 ↔ 1887By similarity
    Disulfide bondi1873 ↔ 1900By similarity
    Disulfide bondi1905 ↔ 1945By similarity
    Disulfide bondi1931 ↔ 1958By similarity
    Disulfide bondi1963 ↔ 2003By similarity
    Disulfide bondi1989 ↔ 2016By similarity
    Disulfide bondi2021 ↔ 2061By similarity
    Disulfide bondi2047 ↔ 2078By similarity
    Disulfide bondi2083 ↔ 2126By similarity
    Disulfide bondi2112 ↔ 2141By similarity
    Disulfide bondi2146 ↔ 2186By similarity
    Disulfide bondi2172 ↔ 2199By similarity
    Disulfide bondi2204 ↔ 2245By similarity
    Disulfide bondi2231 ↔ 2259By similarity
    Disulfide bondi2264 ↔ 2304By similarity
    Disulfide bondi2290 ↔ 2318By similarity
    Disulfide bondi2323 ↔ 2363By similarity
    Disulfide bondi2349 ↔ 2376By similarity
    Disulfide bondi2381 ↔ 2422By similarity
    Disulfide bondi2408 ↔ 2435By similarity
    Disulfide bondi2440 ↔ 2480By similarity
    Disulfide bondi2466 ↔ 2493By similarity
    Disulfide bondi2498 ↔ 2538By similarity
    Disulfide bondi2524 ↔ 2551By similarity
    Disulfide bondi2556 ↔ 2596By similarity
    Disulfide bondi2582 ↔ 2608By similarity
    Disulfide bondi2685 ↔ 2712By similarity
    Disulfide bondi2717 ↔ 2757By similarity
    Disulfide bondi2743 ↔ 2770By similarity
    Disulfide bondi2775 ↔ 2815By similarity
    Disulfide bondi2801 ↔ 2828By similarity
    Disulfide bondi2833 ↔ 2873By similarity
    Disulfide bondi2859 ↔ 2886By similarity
    Disulfide bondi2891 ↔ 2931By similarity
    Disulfide bondi2917 ↔ 2944By similarity
    Disulfide bondi2949 ↔ 2989By similarity
    Disulfide bondi2975 ↔ 3002By similarity
    Disulfide bondi3007 ↔ 3046By similarity
    Glycosylationi3018 – 30181N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi3032 ↔ 3059By similarity
    Disulfide bondi3064 ↔ 3104By similarity
    Disulfide bondi3090 ↔ 3117By similarity
    Disulfide bondi3122 ↔ 3163By similarity
    Disulfide bondi3148 ↔ 3176By similarity
    Disulfide bondi3181 ↔ 3221By similarity
    Glycosylationi3186 – 31861N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi3207 ↔ 3236By similarity
    Disulfide bondi3241 ↔ 3281By similarity
    Disulfide bondi3267 ↔ 3294By similarity
    Disulfide bondi3299 ↔ 3339By similarity
    Disulfide bondi3325 ↔ 3352By similarity
    Disulfide bondi3384 ↔ 3411By similarity
    Disulfide bondi3416 ↔ 3456By similarity
    Disulfide bondi3442 ↔ 3468By similarity
    Disulfide bondi3504 ↔ 3514By similarity
    Disulfide bondi3508 ↔ 3520By similarity
    Disulfide bondi3522 ↔ 3531By similarity
    Disulfide bondi3536 ↔ 3546By similarity
    Disulfide bondi3540 ↔ 3552By similarity
    Disulfide bondi3554 ↔ 3563By similarity

    Post-translational modificationi

    O-glycosylated with core 1 or possibly core 8 glycans.1 Publication

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    MaxQBiQ4LDE5.
    PaxDbiQ4LDE5.
    PRIDEiQ4LDE5.

    PTM databases

    PhosphoSiteiQ4LDE5.

    Expressioni

    Tissue specificityi

    Present in mesenchymal primary cultured cell lysates (at protein level). Highly expressed in placenta. Also expressed in marrow stromal cell. Weakly or not expressed in other tissues.2 Publications

    Gene expression databases

    ArrayExpressiQ4LDE5.
    BgeeiQ4LDE5.
    GenevestigatoriQ4LDE5.

    Organism-specific databases

    HPAiHPA020610.
    HPA021520.

    Interactioni

    Protein-protein interaction databases

    BioGridi123051. 4 interactions.
    IntActiQ4LDE5. 12 interactions.
    MINTiMINT-1197821.

