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Protein

Insulin-like growth factor-binding protein 7

Gene

IGFBP7

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

Functioni

Binds IGF-I and IGF-II with a relatively low affinity. Stimulates prostacyclin (PGI2) production. Stimulates cell adhesion.2 Publications

GO - Biological processi

  • cell adhesion Source: UniProtKB
  • negative regulation of cell proliferation Source: ProtInc
  • regulation of cell growth Source: InterPro
Complete GO annotation...

Keywords - Biological processi

Cell adhesion

Keywords - Ligandi

Growth factor binding

Enzyme and pathway databases

ReactomeiREACT_169168. Senescence-Associated Secretory Phenotype (SASP).

Protein family/group databases

MEROPSiI43.001.

Names & Taxonomyi

Protein namesi
Recommended name:
Insulin-like growth factor-binding protein 7
Short name:
IBP-7
Short name:
IGF-binding protein 7
Short name:
IGFBP-7
Alternative name(s):
IGFBP-rP1
MAC25 protein
PGI2-stimulating factor
Prostacyclin-stimulating factor
Tumor-derived adhesion factor
Short name:
TAF
Gene namesi
Name:IGFBP7
Synonyms:MAC25, PSF
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 4

Organism-specific databases

HGNCiHGNC:5476. IGFBP7.

Subcellular locationi

GO - Cellular componenti

  • extracellular exosome Source: UniProtKB
  • extracellular region Source: Reactome
  • extracellular space Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Involvement in diseasei

Retinal arterial macroaneurysm with supravalvular pulmonic stenosis (RAMSVPS)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionAn autosomal recessive condition characterized by the bilateral appearance of 'beading' along the major retinal arterial trunks, with the subsequent formation of macroaneurysms. Affected individuals also have supravalvular pulmonic stenosis, often requiring surgical correction.

See also OMIM:614224

Organism-specific databases

MIMi614224. phenotype.
Orphaneti284247. Familial retinal arterial macroaneurysm.
PharmGKBiPA29709.

Chemistry

DrugBankiDB00030. Insulin Regular.

Polymorphism and mutation databases

BioMutaiIGFBP7.
DMDMi23396609.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 26263 PublicationsAdd
BLAST
Chaini27 – 282256Insulin-like growth factor-binding protein 7PRO_0000014392Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi171 – 1711N-linked (GlcNAc...)1 Publication
Disulfide bondi181 ↔ 248PROSITE-ProRule annotation

Post-translational modificationi

N-glycosylated.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiQ16270.
PaxDbiQ16270.
PeptideAtlasiQ16270.
PRIDEiQ16270.

PTM databases

PhosphoSiteiQ16270.

Expressioni

Gene expression databases

BgeeiQ16270.
CleanExiHS_IGFBP7.
GenevisibleiQ16270. HS.

Organism-specific databases

HPAiCAB020668.
HPA002196.

Interactioni

Subunit structurei

May interact with VPS24/CHMP3; the relevance of such interaction however remains unclear.

Protein-protein interaction databases

BioGridi109711. 9 interactions.
IntActiQ16270. 9 interactions.
MINTiMINT-7006618.
STRINGi9606.ENSP00000295666.

Structurei

3D structure databases

ProteinModelPortaliQ16270.
SMRiQ16270. Positions 35-154, 157-266.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini28 – 10679IGFBP N-terminalPROSITE-ProRule annotationAdd
BLAST
Domaini105 – 15854Kazal-likePROSITE-ProRule annotationAdd
BLAST
Domaini160 – 264105Ig-like C2-typeAdd
BLAST

Sequence similaritiesi

Contains 1 IGFBP N-terminal domain.PROSITE-ProRule annotation
Contains 1 Kazal-like domain.PROSITE-ProRule annotation

Keywords - Domaini

Immunoglobulin domain, Signal

Phylogenomic databases

eggNOGiNOG40288.
GeneTreeiENSGT00530000063555.
HOGENOMiHOG000261684.
HOVERGENiHBG031621.
InParanoidiQ16270.
OMAiHCAPGME.
OrthoDBiEOG7BW0M2.
PhylomeDBiQ16270.
TreeFamiTF331645.

