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Protein

Signal peptide, CUB and EGF-like domain-containing protein 1

Gene

SCUBE1

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

Functioni

Could function as an adhesive molecule and its matrix bound and soluble fragments may play a critical role in vascular biology.1 Publication

GO - Molecular functioni

  • calcium ion binding Source: UniProtKB
  • identical protein binding Source: MGI
  • protein heterodimerization activity Source: UniProtKB

GO - Biological processi

  • adult heart development Source: UniProtKB
  • blood coagulation Source: UniProtKB
  • endothelial cell differentiation Source: UniProtKB
  • inflammatory response Source: UniProtKB
  • post-embryonic development Source: UniProtKB
  • protein homooligomerization Source: UniProtKB
Complete GO annotation...

Keywords - Ligandi

Calcium

Names & Taxonomyi

Protein namesi
Recommended name:
Signal peptide, CUB and EGF-like domain-containing protein 1
Gene namesi
Name:SCUBE1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 22

Organism-specific databases

HGNCiHGNC:13441. SCUBE1.

Subcellular locationi

GO - Cellular componenti

  • cell surface Source: UniProtKB
  • external side of plasma membrane Source: UniProtKB
  • extracellular space Source: MGI
  • extrinsic component of plasma membrane Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane, Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA35019.

Polymorphism and mutation databases

BioMutaiSCUBE1.
DMDMi145559527.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2323Sequence analysisAdd
BLAST
Chaini24 – 988965Signal peptide, CUB and EGF-like domain-containing protein 1PRO_0000254648Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi37 ↔ 50By similarity
Disulfide bondi44 ↔ 59By similarity
Disulfide bondi61 ↔ 72By similarity
Disulfide bondi78 ↔ 91By similarity
Disulfide bondi87 ↔ 100By similarity
Disulfide bondi102 ↔ 115By similarity
Disulfide bondi121 ↔ 132By similarity
Disulfide bondi128 ↔ 141By similarity
Disulfide bondi286 ↔ 297By similarity
Disulfide bondi293 ↔ 306By similarity
Disulfide bondi308 ↔ 321By similarity
Disulfide bondi327 ↔ 337By similarity
Disulfide bondi333 ↔ 346By similarity
Disulfide bondi348 ↔ 360By similarity
Disulfide bondi366 ↔ 377By similarity
Glycosylationi370 – 3701N-linked (GlcNAc...)Sequence analysis
Disulfide bondi373 ↔ 386By similarity
Disulfide bondi388 ↔ 401By similarity
Glycosylationi466 – 4661N-linked (GlcNAc...)Sequence analysis
Glycosylationi679 – 6791N-linked (GlcNAc...)Sequence analysis
Glycosylationi750 – 7501N-linked (GlcNAc...)Sequence analysis
Glycosylationi779 – 7791N-linked (GlcNAc...)Sequence analysis
Glycosylationi789 – 7891N-linked (GlcNAc...)Sequence analysis
Disulfide bondi798 ↔ 824By similarity
Disulfide bondi851 ↔ 872By similarity

Post-translational modificationi

N-glycosylated.1 Publication
Could be proteolytically cleaved to release a smaller active fragment.

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ8IWY4.
PRIDEiQ8IWY4.

PTM databases

iPTMnetiQ8IWY4.
PhosphoSiteiQ8IWY4.

Expressioni

Tissue specificityi

Detected in endothelial cells. Highly expressed in platelets. Stored in platelet alpha granules, and transferred to the cell surface upon activation and aggregation. A smaller form, probably produced by limited proteolysis, after being released from the storage granules, is associated with thrombus and localized with the subendothelial matrices in atherosclerotic plaques.2 Publications

Inductioni

Down-regulated by inflammatory cytokines.

Gene expression databases

BgeeiQ8IWY4.
CleanExiHS_SCUBE1.
ExpressionAtlasiQ8IWY4. baseline and differential.
GenevisibleiQ8IWY4. HS.

Organism-specific databases

HPAiHPA003190.

Interactioni

Subunit structurei

Forms homooligomers and heterooligomers with SCUBE2 and SCUBE3.By similarity

GO - Molecular functioni

  • identical protein binding Source: MGI
  • protein heterodimerization activity Source: UniProtKB

Protein-protein interaction databases

STRINGi9606.ENSP00000354080.

Structurei

3D structure databases

ProteinModelPortaliQ8IWY4.
SMRiQ8IWY4. Positions 33-405, 798-907.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini33 – 7341EGF-like 1; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini74 – 11643EGF-like 2; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini117 – 15337EGF-like 3; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini166 – 20237EGF-like 4PROSITE-ProRule annotationAdd
BLAST
Domaini206 – 24136EGF-like 5PROSITE-ProRule annotationAdd
BLAST
Domaini245 – 28036EGF-like 6PROSITE-ProRule annotationAdd
BLAST
Domaini282 – 32241EGF-like 7; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini323 – 36139EGF-like 8; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini362 – 40241EGF-like 9; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini798 – 910113CUBPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 CUB domain.PROSITE-ProRule annotation
Contains 9 EGF-like domains.PROSITE-ProRule annotation

Keywords - Domaini

EGF-like domain, Repeat, Signal

Phylogenomic databases

eggNOGiENOG410IR7D. Eukaryota.
ENOG411030G. LUCA.
GeneTreeiENSGT00810000125382.
HOGENOMiHOG000230943.
HOVERGENiHBG054902.
InParanoidiQ8IWY4.
OMAiAPPIKQK.
OrthoDBiEOG7P8P71.
PhylomeDBiQ8IWY4.
TreeFamiTF351672.