    Structurei

    3D structure databases

    ProteinModelPortaliQ4LDE5.
    SMRiQ4LDE5. Positions 79-255, 313-507, 1195-1420, 1445-3563.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini83 – 264182VWFAPROSITE-ProRule annotationAdd
    BLAST
    Domaini376 – 43560Sushi 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini436 – 49560Sushi 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini496 – 56166Sushi 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini560 – 64283HYR 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini643 – 72482HYR 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini725 – 78965Sushi 4PROSITE-ProRule annotationAdd
    BLAST
    Domaini1193 – 122937EGF-like 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini1231 – 126737EGF-like 2; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini1269 – 130537EGF-like 3; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini1307 – 134337EGF-like 4; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini1345 – 138137EGF-like 5; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini1383 – 141937EGF-like 6; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini1430 – 1623194PentaxinAdd
    BLAST
    Domaini1629 – 168759Sushi 5PROSITE-ProRule annotationAdd
    BLAST
    Domaini1688 – 174558Sushi 6PROSITE-ProRule annotationAdd
    BLAST
    Domaini1745 – 178440EGF-like 7; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini1787 – 184458Sushi 7PROSITE-ProRule annotationAdd
    BLAST
    Domaini1845 – 190258Sushi 8PROSITE-ProRule annotationAdd
    BLAST
    Domaini1903 – 196058Sushi 9PROSITE-ProRule annotationAdd
    BLAST
    Domaini1961 – 201858Sushi 10PROSITE-ProRule annotationAdd
    BLAST
    Domaini2019 – 208062Sushi 11PROSITE-ProRule annotationAdd
    BLAST
    Domaini2081 – 214363Sushi 12PROSITE-ProRule annotationAdd
    BLAST
    Domaini2144 – 220158Sushi 13PROSITE-ProRule annotationAdd
    BLAST
    Domaini2202 – 226160Sushi 14PROSITE-ProRule annotationAdd
    BLAST
    Domaini2262 – 232059Sushi 15PROSITE-ProRule annotationAdd
    BLAST
    Domaini2321 – 237858Sushi 16PROSITE-ProRule annotationAdd
    BLAST
    Domaini2379 – 243759Sushi 17PROSITE-ProRule annotationAdd
    BLAST
    Domaini2438 – 249558Sushi 18PROSITE-ProRule annotationAdd
    BLAST
    Domaini2496 – 255358Sushi 19PROSITE-ProRule annotationAdd
    BLAST
    Domaini2554 – 261057Sushi 20PROSITE-ProRule annotationAdd
    BLAST
    Domaini2663 – 271452Sushi 21PROSITE-ProRule annotationAdd
    BLAST
    Domaini2715 – 277258Sushi 22PROSITE-ProRule annotationAdd
    BLAST
    Domaini2773 – 283058Sushi 23PROSITE-ProRule annotationAdd
    BLAST
    Domaini2831 – 288858Sushi 24PROSITE-ProRule annotationAdd
    BLAST
    Domaini2889 – 294658Sushi 25PROSITE-ProRule annotationAdd
    BLAST
    Domaini2947 – 300458Sushi 26PROSITE-ProRule annotationAdd
    BLAST
    Domaini3005 – 306157Sushi 27PROSITE-ProRule annotationAdd
    BLAST
    Domaini3062 – 311958Sushi 28PROSITE-ProRule annotationAdd
    BLAST
    Domaini3120 – 317859Sushi 29PROSITE-ProRule annotationAdd
    BLAST
    Domaini3179 – 323860Sushi 30PROSITE-ProRule annotationAdd
    BLAST
    Domaini3239 – 329658Sushi 31PROSITE-ProRule annotationAdd
    BLAST
    Domaini3297 – 335458Sushi 32PROSITE-ProRule annotationAdd
    BLAST
    Domaini3355 – 341359Sushi 33PROSITE-ProRule annotationAdd
    BLAST
    Domaini3414 – 347057Sushi 34PROSITE-ProRule annotationAdd
    BLAST
    Domaini3500 – 353233EGF-like 8PROSITE-ProRule annotationAdd
    BLAST
    Domaini3533 – 356432EGF-like 9PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni887 – 8948O-glycosylated at one site

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi2845 – 28473Cell attachment siteSequence Analysis

    Sequence similaritiesi

    Contains 9 EGF-like domains.PROSITE-ProRule annotation
    Contains 2 HYR domains.PROSITE-ProRule annotation
    Contains 1 pentaxin domain.Curated
    Contains 34 Sushi (CCP/SCR) domains.PROSITE-ProRule annotation
    Contains 1 VWFA domain.PROSITE-ProRule annotation

    Keywords - Domaini

    EGF-like domain, Repeat, Signal, Sushi

    Phylogenomic databases

    eggNOGiNOG12793.
    HOVERGENiHBG108523.
    KOiK17495.
    OMAiIDCRLED.
    OrthoDBiEOG7BS48H.
    PhylomeDBiQ4LDE5.
    TreeFamiTF342247.