Family and domain databases

Gene3Di2.60.40.10. 1 hit.
InterProiIPR009030. Growth_fac_rcpt_N_dom.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003599. Ig_sub.
IPR000867. IGFBP-like.
IPR011390. IGFBP_rP_mac25.
IPR002350. Kazal_dom.
[Graphical view]
PANTHERiPTHR14186. PTHR14186. 1 hit.
PfamiPF07679. I-set. 1 hit.
PF00219. IGFBP. 1 hit.
PF07648. Kazal_2. 1 hit.
[Graphical view]
PIRSFiPIRSF018239. IGFBP_rP_mac25. 1 hit.
SMARTiSM00121. IB. 1 hit.
SM00409. IG. 1 hit.
SM00280. KAZAL. 1 hit.
[Graphical view]
SUPFAMiSSF57184. SSF57184. 1 hit.
PROSITEiPS50835. IG_LIKE. 1 hit.
PS51323. IGFBP_N_2. 1 hit.
PS51465. KAZAL_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. AlignAdd to basket

Isoform 1 (identifier: Q16270-1) [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
MERPSLRALL LGAAGLLLLL LPLSSSSSSD TCGPCEPASC PPLPPLGCLL
60 70 80 90 100
GETRDACGCC PMCARGEGEP CGGGGAGRGY CAPGMECVKS RKRRKGKAGA
110 120 130 140 150
AAGGPGVSGV CVCKSRYPVC GSDGTTYPSG CQLRAASQRA ESRGEKAITQ
160 170 180 190 200
VSKGTCEQGP SIVTPPKDIW NVTGAQVYLS CEVIGIPTPV LIWNKVKRGH
210 220 230 240 250
YGVQRTELLP GDRDNLAIQT RGGPEKHEVT GWVLVSPLSK EDAGEYECHA
260 270 280
SNSQGQASAS AKITVVDALH EIPVKKGEGA EL
Length:282
Mass (Da):29,130
Last modified:November 1, 1996 - v1
Checksum:i75F96EBC3B444D37
GO
Isoform 2 (identifier: Q16270-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     278-282: EGAEL → TQ

Show »
Length:279
Mass (Da):28,860
Checksum:i3281F44D371F721E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti4 – 41P → A in AAA16187 (PubMed:7694637).Curated
Sequence conflicti13 – 131A → P in AAA16187 (PubMed:7694637).Curated
Sequence conflicti69 – 691E → G in BAH14453 (PubMed:14702039).Curated
Sequence conflicti273 – 28210PVKKGEGAEL → ASEKR in AAA16187 (PubMed:7694637).Curated

RNA editingi

Edited at positions 78 and 95.1 Publication
Partially edited. In the brain, position 78 is edited at about 55% and position 95 at about 31%.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti11 – 111L → F.2 Publications
Corresponds to variant rs11573021 [ dbSNP | Ensembl ].
VAR_018959
Natural varianti78 – 781R → G in RNA edited version.
VAR_063638
Natural varianti95 – 951K → R in RNA edited version.
VAR_063639

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei278 – 2825EGAEL → TQ in isoform 2. 1 PublicationVSP_045297

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L19182 mRNA. Translation: AAA16187.1.
S75725 mRNA. Translation: AAB32370.1.
AY518539 Genomic DNA. Translation: AAR89912.1.
BT006654 mRNA. Translation: AAP35300.1.
AK303915 mRNA. Translation: BAG64844.1.
AK316082 mRNA. Translation: BAH14453.1.
AC069307 Genomic DNA. No translation available.
AC111197 Genomic DNA. No translation available.
BC017201 mRNA. Translation: AAH17201.1.
BC066339 mRNA. Translation: AAH66339.1.
CCDSiCCDS3512.1. [Q16270-1]
CCDS58900.1. [Q16270-2]
PIRiI52825.
PC2030.
S50031.
RefSeqiNP_001240764.1. NM_001253835.1. [Q16270-2]
NP_001544.1. NM_001553.2. [Q16270-1]
UniGeneiHs.479808.
Hs.691061.

