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Q9NS15

- LTBP3_HUMAN

UniProt

Q9NS15 - LTBP3_HUMAN

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Protein

Latent-transforming growth factor beta-binding protein 3

Gene
LTBP3
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

May be involved in the assembly, secretion and targeting of TGFB1 to sites at which it is stored and/or activated. May play critical roles in controlling and directing the activity of TGFB1. May have a structural role in the extra cellular matrix (ECM).

GO - Molecular functioni

  1. calcium ion binding Source: InterPro
  2. transforming growth factor beta binding Source: UniProt

GO - Biological processi

  1. bone morphogenesis Source: Ensembl
  2. bone remodeling Source: Ensembl
  3. extracellular matrix organization Source: Reactome
  4. lung saccule development Source: Ensembl
  5. negative regulation of bone mineralization Source: Ensembl
  6. negative regulation of chondrocyte differentiation Source: Ensembl
  7. positive regulation of bone resorption Source: Ensembl
  8. positive regulation of mesenchymal stem cell differentiation Source: UniProt
  9. positive regulation of mesenchymal stem cell proliferation Source: UniProt
  10. transforming growth factor beta activation Source: UniProt
  11. transforming growth factor beta receptor signaling pathway Source: Ensembl
Complete GO annotation...

Keywords - Ligandi

Growth factor binding

Enzyme and pathway databases

ReactomeiREACT_150331. Molecules associated with elastic fibres.

Names & Taxonomyi

Protein namesi
Recommended name:
Latent-transforming growth factor beta-binding protein 3
Short name:
LTBP-3
Gene namesi
Name:LTBP3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 11

Organism-specific databases

HGNCiHGNC:6716. LTBP3.

Subcellular locationi

Secreted By similarity
Note: Secretion occurs after coexpression with TGFB1 and requires complexing with 'Cys-33' of the TGFB1 propeptide By similarity.

GO - Cellular componenti

  1. extracellular matrix Source: UniProt
  2. extracellular region Source: Reactome
  3. extracellular vesicular exosome Source: UniProt
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Involvement in diseasei

Tooth agenesis selective 6 (STHAG6) [MIM:613097]: A form of selective tooth agenesis, a common anomaly characterized by the congenital absence of one or more teeth. Selective tooth agenesis without associated systemic disorders has sometimes been divided into 2 types: oligodontia, defined as agenesis of 6 or more permanent teeth, and hypodontia, defined as agenesis of less than 6 teeth. The number in both cases does not include absence of third molars (wisdom teeth). In tooth agenesis selective type 6, alveolar bone is absent where the teeth are missing. Some individuals have short stature.
Note: The disease is caused by mutations affecting the gene represented in this entry.1 Publication

Organism-specific databases

MIMi613097. phenotype.
Orphaneti2227. Hypodontia.
99798. Oligodontia.
PharmGKBiPA30479.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 4343 Reviewed predictionAdd
BLAST
Chaini44 – 13031260Latent-transforming growth factor beta-binding protein 3PRO_0000007646Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi89 – 891N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi113 ↔ 123 By similarity
Disulfide bondi117 ↔ 129 By similarity
Disulfide bondi131 ↔ 140 By similarity
Glycosylationi349 – 3491N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi359 ↔ 370 By similarity
Disulfide bondi365 ↔ 379 By similarity
Disulfide bondi381 ↔ 394 By similarity
Disulfide bondi578 ↔ 590 By similarity
Disulfide bondi585 ↔ 599 By similarity
Disulfide bondi601 ↔ 614 By similarity
Disulfide bondi620 ↔ 632 By similarity
Disulfide bondi625 ↔ 641 By similarity
Disulfide bondi643 ↔ 658 By similarity
Disulfide bondi664 ↔ 676 By similarity
Disulfide bondi670 ↔ 685 By similarity
Disulfide bondi687 ↔ 701 By similarity
Disulfide bondi748 ↔ 759 By similarity
Disulfide bondi754 ↔ 768 By similarity
Disulfide bondi770 ↔ 783 By similarity
Disulfide bondi789 ↔ 800 By similarity
Disulfide bondi795 ↔ 809 By similarity
Disulfide bondi811 ↔ 824 By similarity
Disulfide bondi830 ↔ 841 By similarity
Disulfide bondi836 ↔ 850 By similarity
Glycosylationi845 – 8451N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi852 ↔ 864 By similarity
Disulfide bondi870 ↔ 883 By similarity
Disulfide bondi877 ↔ 892 By similarity
Disulfide bondi894 ↔ 907 By similarity
Glycosylationi936 – 9361N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi997 ↔ 1010 By similarity
Disulfide bondi1005 ↔ 1019 By similarity
Disulfide bondi1021 ↔ 1034 By similarity
Disulfide bondi1040 ↔ 1051 By similarity
Disulfide bondi1046 ↔ 1060 By similarity
Disulfide bondi1062 ↔ 1075 By similarity
Disulfide bondi1086 ↔ 1097 By similarity
Disulfide bondi1092 ↔ 1106 By similarity
Disulfide bondi1108 ↔ 1121 By similarity
Disulfide bondi1258 ↔ 1273 By similarity
Disulfide bondi1268 ↔ 1282 By similarity
Glycosylationi1275 – 12751N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi1284 ↔ 1297 By similarity