    Family and domain databases

    Gene3Di2.40.155.10. 1 hit.
    2.60.120.200. 1 hit.
    3.40.50.410. 1 hit.
    InterProiIPR008985. ConA-like_lec_gl_sf.
    IPR013320. ConA-like_subgrp.
    IPR000742. EG-like_dom.
    IPR001881. EGF-like_Ca-bd_dom.
    IPR013032. EGF-like_CS.
    IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
    IPR018097. EGF_Ca-bd_CS.
    IPR023413. GFP_like.
    IPR009030. Growth_fac_rcpt_N_dom.
    IPR003410. Hyalin.
    IPR001759. Pentaxin.
    IPR000436. Sushi_SCR_CCP.
    IPR011641. Tyr-kin_ephrin_A/B_rcpt-like.
    IPR002035. VWF_A.
    [Graphical view]
    PfamiPF00008. EGF. 5 hits.
    PF07645. EGF_CA. 1 hit.
    PF07699. GCC2_GCC3. 4 hits.
    PF12661. hEGF. 1 hit.
    PF02494. HYR. 2 hits.
    PF00354. Pentaxin. 1 hit.
    PF00084. Sushi. 32 hits.
    PF00092. VWA. 1 hit.
    [Graphical view]
    PRINTSiPR00895. PENTAXIN.
    SMARTiSM00032. CCP. 34 hits.
    SM00181. EGF. 4 hits.
    SM00179. EGF_CA. 6 hits.
    SM00327. VWA. 1 hit.
    [Graphical view]
    SUPFAMiSSF49899. SSF49899. 1 hit.
    SSF53300. SSF53300. 1 hit.
    SSF57184. SSF57184. 3 hits.
    SSF57535. SSF57535. 33 hits.
    PROSITEiPS00010. ASX_HYDROXYL. 6 hits.
    PS00022. EGF_1. 9 hits.
    PS01186. EGF_2. 11 hits.
    PS50026. EGF_3. 9 hits.
    PS01187. EGF_CA. 6 hits.
    PS50825. HYR. 2 hits.
    PS50923. SUSHI. 34 hits.
    PS50234. VWFA. 1 hit.
    [Graphical view]

    Sequences (4)i

    Sequence statusi: Complete.

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

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q4LDE5-1) [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