Family and domain databases

Gene3Di2.60.120.290. 1 hit.
InterProiIPR026823. cEGF.
IPR000859. CUB_dom.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR024731. EGF_dom.
IPR009030. Growth_fac_rcpt_.
IPR011641. Tyr-kin_ephrin_A/B_rcpt-like.
[Graphical view]
PfamiPF12662. cEGF. 1 hit.
PF00431. CUB. 1 hit.
PF12947. EGF_3. 1 hit.
PF07645. EGF_CA. 2 hits.
PF07699. Ephrin_rec_like. 3 hits.
[Graphical view]
SMARTiSM00042. CUB. 1 hit.
SM00181. EGF. 10 hits.
SM00179. EGF_CA. 7 hits.
SM01411. Ephrin_rec_like. 3 hits.
[Graphical view]
SUPFAMiSSF49854. SSF49854. 1 hit.
SSF57184. SSF57184. 3 hits.
PROSITEiPS00010. ASX_HYDROXYL. 6 hits.
PS01180. CUB. 1 hit.
PS01186. EGF_2. 7 hits.
PS50026. EGF_3. 6 hits.
PS01187. EGF_CA. 6 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q8IWY4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGAAAVRWHL CVLLALGTRG RLAGGSGLPG SVDVDECSEG TDDCHIDAIC
60 70 80 90 100
QNTPKSYKCL CKPGYKGEGK QCEDIDECEN DYYNGGCVHE CINIPGNYRC
110 120 130 140 150
TCFDGFMLAH DGHNCLDVDE CQDNNGGCQQ ICVNAMGSYE CQCHSGFFLS
160 170 180 190 200
DNQHTCIHRS NEGMNCMNKD HGCAHICRET PKGGVACDCR PGFDLAQNQK
210 220 230 240 250
DCTLTCNYGN GGCQHSCEDT DTGPTCGCHQ KYALHSDGRT CIETCAVNNG
260 270 280 290 300
GCDRTCKDTA TGVRCSCPVG FTLQPDGKTC KDINECLVNN GGCDHFCRNT
310 320 330 340 350
VGSFECGCRK GYKLLTDERT CQDIDECSFE RTCDHICINS PGSFQCLCHR
360 370 380 390 400
GYILYGTTHC GDVDECSMSN GSCDQGCVNT KGSYECVCPP GRRLHWNGKD
410 420 430 440 450
CVETGKCLSR AKTSPRAQLS CSKAGGVESC FLSCPAHTLF VPDSENSYVL
460 470 480 490 500
SCGVPGPQGK ALQKRNGTSS GLGPSCSDAP TTPIKQKARF KIRDAKCHLR
510 520 530 540 550
PHSQARAKET ARQPLLDHCH VTFVTLKCDS SKKRRRGRKS PSKEVSHITA
560 570 580 590 600
EFEIETKMEE ASDTCEADCL RKRAEQSLQA AIKTLRKSIG RQQFYVQVSG
610 620 630 640 650
TEYEVAQRPA KALEGQGACG AGQVLQDSKC VACGPGTHFG GELGQCVSCM
660 670 680 690 700
PGTYQDMEGQ LSCTPCPSSD GLGLPGARNV SECGGQCSPG FFSADGFKPC
710 720 730 740 750
QACPVGTYQP EPGRTGCFPC GGGLLTKHEG TTSFQDCEAK VHCSPGHHYN
760 770 780 790 800
TTTHRCIRCP VGTYQPEFGQ NHCITCPGNT STDFDGSTNV THCKNQHCGG
810 820 830 840 850
ELGDYTGYIE SPNYPGDYPA NAECVWHIAP PPKRRILIVV PEIFLPIEDE
860 870 880 890 900
CGDVLVMRKS ASPTSITTYE TCQTYERPIA FTSRSRKLWI QFKSNEGNSG
910 920 930 940 950
KGFQVPYVTY DEDYQQLIED IVRDGRLYAS ENHQEILKDK KLIKALFDVL
960 970 980
AHPQNYFKYT AQESKEMFPR SFIKLLRSKV SRFLRPYK
Length:988
Mass (Da):107,910
Last modified:April 17, 2007 - v3
Checksum:iAB2C2AB53F3D3C2B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti53 – 531T → A in AAN77133 (PubMed:12270931).Curated
Sequence conflicti73 – 731E → G in AAN77133 (PubMed:12270931).Curated
Sequence conflicti234 – 2341L → P in AAN77133 (PubMed:12270931).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti398 – 3981G → R.1 Publication
Corresponds to variant rs129415 [ dbSNP | Ensembl ].
VAR_028850
Natural varianti648 – 6481S → P.1 Publication
Corresponds to variant rs138993 [ dbSNP | Ensembl ].
VAR_028851

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF525689 mRNA. Translation: AAN77133.1.
Z99756, Z82214 Genomic DNA. Translation: CAI18854.1.
Z82214, Z99756 Genomic DNA. Translation: CAI21674.1.
CCDSiCCDS14048.1.
RefSeqiNP_766638.2. NM_173050.3.
UniGeneiHs.133995.