Post-translational modificationi

Contains hydroxylated asparagine residues By similarity.
Two intrachain disulfide bonds from the TB3 domain are rearranged upon TGFB1 binding, and form interchain bonds with TGFB1 propeptide, anchoring it to the extracellular matrix.

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiQ9NS15.
PaxDbiQ9NS15.
PRIDEiQ9NS15.

PTM databases

PhosphoSiteiQ9NS15.

Expressioni

Tissue specificityi

Isoform 2 is expressed prominently in heart, skeletal muscle, prostate, testis, small intestine and ovary. Isoform 1 is strongly expressed in pancreas and liver.

Gene expression databases

ArrayExpressiQ9NS15.
BgeeiQ9NS15.
CleanExiHS_LTBP3.
GenevestigatoriQ9NS15.

Interactioni

Subunit structurei

Forms part of the large latent transforming growth factor beta precursor complex; removal is essential for activation of complex.

Protein-protein interaction databases

BioGridi110232. 8 interactions.
IntActiQ9NS15. 6 interactions.
MINTiMINT-1184940.
STRINGi9606.ENSP00000301873.

Structurei

3D structure databases

ProteinModelPortaliQ9NS15.
SMRiQ9NS15. Positions 296-461, 573-1122, 1234-1297.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini109 – 14133EGF-like 1Add
BLAST
Domaini277 – 33155TB 1Add
BLAST
Domaini355 – 39541EGF-like 2; calcium-binding Reviewed predictionAdd
BLAST
Domaini403 – 45553TB 2Add
BLAST
Domaini574 – 61542EGF-like 3Add
BLAST
Domaini616 – 65944EGF-like 4; calcium-binding Reviewed predictionAdd
BLAST
Domaini660 – 70243EGF-like 5; calcium-binding Reviewed predictionAdd
BLAST
Domaini744 – 78441EGF-like 6; calcium-binding Reviewed predictionAdd
BLAST
Domaini785 – 82541EGF-like 7; calcium-binding Reviewed predictionAdd
BLAST
Domaini826 – 86540EGF-like 8; calcium-binding Reviewed predictionAdd
BLAST
Domaini866 – 90843EGF-like 9; calcium-binding Reviewed predictionAdd
BLAST
Domaini917 – 97155TB 3Add
BLAST
Domaini993 – 103543EGF-like 10; calcium-binding Reviewed predictionAdd
BLAST
Domaini1036 – 107641EGF-like 11; calcium-binding Reviewed predictionAdd
BLAST
Domaini1082 – 112241EGF-like 12; calcium-binding Reviewed predictionAdd
BLAST
Domaini1136 – 118651TB 4Add
BLAST
Domaini1254 – 129845EGF-like 13; calcium-binding Reviewed predictionAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi3 – 167165Gly-richAdd
BLAST
Compositional biasi578 – 894317Cys-richAdd
BLAST

Sequence similaritiesi

Belongs to the LTBP family.
Contains 13 EGF-like domains.

Keywords - Domaini

EGF-like domain, Repeat, Signal

Phylogenomic databases

eggNOGiNOG261244.
HOGENOMiHOG000293153.
HOVERGENiHBG052370.
InParanoidiQ9NS15.
KOiK08023.
OMAiEGPPAQH.
PhylomeDBiQ9NS15.
TreeFamiTF317514.