    MWPRLAFCCW GLALVSGWAT FQQMSPSRNF SFRLFPETAP GAPGSIPAPP     50
    APGDEAAGSR VERLGQAFRR RVRLLRELSE RLELVFLVDD SSSVGEVNFR 100
    SELMFVRKLL SDFPVVPTAT RVAIVTFSSK NYVVPRVDYI STRRARQHKC 150
    ALLLQEIPAI SYRGGGTYTK GAFQQAAQIL LHARENSTKV VFLITDGYSN 200
    GGDPRPIAAS LRDSGVEIFT FGIWQGNIRE LNDMASTPKE EHCYLLHSFE 250
    EFEALARRAL HEDLPSGSFI QDDMVHCSYL CDEGKDCCDR MGSCKCGTHT 300
    GHFECICEKG YYGKGLQYEC TACPSGTYKP EGSPGGISSC IPCPDENHTS 350
    PPGSTSPEDC VCREGYRASG QTCELVHCPA LKPPENGYFI QNTCNNHFNA 400
    ACGVRCHPGF DLVGSSIILC LPNGLWSGSE SYCRVRTCPH LRQPKHGHIS 450
    CSTREMLYKT TCLVACDEGY RLEGSDKLTC QGNSQWDGPE PRCVERHCST 500
    FQMPKDVIIS PHNCGKQPAK FGTICYVSCR QGFILSGVKE MLRCTTSGKW 550
    NVGVQAAVCK DVEAPQINCP KDIEAKTLEQ QDSANVTWQI PTAKDNSGEK 600
    VSVHVHPAFT PPYLFPIGDV AIVYTATDLS GNQASCIFHI KVIDAEPPVI 650
    DWCRSPPPVQ VSEKVHAASW DEPQFSDNSG AELVITRSHT QGDLFPQGET 700
    IVQYTATDPS GNNRTCDIHI VIKGSPCEIP FTPVNGDFIC TPDNTGVNCT 750
    LTCLEGYDFT EGSTDKYYCA YEDGVWKPTY TTEWPDCAKK RFANHGFKSF 800
    EMFYKAARCD DTDLMKKFSE AFETTLGKMV PSFCSDAEDI DCRLEENLTK 850
    KYCLEYNYDY ENGFAIGPGG WGAANRLDYS YDDFLDTVQE TATSIGNAKS 900
    SRIKRSAPLS DYKIKLIFNI TASVPLPDER NDTLEWENQQ RLLQTLETIT 950
    NKLKRTLNKD PMYSFQLASE ILIADSNSLE TKKASPFCRP GSVLRGRMCV 1000
    NCPLGTYYNL EHFTCESCRI GSYQDEEGQL ECKLCPSGMY TEYIHSRNIS 1050
    DCKAQCKQGT YSYSGLETCE SCPLGTYQPK FGSRSCLSCP ENTSTVKRGA 1100
    VNISACGVPC PEGKFSRSGL MPCHPCPRDY YQPNAGKAFC LACPFYGTTP 1150
    FAGSRSITEC SSFSSTFSAA EESVVPPASL GHIKKRHEIS SQVFHECFFN 1200
    PCHNSGTCQQ LGRGYVCLCP LGYTGLKCET DIDECSPLPC LNNGVCKDLV 1250
    GEFICECPSG YTGQRCEENI NECSSSPCLN KGICVDGVAG YRCTCVKGFV 1300
    GLHCETEVNE CQSNPCLNNA VCEDQVGGFL CKCPPGFLGT RCGKNVDECL 1350
    SQPCKNGATC KDGANSFRCL CAAGFTGSHC ELNINECQSN PCRNQATCVD 1400
    ELNSYSCKCQ PGFSGKRCET EQSTGFNLDF EVSGIYGYVM LDGMLPSLHA 1450
    LTCTFWMKSS DDMNYGTPIS YAVDNGSDNT LLLTDYNGWV LYVNGREKIT 1500
    NCPSVNDGRW HHIAITWTSA NGIWKVYIDG KLSDGGAGLS VGLPIPGGGA 1550
    LVLGQEQDKK GEGFSPAESF VGSISQLNLW DYVLSPQQVK SLATSCPEEL 1600
    SKGNVLAWPD FLSGIVGKVK IDSKSIFCSD CPRLGGSVPH LRTASEDLKP 1650
    GSKVNLFCDP GFQLVGNPVQ YCLNQGQWTQ PLPHCERISC GVPPPLENGF 1700
    HSADDFYAGS TVTYQCNNGY YLLGDSRMFC TDNGSWNGVS PSCLDVDECA 1750
    VGSDCSEHAS CLNVDGSYIC SCVPPYTGDG KNCAEPIKCK APGNPENGHS 1800
    SGEIYTVGAE VTFSCQEGYQ LMGVTKITCL ESGEWNHLIP YCKAVSCGKP 1850
    AIPENGCIEE LAFTFGSKVT YRCNKGYTLA GDKESSCLAN SSWSHSPPVC 1900