Genome annotation databases

EnsembliENST00000295666; ENSP00000295666; ENSG00000163453.
ENST00000514062; ENSP00000486293; ENSG00000163453. [Q16270-2]
GeneIDi3490.
KEGGihsa:3490.
UCSCiuc003hcn.3. human. [Q16270-1]
uc011cag.2. human.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism, RNA editing

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L19182 mRNA. Translation: AAA16187.1.
S75725 mRNA. Translation: AAB32370.1.
AY518539 Genomic DNA. Translation: AAR89912.1.
BT006654 mRNA. Translation: AAP35300.1.
AK303915 mRNA. Translation: BAG64844.1.
AK316082 mRNA. Translation: BAH14453.1.
AC069307 Genomic DNA. No translation available.
AC111197 Genomic DNA. No translation available.
BC017201 mRNA. Translation: AAH17201.1.
BC066339 mRNA. Translation: AAH66339.1.
CCDSiCCDS3512.1. [Q16270-1]
CCDS58900.1. [Q16270-2]
PIRiI52825.
PC2030.
S50031.
RefSeqiNP_001240764.1. NM_001253835.1. [Q16270-2]
NP_001544.1. NM_001553.2. [Q16270-1]
UniGeneiHs.479808.
Hs.691061.

3D structure databases

ProteinModelPortaliQ16270.
SMRiQ16270. Positions 35-154, 157-266.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109711. 9 interactions.
IntActiQ16270. 9 interactions.
MINTiMINT-7006618.
STRINGi9606.ENSP00000295666.

Chemistry

DrugBankiDB00030. Insulin Regular.

Protein family/group databases

MEROPSiI43.001.

PTM databases

PhosphoSiteiQ16270.

Polymorphism and mutation databases

BioMutaiIGFBP7.
DMDMi23396609.

Proteomic databases

MaxQBiQ16270.
PaxDbiQ16270.
PeptideAtlasiQ16270.
PRIDEiQ16270.

Protocols and materials databases

DNASUi3490.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000295666; ENSP00000295666; ENSG00000163453.
ENST00000514062; ENSP00000486293; ENSG00000163453. [Q16270-2]
GeneIDi3490.
KEGGihsa:3490.
UCSCiuc003hcn.3. human. [Q16270-1]
uc011cag.2. human.

Organism-specific databases

CTDi3490.
GeneCardsiGC04M057897.
HGNCiHGNC:5476. IGFBP7.
HPAiCAB020668.
HPA002196.
MIMi602867. gene.
614224. phenotype.
neXtProtiNX_Q16270.
Orphaneti284247. Familial retinal arterial macroaneurysm.
PharmGKBiPA29709.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG40288.
GeneTreeiENSGT00530000063555.
HOGENOMiHOG000261684.
HOVERGENiHBG031621.
InParanoidiQ16270.
OMAiHCAPGME.
OrthoDBiEOG7BW0M2.
PhylomeDBiQ16270.
TreeFamiTF331645.

Enzyme and pathway databases

ReactomeiREACT_169168. Senescence-Associated Secretory Phenotype (SASP).

Miscellaneous databases

ChiTaRSiIGFBP7. human.
GeneWikiiIGFBP7.
GenomeRNAii3490.
NextBioi13726.
PROiQ16270.
SOURCEiSearch...

Gene expression databases

BgeeiQ16270.
CleanExiHS_IGFBP7.
GenevisibleiQ16270. HS.

