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Q16270 (IBP7_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 136. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:IGFBP7
Synonyms:MAC25, PSF
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length282 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Binds IGF-I and IGF-II with a relatively low affinity. Stimulates prostacyclin (PGI2) production. Stimulates cell adhesion. Ref.8 Ref.10

Subunit structure

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

Subcellular location

Secreted.

Post-translational modification

N-glycosylated. Ref.10

Involvement in disease

Retinal arterial macroaneurysm with supravalvular pulmonic stenosis (RAMSVPS) [MIM:614224]: An 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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.13

Sequence similarities

Contains 1 Ig-like C2-type (immunoglobulin-like) domain.

Contains 1 IGFBP N-terminal domain.

Contains 1 Kazal-like domain.

RNA editing

Edited at positions 78 and 95.
Partially edited. In the brain, position 78 is edited at about 55% and position 95 at about 31%. Ref.1 Ref.12

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q16270-1)

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.
Isoform 2 (identifier: Q16270-2)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2626 Ref.8 Ref.9 Ref.10
Chain27 – 282256Insulin-like growth factor-binding protein 7
PRO_0000014392

Regions

Domain28 – 10679IGFBP N-terminal
Domain105 – 15854Kazal-like
Domain160 – 264105Ig-like C2-type

Amino acid modifications

Glycosylation1711N-linked (GlcNAc...) Probable
Disulfide bond181 ↔ 248 By similarity

Natural variations

Alternative sequence278 – 2825EGAEL → TQ in isoform 2.
VSP_045297
Natural variant111L → F. Ref.1 Ref.4
Corresponds to variant rs11573021 [ dbSNP | Ensembl ].
VAR_018959
Natural variant781R → G in RNA edited version.
VAR_063638
Natural variant951K → R in RNA edited version.
VAR_063639

Experimental info

Sequence conflict41P → A in AAA16187. Ref.1
Sequence conflict131A → P in AAA16187. Ref.1
Sequence conflict691E → G in BAH14453. Ref.5
Sequence conflict273 – 28210PVKKGEGAEL → ASEKR in AAA16187. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 75F96EBC3B444D37

FASTA28229,130
        10         20         30         40         50         60 
MERPSLRALL LGAAGLLLLL LPLSSSSSSD TCGPCEPASC PPLPPLGCLL GETRDACGCC 

        70         80         90        100        110        120 
PMCARGEGEP CGGGGAGRGY CAPGMECVKS RKRRKGKAGA AAGGPGVSGV CVCKSRYPVC 

       130        140        150        160        170        180 
GSDGTTYPSG CQLRAASQRA ESRGEKAITQ VSKGTCEQGP SIVTPPKDIW NVTGAQVYLS 

       190        200        210        220        230        240 
CEVIGIPTPV LIWNKVKRGH YGVQRTELLP GDRDNLAIQT RGGPEKHEVT GWVLVSPLSK 

       250        260        270        280 
EDAGEYECHA SNSQGQASAS AKITVVDALH EIPVKKGEGA EL 

« Hide

Isoform 2 [UniParc].

Checksum: 3281F44D371F721E
Show »

FASTA27928,860

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRI52825.
PC2030.
S50031.
RefSeqNP_001240764.1. NM_001253835.1.
NP_001544.1. NM_001553.2.
UniGeneHs.479808.
Hs.691061.

3D structure databases

ProteinModelPortalQ16270.
SMRQ16270. Positions 35-271.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109711. 10 interactions.
IntActQ16270. 9 interactions.
MINTMINT-7006618.
STRING9606.ENSP00000295666.

Chemistry

DrugBankDB00047. Insulin Glargine recombinant.
DB00046. Insulin Lyspro recombinant.
DB00030. Insulin recombinant.
DB00071. Insulin, porcine.

Protein family/group databases

MEROPSI43.001.

PTM databases

PhosphoSiteQ16270.

Polymorphism databases

DMDM23396609.

Proteomic databases

PaxDbQ16270.
PeptideAtlasQ16270.
PRIDEQ16270.

Protocols and materials databases

DNASU3490.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000295666; ENSP00000295666; ENSG00000163453. [Q16270-1]
ENST00000537922; ENSP00000444146; ENSG00000163453. [Q16270-2]
GeneID3490.
KEGGhsa:3490.
UCSCuc003hcn.3. human. [Q16270-1]
uc011cag.2. human.

Organism-specific databases

CTD3490.
GeneCardsGC04M057897.
HGNCHGNC:5476. IGFBP7.
HPACAB020668.
HPA002196.
MIM602867. gene.
614224. phenotype.
neXtProtNX_Q16270.
Orphanet284247. Familial retinal arterial macroaneurysm.
PharmGKBPA29709.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG40288.
HOGENOMHOG000261684.
HOVERGENHBG031621.
InParanoidQ16270.
OMAHCAPGME.
OrthoDBEOG7BW0M2.
PhylomeDBQ16270.
TreeFamTF331645.

Enzyme and pathway databases

ReactomeREACT_120956. Cellular responses to stress.

Gene expression databases

BgeeQ16270.
CleanExHS_IGFBP7.
GenevestigatorQ16270.

Family and domain databases

Gene3D2.60.40.10. 1 hit.
InterProIPR009030. 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]
PANTHERPTHR14186. PTHR14186. 1 hit.
PfamPF07679. I-set. 1 hit.
PF00219. IGFBP. 1 hit.
PF07648. Kazal_2. 1 hit.
[Graphical view]
PIRSFPIRSF018239. IGFBP_rP_mac25. 1 hit.
SMARTSM00121. IB. 1 hit.
SM00409. IG. 1 hit.
SM00280. KAZAL. 1 hit.
[Graphical view]
SUPFAMSSF57184. SSF57184. 1 hit.
PROSITEPS50835. IG_LIKE. 1 hit.
PS51323. IGFBP_N_2. 1 hit.
PS51465. KAZAL_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSIGFBP7. human.
GeneWikiIGFBP7.
GenomeRNAi3490.
NextBio13726.
PROQ16270.
SOURCESearch...

Entry information

Entry nameIBP7_HUMAN
AccessionPrimary (citable) accession number: Q16270
Secondary accession number(s): B4E1N2 expand/collapse secondary AC list , B7Z9W7, Q07822, Q53YE6, Q9UCA8
Entry history
Integrated into UniProtKB/Swiss-Prot: September 19, 2002
Last sequence update: November 1, 1996
Last modified: April 16, 2014
This is version 136 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 4

Human chromosome 4: entries, gene names and cross-references to MIM