    EPVKCSSPEN INNGKYILSG LTYLSTASYS CDTGYSLQGP SIIECTASGI 1950
    WDRAPPACHL VFCGEPPAIK DAVITGNNFT FRNTVTYTCK EGYTLAGLDT 2000
    IECLADGKWS RSDQQCLAVS CDEPPIVDHA SPETAHRLFG DIAFYYCSDG 2050
    YSLADNSQLL CNAQGKWVPP EGQDMPRCIA HFCEKPPSVS YSILESVSKA 2100
    KFAAGSVVSF KCMEGFVLNT SAKIECMRGG QWNPSPMSIQ CIPVRCGEPP 2150
    SIMNGYASGS NYSFGAMVAY SCNKGFYIKG EKKSTCEATG QWSSPIPTCH 2200
    PVSCGEPPKV ENGFLEHTTG RIFESEVRYQ CNPGYKSVGS PVFVCQANRH 2250
    WHSESPLMCV PLDCGKPPPI QNGFMKGENF EVGSKVQFFC NEGYELVGDS 2300
    SWTCQKSGKW NKKSNPKCMP AKCPEPPLLE NQLVLKELTT EVGVVTFSCK 2350
    EGHVLQGPSV LKCLPSQQWN DSFPVCKIVL CTPPPLISFG VPIPSSALHF 2400
    GSTVKYSCVG GFFLRGNSTT LCQPDGTWSS PLPECVPVEC PQPEEIPNGI 2450
    IDVQGLAYLS TALYTCKPGF ELVGNTTTLC GENGHWLGGK PTCKAIECLK 2500
    PKEILNGKFS YTDLHYGQTV TYSCNRGFRL EGPSALTCLE TGDWDVDAPS 2550
    CNAIHCDSPQ PIENGFVEGA DYSYGAIIIY SCFPGFQVAG HAMQTCEESG 2600
    WSSSIPTCMP IDCGLPPHID FGDCTKLKDD QGYFEQEDDM MEVPYVTPHP 2650
    PYHLGAVAKT WENTKESPAT HSSNFLYGTM VSYTCNPGYE LLGNPVLICQ 2700
    EDGTWNGSAP SCISIECDLP TAPENGFLRF TETSMGSAVQ YSCKPGHILA 2750
    GSDLRLCLEN RKWSGASPRC EAISCKKPNP VMNGSIKGSN YTYLSTLYYE 2800
    CDPGYVLNGT ERRTCQDDKN WDEDEPICIP VDCSSPPVSA NGQVRGDEYT 2850
    FQKEIEYTCN EGFLLEGARS RVCLANGSWS GATPDCVPVR CATPPQLANG 2900
    VTEGLDYGFM KEVTFHCHEG YILHGAPKLT CQSDGNWDAE IPLCKPVNCG 2950
    PPEDLAHGFP NGFSFIHGGH IQYQCFPGYK LHGNSSRRCL SNGSWSGSSP 3000
    SCLPCRCSTP VIEYGTVNGT DFDCGKAARI QCFKGFKLLG LSEITCEADG 3050
    QWSSGFPHCE HTSCGSLPMI PNAFISETSS WKENVITYSC RSGYVIQGSS 3100
    DLICTEKGVW SQPYPVCEPL SCGSPPSVAN AVATGEAHTY ESEVKLRCLE 3150
    GYTMDTDTDT FTCQKDGRWF PERISCSPKK CPLPENITHI LVHGDDFSVN 3200
    RQVSVSCAEG YTFEGVNISV CQLDGTWEPP FSDESCSPVS CGKPESPEHG 3250
    FVVGSKYTFE STIIYQCEPG YELEGNRERV CQENRQWSGG VAICKETRCE 3300
    TPLEFLNGKA DIENRTTGPN VVYSCNRGYS LEGPSEAHCT ENGTWSHPVP 3350
    LCKPNPCPVP FVIPENALLS EKEFYVDQNV SIKCREGFLL QGHGIITCNP 3400
    DETWTQTSAK CEKISCGPPA HVENAIARGV HYQYGDMITY SCYSGYMLEG 3450
    FLRSVCLENG TWTSPPICRA VCRFPCQNGG ICQRPNACSC PEGWMGRLCE 3500
    EPICILPCLN GGRCVAPYQC DCPPGWTGSR CHTAVCQSPC LNGGKCVRPN 3550
    RCHCLSSWTG HNCSRKRRTG F 3571
    Length:3,571
    Mass (Da):390,170
    Last modified:May 18, 2010 - v3
    Checksum:i8F52DE456CED5DED
    GO
    Isoform 2 (identifier: Q4LDE5-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         868-868: P → N
         869-3571: Missing.