Family and domain databases

Gene3Di3.90.290.10. 5 hits.
InterProiIPR026823. cEGF.
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.
IPR009030. Growth_fac_rcpt_N_dom.
IPR017878. TB_dom.
[Graphical view]
PfamiPF12662. cEGF. 1 hit.
PF07645. EGF_CA. 10 hits.
PF00683. TB. 4 hits.
[Graphical view]
SMARTiSM00181. EGF. 3 hits.
SM00179. EGF_CA. 12 hits.
[Graphical view]
SUPFAMiSSF57184. SSF57184. 4 hits.
SSF57581. SSF57581. 4 hits.
PROSITEiPS00010. ASX_HYDROXYL. 11 hits.
PS00022. EGF_1. 1 hit.
PS01186. EGF_2. 8 hits.
PS50026. EGF_3. 13 hits.
PS01187. EGF_CA. 12 hits.
PS51364. TB. 4 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9NS15-1) [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

MPGPRGAAGG LAPEMRGAGA AGLLALLLLL LLLLLGLGGR VEGGPAGERG     50
AGGGGALARE RFKVVFAPVI CKRTCLKGQC RDSCQQGSNM TLIGENGHST 100
DTLTGSGFRV VVCPLPCMNG GQCSSRNQCL CPPDFTGRFC QVPAGGAGGG 150
TGGSGPGLSR TGALSTGALP PLAPEGDSVA SKHAIYAVQV IADPPGPGEG 200
PPAQHAAFLV PLGPGQISAE VQAPPPVVNV RVHHPPEASV QVHRIESSNA 250
ESAAPSQHLL PHPKPSHPRP PTQKPLGRCF QDTLPKQPCG SNPLPGLTKQ 300
EDCCGSIGTA WGQSKCHKCP QLQYTGVQKP GPVRGEVGAD CPQGYKRLNS 350
THCQDINECA MPGVCRHGDC LNNPGSYRCV CPPGHSLGPS RTQCIADKPE 400
EKSLCFRLVS PEHQCQHPLT TRLTRQLCCC SVGKAWGARC QRCPTDGTAA 450
FKEICPAGKG YHILTSHQTL TIQGESDFSL FLHPDGPPKP QQLPESPSQA 500
PPPEDTEEER GVTTDSPVSE ERSVQQSHPT ATTTPARPYP ELISRPSPPT 550
MRWFLPDLPP SRSAVEIAPT QVTETDECRL NQNICGHGEC VPGPPDYSCH 600
CNPGYRSHPQ HRYCVDVNEC EAEPCGPGRG ICMNTGGSYN CHCNRGYRLH 650
VGAGGRSCVD LNECAKPHLC GDGGFCINFP GHYKCNCYPG YRLKASRPPV 700
CEDIDECRDP SSCPDGKCEN KPGSFKCIAC QPGYRSQGGG ACRDVNECAE 750
GSPCSPGWCE NLPGSFRCTC AQGYAPAPDG RSCLDVDECE AGDVCDNGIC 800
SNTPGSFQCQ CLSGYHLSRD RSHCEDIDEC DFPAACIGGD CINTNGSYRC 850
LCPQGHRLVG GRKCQDIDEC SQDPSLCLPH GACKNLQGSY VCVCDEGFTP 900
TQDQHGCEEV EQPHHKKECY LNFDDTVFCD SVLATNVTQQ ECCCSLGAGW 950
GDHCEIYPCP VYSSAEFHSL CPDGKGYTQD NNIVNYGIPA HRDIDECMLF 1000
GSEICKEGKC VNTQPGYECY CKQGFYYDGN LLECVDVDEC LDESNCRNGV 1050
CENTRGGYRC ACTPPAEYSP AQRQCLSPEE MDVDECQDPA ACRPGRCVNL 1100
PGSYRCECRP PWVPGPSGRD CQLPESPAER APERRDVCWS QRGEDGMCAG 1150
PLAGPALTFD DCCCRQGRGW GAQCRPCPPR GAGSHCPTSQ SESNSFWDTS 1200
PLLLGKPPRD EDSSEEDSDE CRCVSGRCVP RPGGAVCECP GGFQLDASRA 1250
RCVDIDECRE LNQRGLLCKS ERCVNTSGSF RCVCKAGFAR SRPHGACVPQ 1300
RRR 1303
Length:1,303
Mass (Da):139,359
Last modified:October 17, 2006 - v4
Checksum:i3BC6B1EE19198414
GO
Isoform 2 (identifier: Q9NS15-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1082-1128: Missing.

Show »
Length:1,256
Mass (Da):134,292
Checksum:i1D930E5D208601E2
GO

Sequence cautioni

The sequence BAB15767.1 differs from that shown. Reason: Erroneous initiation.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1082 – 112847Missing in isoform 2. VSP_009241Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti35 – 351Missing in BAB15767. 1 Publication
Sequence conflicti477 – 4771D → H in AAB64201. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF135960 mRNA. Translation: AAF62352.3.
AK024477 mRNA. Translation: BAB15767.1. Different initiation.
AF011407 mRNA. Translation: AAB64201.1.
BC008761 mRNA. Translation: AAH08761.2.
AL117551 mRNA. Translation: CAB55988.1.
CCDSiCCDS44647.1. [Q9NS15-1]
CCDS8103.1. [Q9NS15-2]
PIRiT17298.
RefSeqiNP_001123616.1. NM_001130144.2. [Q9NS15-1]
NP_001157738.1. NM_001164266.1.
NP_066548.2. NM_021070.4. [Q9NS15-2]
UniGeneiHs.289019.