Family and domain databases

Gene3Di2.60.40.10. 1 hit.
InterProiIPR009030. Growth_fac_rcpt_N_dom.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003599. Ig_sub.
IPR000867. IGFBP-like.
IPR011390. IGFBP_rP_mac25.
IPR002350. Kazal_dom.
[Graphical view]
PANTHERiPTHR14186. PTHR14186. 1 hit.
PfamiPF07679. I-set. 1 hit.
PF00219. IGFBP. 1 hit.
PF07648. Kazal_2. 1 hit.
[Graphical view]
PIRSFiPIRSF018239. IGFBP_rP_mac25. 1 hit.
SMARTiSM00121. IB. 1 hit.
SM00409. IG. 1 hit.
SM00280. KAZAL. 1 hit.
[Graphical view]
SUPFAMiSSF57184. SSF57184. 1 hit.
PROSITEiPS50835. IG_LIKE. 1 hit.
PS51323. IGFBP_N_2. 1 hit.
PS51465. KAZAL_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification and characterization of genes differentially expressed in meningiomas."
    Murphy M., Pykett M.J., Harnish P., Zang K.D., George D.L.
    Cell Growth Differ. 4:715-722(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT PHE-11, RNA EDITING OF POSITION 95.
    Tissue: Leptomeninges.
  2. "Purification and molecular cloning of prostacyclin-stimulating factor from serum-free conditioned medium of human diploid fibroblast cells."
    Yamauchi T., Umeda F., Masakado M., Isaji M., Mizushima S., Nawata H.
    Biochem. J. 303:591-598(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  3. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  4. NIEHS SNPs program
    Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT PHE-11.
  5. "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 2).
    Tissue: Thalamus and Trachea.
  6. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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).
    Tissue: Testis and Uterus.
  8. "Cell adhesion activity of a 30-kDa major secreted protein from human bladder carcinoma cells."
    Akaogi K., Okabe Y., Funahashi K., Yoshitake Y., Nishikawa K., Yasumitsu H., Umeda M., Miyazaki K.
    Biochem. Biophys. Res. Commun. 198:1046-1053(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 27-46, FUNCTION.
    Tissue: Urinary bladder carcinoma.
  9. "Signal peptide prediction based on analysis of experimentally verified cleavage sites."
    Zhang Z., Henzel W.J.
    Protein Sci. 13:2819-2824(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 27-41.
  10. "Synthesis and characterization of insulin-like growth factor-binding protein (IGFBP)-7. Recombinant human mac25 protein specifically binds IGF-I and -II."
    Oh Y., Nagalla S.R., Yamanaka Y., Kim H.-S., Wilson E., Rosenfeld R.G.
    J. Biol. Chem. 271:30322-30325(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 27-36, FUNCTION, GLYCOSYLATION.
  11. "Interaction of IGF-binding protein-related protein 1 with a novel protein, neuroendocrine differentiation factor, results in neuroendocrine differentiation of prostate cancer cells."
    Wilson E.M., Oh Y., Hwa V., Rosenfeld R.G.
    J. Clin. Endocrinol. Metab. 86:4504-4511(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: POSSIBLE INTERACTION WITH CHMP3.
  12. "Screening of human SNP database identifies recoding sites of A-to-I RNA editing."
    Gommans W.M., Tatalias N.E., Sie C.P., Dupuis D., Vendetti N., Smith L., Kaushal R., Maas S.
    RNA 14:2074-2085(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: RNA EDITING OF POSITIONS 78 AND 95.
  13. "Mutation of IGFBP7 causes upregulation of BRAF/MEK/ERK pathway and familial retinal arterial macroaneurysms."
    Abu-Safieh L., Abboud E.B., Alkuraya H., Shamseldin H., Al-Enzi S., Al-Abdi L., Hashem M., Colak D., Jarallah A., Ahmad H., Bobis S., Nemer G., Bitar F., Alkuraya F.S.
    Am. J. Hum. Genet. 89:313-319(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN RAMSVPS.

Entry informationi

Entry nameiIBP7_HUMAN
AccessioniPrimary (citable) accession number: Q16270
Secondary accession number(s): B4E1N2
, B7Z9W7, Q07822, Q53YE6, Q9UCA8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 19, 2002
Last sequence update: November 1, 1996
Last modified: July 22, 2015
This is version 148 of the entry and version 1 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 4
    Human chromosome 4: 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

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 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.