    Show »
    Length:868
    Mass (Da):96,134
    Checksum:i516974CD450855FD
    GO
    Isoform 3 (identifier: Q4LDE5-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-2074: Missing.

    Show »
    Length:1,497
    Mass (Da):163,559
    Checksum:i98D8650DB3B69DD4
    GO
    Isoform 4 (identifier: Q4LDE5-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1547-3571: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:1,546
    Mass (Da):170,093
    Checksum:iB304C96189C62CD1
    GO

    Sequence cautioni

    The sequence AAG48257.1 differs from that shown. Reason: Frameshift at positions 2630, 2638 and 2655.
    The sequence AAG48257.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence BAB14617.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence BAB55420.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence CAH73557.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence CAH74138.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence CAH73558.1 differs from that shown. Reason: Erroneous gene model prediction.
    The sequence CAH74139.1 differs from that shown. Reason: Erroneous gene model prediction.
    The sequence CAI14068.1 differs from that shown. Reason: Erroneous gene model prediction.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti429 – 4291S → L in CAF04067. (PubMed:16206243)Curated
    Sequence conflicti429 – 4291S → L in BAB55420. (PubMed:14702039)Curated
    Sequence conflicti604 – 6041H → R in BAB14617. (PubMed:14702039)Curated
    Sequence conflicti822 – 8221F → L in BAB14617. (PubMed:14702039)Curated
    Sequence conflicti842 – 8421C → W in CAF04067. (PubMed:16206243)Curated
    Sequence conflicti842 – 8421C → W in BAB55420. (PubMed:14702039)Curated
    Sequence conflicti980 – 9801E → G in CAF04067. (PubMed:16206243)Curated
    Sequence conflicti980 – 9801E → G in BAB55420. (PubMed:14702039)Curated
    Sequence conflicti1063 – 10631Y → C in CAF04067. (PubMed:16206243)Curated
    Sequence conflicti1063 – 10631Y → C in BAB55420. (PubMed:14702039)Curated
    Sequence conflicti1442 – 14421D → V in CAF04067. (PubMed:16206243)Curated
    Sequence conflicti1442 – 14421D → V in BAB55420. (PubMed:14702039)Curated
    Sequence conflicti1546 – 15461P → PGMF in CAF04067. (PubMed:16206243)Curated
    Sequence conflicti1775 – 17751P → S in CAF04067. (PubMed:16206243)Curated
    Sequence conflicti2179 – 21791K → E in CAD97901. (PubMed:17974005)Curated
    Sequence conflicti2189 – 21891T → S in BAC11489. (PubMed:14702039)Curated
    Sequence conflicti2237 – 22371S → P in BAC11489. (PubMed:14702039)Curated
    Sequence conflicti2246 – 22461Q → H in BAC11489. (PubMed:14702039)Curated
    Sequence conflicti2259 – 22591C → W in BAC11489. (PubMed:14702039)Curated
    Sequence conflicti2299 – 22991D → G in CAD97988. (PubMed:17974005)Curated
    Sequence conflicti2454 – 24541Q → R in BAC11489. (PubMed:14702039)Curated
    Sequence conflicti2519 – 25191T → I in CAD97901. (PubMed:17974005)Curated
    Sequence conflicti2623 – 26231D → A in AAG48257. (PubMed:12747765)Curated
    Sequence conflicti2705 – 27051W → R in BAC11489. (PubMed:14702039)Curated
    Sequence conflicti2753 – 27531D → G in BAC11489. (PubMed:14702039)Curated
    Sequence conflicti2833 – 28331C → R in BAC11489. (PubMed:14702039)Curated
    Sequence conflicti2857 – 28571Y → H in CAD97901. (PubMed:17974005)Curated
    Sequence conflicti3005 – 30051C → F in BAC11489. (PubMed:14702039)Curated
    Sequence conflicti3186 – 31861N → S in CAD97988. (PubMed:17974005)Curated
    Sequence conflicti3302 – 33021P → Q in CAF04067. (PubMed:16206243)Curated
    Sequence conflicti3302 – 33021P → Q in BAC11489. (PubMed:14702039)Curated
    Sequence conflicti3398 – 33981C → Y in CAF04067. (PubMed:16206243)Curated
    Sequence conflicti3398 – 33981C → Y in BAC11489. (PubMed:14702039)Curated
    Sequence conflicti3565 – 35651R → G in CAD97988. (PubMed:17974005)Curated
    Sequence conflicti3567 – 35671R → G in CAD97988. (PubMed:17974005)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti332 – 3321G → A.1 Publication
    Corresponds to variant rs3818764 [ dbSNP | Ensembl ].
    VAR_039153
    Natural varianti428 – 4281G → S.
    Corresponds to variant rs10980419 [ dbSNP | Ensembl ].
    VAR_039154
    Natural varianti507 – 5071V → I.
    Corresponds to variant rs872665 [ dbSNP | Ensembl ].
    VAR_039155
    Natural varianti581 – 5811Q → H.
    Corresponds to variant rs10817033 [ dbSNP | Ensembl ].
    VAR_039156
    Natural varianti637 – 6371I → V.
    Corresponds to variant rs13286541 [ dbSNP | Ensembl ].
    VAR_039157
    Natural varianti899 – 8991K → R.
    Corresponds to variant rs10817025 [ dbSNP | Ensembl ].
    VAR_039158
    Natural varianti1157 – 11571I → V.
    Corresponds to variant rs7038903 [ dbSNP | Ensembl ].
    VAR_039159
    Natural varianti1330 – 13301L → M.
    Corresponds to variant rs10817021 [ dbSNP | Ensembl ].
    VAR_039160
    Natural varianti1416 – 14161K → Q.
    Corresponds to variant rs1889323 [ dbSNP | Ensembl ].
    VAR_039161
    Natural varianti1444 – 14441M → L.
    Corresponds to variant rs7863519 [ dbSNP | Ensembl ].
    VAR_039162
    Natural varianti1648 – 16481L → V.
    Corresponds to variant rs7852962 [ dbSNP | Ensembl ].
    VAR_039163
    Natural varianti1810 – 18101E → A.
    Corresponds to variant rs2986671 [ dbSNP | Ensembl ].
    VAR_039164
    Natural varianti1953 – 19531R → K.
    Corresponds to variant rs17204832 [ dbSNP | Ensembl ].
    VAR_039165
    Natural varianti2607 – 26071T → A.
    Corresponds to variant rs3802433 [ dbSNP | Ensembl ].
    VAR_039166
    Natural varianti2750 – 27501A → V.1 Publication
    Corresponds to variant rs7030192 [ dbSNP | Ensembl ].
    VAR_039167
    Natural varianti2922 – 29221I → V.
    Corresponds to variant rs16914996 [ dbSNP | Ensembl ].
    VAR_039168
    Natural varianti3161 – 31611F → I.1 Publication
    Corresponds to variant rs3739451 [ dbSNP | Ensembl ].
    VAR_039169
    Natural varianti3230 – 32301P → T.
    Corresponds to variant rs16914992 [ dbSNP | Ensembl ].
    VAR_039170
    Natural varianti3559 – 35591T → M.
    Corresponds to variant rs17204533 [ dbSNP | Ensembl ].
    VAR_039171