Genome annotation databases

EnsembliENST00000360835; ENSP00000354080; ENSG00000159307.
GeneIDi80274.
KEGGihsa:80274.
UCSCiuc003bdt.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF525689 mRNA. Translation: AAN77133.1.
Z99756, Z82214 Genomic DNA. Translation: CAI18854.1.
Z82214, Z99756 Genomic DNA. Translation: CAI21674.1.
CCDSiCCDS14048.1.
RefSeqiNP_766638.2. NM_173050.3.
UniGeneiHs.133995.

3D structure databases

ProteinModelPortaliQ8IWY4.
SMRiQ8IWY4. Positions 33-405, 798-907.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9606.ENSP00000354080.

PTM databases

iPTMnetiQ8IWY4.
PhosphoSiteiQ8IWY4.

Polymorphism and mutation databases

BioMutaiSCUBE1.
DMDMi145559527.

Proteomic databases

PaxDbiQ8IWY4.
PRIDEiQ8IWY4.

Protocols and materials databases

DNASUi80274.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000360835; ENSP00000354080; ENSG00000159307.
GeneIDi80274.
KEGGihsa:80274.
UCSCiuc003bdt.3. human.

Organism-specific databases

CTDi80274.
GeneCardsiSCUBE1.
H-InvDBHIX0027842.
HGNCiHGNC:13441. SCUBE1.
HPAiHPA003190.
MIMi611746. gene.
neXtProtiNX_Q8IWY4.
PharmGKBiPA35019.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IR7D. Eukaryota.
ENOG411030G. LUCA.
GeneTreeiENSGT00810000125382.
HOGENOMiHOG000230943.
HOVERGENiHBG054902.
InParanoidiQ8IWY4.
OMAiAPPIKQK.
OrthoDBiEOG7P8P71.
PhylomeDBiQ8IWY4.
TreeFamiTF351672.

Miscellaneous databases

GenomeRNAii80274.
NextBioi70745.
PROiQ8IWY4.
SOURCEiSearch...

Gene expression databases

BgeeiQ8IWY4.
CleanExiHS_SCUBE1.
ExpressionAtlasiQ8IWY4. baseline and differential.
GenevisibleiQ8IWY4. HS.

Family and domain databases

Gene3Di2.60.120.290. 1 hit.
InterProiIPR026823. cEGF.
IPR000859. CUB_dom.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR024731. EGF_dom.
IPR009030. Growth_fac_rcpt_.
IPR011641. Tyr-kin_ephrin_A/B_rcpt-like.
[Graphical view]
PfamiPF12662. cEGF. 1 hit.
PF00431. CUB. 1 hit.
PF12947. EGF_3. 1 hit.
PF07645. EGF_CA. 2 hits.
PF07699. Ephrin_rec_like. 3 hits.
[Graphical view]
SMARTiSM00042. CUB. 1 hit.
SM00181. EGF. 10 hits.
SM00179. EGF_CA. 7 hits.
SM01411. Ephrin_rec_like. 3 hits.
[Graphical view]
SUPFAMiSSF49854. SSF49854. 1 hit.
SSF57184. SSF57184. 3 hits.
PROSITEiPS00010. ASX_HYDROXYL. 6 hits.
PS01180. CUB. 1 hit.
PS01186. EGF_2. 7 hits.
PS50026. EGF_3. 6 hits.
PS01187. EGF_CA. 6 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of a novel family of cell-surface proteins expressed in human vascular endothelium."
    Yang R.-B., Ng C.K.D., Wasserman S.M., Colman S.D., Shenoy S., Mehraban F., Koemueves L.G., Tomlinson J.E., Topper J.N.
    J. Biol. Chem. 277:46364-46373(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS ARG-398 AND PRO-648, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, GLYCOSYLATION.
  2. "The DNA sequence of human chromosome 22."
    Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M.
    , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
    Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "Localization and characterization of a novel secreted protein SCUBE1 in human platelets."
    Tu C.-F., Su Y.-H., Huang Y.-N., Tsai M.-T., Li L.-T., Chen Y.-L., Cheng C.-J., Dai D.-F., Yang R.-B.
    Cardiovasc. Res. 71:486-495(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  4. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.

Entry informationi

Entry nameiSCUB1_HUMAN
AccessioniPrimary (citable) accession number: Q8IWY4
Secondary accession number(s): Q5R336
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: April 17, 2007
Last modified: May 11, 2016
This is version 110 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 22
    Human chromosome 22: 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.