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 20742074Missing in isoform 3. 2 PublicationsVSP_031625Add
    BLAST
    Alternative sequencei868 – 8681P → N in isoform 2. 2 PublicationsVSP_031626
    Alternative sequencei869 – 35712703Missing in isoform 2. 2 PublicationsVSP_031627Add
    BLAST
    Alternative sequencei1547 – 35712025Missing in isoform 4. 1 PublicationVSP_031628Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ619977 mRNA. Translation: CAF04067.1.
    AY916667 mRNA. Translation: AAX12481.1.
    AK023591 mRNA. Translation: BAB14617.1. Different initiation.
    AK075235 mRNA. Translation: BAC11489.1.
    AK027870 mRNA. Translation: BAB55420.1. Different initiation.
    AL158158 Genomic DNA. Translation: CAI14071.1.
    AL592463, AL354982 Genomic DNA. Translation: CAH73557.1. Different initiation.
    AL592463, AL158158, AL354982 Genomic DNA. Translation: CAH73558.1. Sequence problems.
    AL354982, AL592463 Genomic DNA. Translation: CAH74138.1. Different initiation.
    AL354982, AL158158, AL592463 Genomic DNA. Translation: CAH74139.1. Sequence problems.
    AL158158, AL354982, AL592463 Genomic DNA. Translation: CAI14068.1. Sequence problems.
    BC030816 mRNA. Translation: AAH30816.1.
    BX537918 mRNA. Translation: CAD97901.1.
    BX538049 mRNA. Translation: CAD97988.1.
    AF308289 mRNA. Translation: AAG48257.1. Sequence problems.
    CCDSiCCDS48004.1. [Q4LDE5-1]
    RefSeqiNP_699197.3. NM_153366.3. [Q4LDE5-1]
    UniGeneiHs.522334.
    Hs.726867.

    Genome annotation databases

    EnsembliENST00000297826; ENSP00000297826; ENSG00000165124. [Q4LDE5-3]
    ENST00000401783; ENSP00000384917; ENSG00000165124. [Q4LDE5-1]
    GeneIDi79987.
    KEGGihsa:79987.
    UCSCiuc004beu.2. human. [Q4LDE5-2]
    uc010mty.3. human. [Q4LDE5-3]
    uc010mtz.3. human. [Q4LDE5-1]
    uc010mua.1. human. [Q4LDE5-4]

    Polymorphism databases

    DMDMi296452942.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ619977 mRNA. Translation: CAF04067.1 .
    AY916667 mRNA. Translation: AAX12481.1 .
    AK023591 mRNA. Translation: BAB14617.1 . Different initiation.
    AK075235 mRNA. Translation: BAC11489.1 .
    AK027870 mRNA. Translation: BAB55420.1 . Different initiation.
    AL158158 Genomic DNA. Translation: CAI14071.1 .
    AL592463 , AL354982 Genomic DNA. Translation: CAH73557.1 . Different initiation.
    AL592463 , AL158158 , AL354982 Genomic DNA. Translation: CAH73558.1 . Sequence problems.
    AL354982 , AL592463 Genomic DNA. Translation: CAH74138.1 . Different initiation.
    AL354982 , AL158158 , AL592463 Genomic DNA. Translation: CAH74139.1 . Sequence problems.
    AL158158 , AL354982 , AL592463 Genomic DNA. Translation: CAI14068.1 . Sequence problems.
    BC030816 mRNA. Translation: AAH30816.1 .
    BX537918 mRNA. Translation: CAD97901.1 .
    BX538049 mRNA. Translation: CAD97988.1 .
    AF308289 mRNA. Translation: AAG48257.1 . Sequence problems.
    CCDSi CCDS48004.1. [Q4LDE5-1 ]
    RefSeqi NP_699197.3. NM_153366.3. [Q4LDE5-1 ]
    UniGenei Hs.522334.
    Hs.726867.

    3D structure databases

    ProteinModelPortali Q4LDE5.
    SMRi Q4LDE5. Positions 79-255, 313-507, 1195-1420, 1445-3563.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 123051. 4 interactions.
    IntActi Q4LDE5. 12 interactions.
    MINTi MINT-1197821.

    PTM databases

    PhosphoSitei Q4LDE5.

    Polymorphism databases

    DMDMi 296452942.

    Proteomic databases

    MaxQBi Q4LDE5.
    PaxDbi Q4LDE5.
    PRIDEi Q4LDE5.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000297826 ; ENSP00000297826 ; ENSG00000165124 . [Q4LDE5-3 ]
    ENST00000401783 ; ENSP00000384917 ; ENSG00000165124 . [Q4LDE5-1 ]
    GeneIDi 79987.
    KEGGi hsa:79987.
    UCSCi uc004beu.2. human. [Q4LDE5-2 ]
    uc010mty.3. human. [Q4LDE5-3 ]
    uc010mtz.3. human. [Q4LDE5-1 ]
    uc010mua.1. human. [Q4LDE5-4 ]

    Organism-specific databases

    CTDi 79987.
    GeneCardsi GC09M113127.
    H-InvDB HIX0008277.
    HIX0035094.
    HGNCi HGNC:15985. SVEP1.
    HPAi HPA020610.
    HPA021520.
    MIMi 611691. gene.
    neXtProti NX_Q4LDE5.
    PharmGKBi PA25971.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG12793.
    HOVERGENi HBG108523.
    KOi K17495.
    OMAi IDCRLED.
    OrthoDBi EOG7BS48H.
    PhylomeDBi Q4LDE5.
    TreeFami TF342247.

    Miscellaneous databases

    GenomeRNAii 79987.
    NextBioi 70034.
    PROi Q4LDE5.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q4LDE5.
    Bgeei Q4LDE5.
    Genevestigatori Q4LDE5.

    Family and domain databases

    Gene3Di 2.40.155.10. 1 hit.
    2.60.120.200. 1 hit.
    3.40.50.410. 1 hit.
    InterProi IPR008985. ConA-like_lec_gl_sf.
    IPR013320. ConA-like_subgrp.
    IPR000742. EG-like_dom.
    IPR001881. EGF-like_Ca-bd_dom.
    IPR013032. EGF-like_CS.
    IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
    IPR018097. EGF_Ca-bd_CS.
    IPR023413. GFP_like.
    IPR009030. Growth_fac_rcpt_N_dom.
    IPR003410. Hyalin.
    IPR001759. Pentaxin.
    IPR000436. Sushi_SCR_CCP.
    IPR011641. Tyr-kin_ephrin_A/B_rcpt-like.
    IPR002035. VWF_A.
    [Graphical view ]
    Pfami PF00008. EGF. 5 hits.
    PF07645. EGF_CA. 1 hit.
    PF07699. GCC2_GCC3. 4 hits.
    PF12661. hEGF. 1 hit.
    PF02494. HYR. 2 hits.
    PF00354. Pentaxin. 1 hit.
    PF00084. Sushi. 32 hits.
    PF00092. VWA. 1 hit.
    [Graphical view ]
    PRINTSi PR00895. PENTAXIN.
    SMARTi SM00032. CCP. 34 hits.
    SM00181. EGF. 4 hits.
    SM00179. EGF_CA. 6 hits.
    SM00327. VWA. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49899. SSF49899. 1 hit.
    SSF53300. SSF53300. 1 hit.
    SSF57184. SSF57184. 3 hits.
    SSF57535. SSF57535. 33 hits.
    PROSITEi PS00010. ASX_HYDROXYL. 6 hits.
    PS00022. EGF_1. 9 hits.
    PS01186. EGF_2. 11 hits.
    PS50026. EGF_3. 9 hits.
    PS01187. EGF_CA. 6 hits.
    PS50825. HYR. 2 hits.
    PS50923. SUSHI. 34 hits.
    PS50234. VWFA. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular and cellular characterization of SEL-OB/SVEP1 in osteogenic cells in vivo and in vitro."
      Shur I., Socher R., Hameiri M., Fried A., Benayahu D.
      J. Cell. Physiol. 206:420-427(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    2. Han J., Fang Y., Yan J., Ye Q.
      Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
      Tissue: Mammary gland.
    3. "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] (ISOFORM 3), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 195-3571 (ISOFORM 4), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 318-868 (ISOFORM 2), VARIANTS ALA-332 AND VAL-2750.
      Tissue: Placenta.
    4. "DNA sequence and analysis of human chromosome 9."
      Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
      , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
      Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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 2).
      Tissue: Placenta.
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2131-3571, VARIANT ILE-3161.
      Tissue: Colon endothelium.
    7. "Humoral immunity to human breast cancer: antigen definition and quantitative analysis of mRNA expression."
      Scanlan M.J., Gout I., Gordon C.M., Williamson B., Stockert E., Gure A.O., Jaeger D., Chen Y.-T., Mackay A., O'Hare M.J., Old L.J.
      Cancer Immun. 1:4-4(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2269-2756.
      Tissue: Mammary gland.
    8. "Polydom: a secreted protein with pentraxin, complement control protein, epidermal growth factor and von Willebrand factor A domains."
      Gilges D., Vinit M.-A., Callebaut I., Coulombel L., Cacheux V., Romeo P.-H., Vigon I.
      Biochem. J. 352:49-59(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    9. "Human urinary glycoproteomics; attachment site specific analysis of N-and O-linked glycosylations by CID and ECD."
      Halim A., Nilsson J., Ruetschi U., Hesse C., Larson G.
      Mol. Cell. Proteomics 0:0-0(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION, STRUCTURE OF CARBOHYDRATES, IDENTIFICATION BY MASS SPECTROMETRY.

    Entry informationi

    Entry nameiSVEP1_HUMAN
    AccessioniPrimary (citable) accession number: Q4LDE5
    Secondary accession number(s): Q0P675
    , Q5D213, Q5T938, Q5VTE4, Q5VTE5, Q7Z387, Q7Z3G3, Q8NBT9, Q96JU7, Q9H284, Q9H8J9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 26, 2008
    Last sequence update: May 18, 2010
    Last modified: October 1, 2014
    This is version 94 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 9
      Human chromosome 9: 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