Genome annotation databases

EnsembliENST00000301873; ENSP00000301873; ENSG00000168056. [Q9NS15-1]
ENST00000322147; ENSP00000326647; ENSG00000168056. [Q9NS15-2]
GeneIDi4054.
KEGGihsa:4054.
UCSCiuc001oei.3. human. [Q9NS15-2]
uc001oej.3. human. [Q9NS15-1]

Polymorphism databases

DMDMi116242623.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF135960 mRNA. Translation: AAF62352.3 .
AK024477 mRNA. Translation: BAB15767.1 . Different initiation.
AF011407 mRNA. Translation: AAB64201.1 .
BC008761 mRNA. Translation: AAH08761.2 .
AL117551 mRNA. Translation: CAB55988.1 .
CCDSi CCDS44647.1. [Q9NS15-1 ]
CCDS8103.1. [Q9NS15-2 ]
PIRi T17298.
RefSeqi NP_001123616.1. NM_001130144.2. [Q9NS15-1 ]
NP_001157738.1. NM_001164266.1.
NP_066548.2. NM_021070.4. [Q9NS15-2 ]
UniGenei Hs.289019.

3D structure databases

ProteinModelPortali Q9NS15.
SMRi Q9NS15. Positions 296-461, 573-1122, 1234-1297.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 110232. 8 interactions.
IntActi Q9NS15. 6 interactions.
MINTi MINT-1184940.
STRINGi 9606.ENSP00000301873.

PTM databases

PhosphoSitei Q9NS15.

Polymorphism databases

DMDMi 116242623.

Proteomic databases

MaxQBi Q9NS15.
PaxDbi Q9NS15.
PRIDEi Q9NS15.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000301873 ; ENSP00000301873 ; ENSG00000168056 . [Q9NS15-1 ]
ENST00000322147 ; ENSP00000326647 ; ENSG00000168056 . [Q9NS15-2 ]
GeneIDi 4054.
KEGGi hsa:4054.
UCSCi uc001oei.3. human. [Q9NS15-2 ]
uc001oej.3. human. [Q9NS15-1 ]

Organism-specific databases

CTDi 4054.
GeneCardsi GC11M065306.
HGNCi HGNC:6716. LTBP3.
MIMi 602090. gene.
613097. phenotype.
neXtProti NX_Q9NS15.
Orphaneti 2227. Hypodontia.
99798. Oligodontia.
PharmGKBi PA30479.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG261244.
HOGENOMi HOG000293153.
HOVERGENi HBG052370.
InParanoidi Q9NS15.
KOi K08023.
OMAi EGPPAQH.
PhylomeDBi Q9NS15.
TreeFami TF317514.

Enzyme and pathway databases

Reactomei REACT_150331. Molecules associated with elastic fibres.

Miscellaneous databases

ChiTaRSi LTBP3. human.
GeneWikii LTBP3.
GenomeRNAii 4054.
NextBioi 15884.
PROi Q9NS15.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9NS15.
Bgeei Q9NS15.
CleanExi HS_LTBP3.
Genevestigatori Q9NS15.

Family and domain databases

Gene3Di 3.90.290.10. 5 hits.
InterProi IPR026823. cEGF.
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.
IPR009030. Growth_fac_rcpt_N_dom.
IPR017878. TB_dom.
[Graphical view ]
Pfami PF12662. cEGF. 1 hit.
PF07645. EGF_CA. 10 hits.
PF00683. TB. 4 hits.
[Graphical view ]
SMARTi SM00181. EGF. 3 hits.
SM00179. EGF_CA. 12 hits.
[Graphical view ]
SUPFAMi SSF57184. SSF57184. 4 hits.
SSF57581. SSF57581. 4 hits.
PROSITEi PS00010. ASX_HYDROXYL. 11 hits.
PS00022. EGF_1. 1 hit.
PS01186. EGF_2. 8 hits.
PS50026. EGF_3. 13 hits.
PS01187. EGF_CA. 12 hits.
PS51364. TB. 4 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Secretion of human latent TGF-beta-binding protein-3 (LTBP-3) is dependent on co-expression of TGF-beta."
    Penttinen C., Saharinen J., Weikkolainen K., Hyytiainen M., Keski-Oja J.
    J. Cell Sci. 115:3457-3468(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION (ISOFORM 2).
  2. "The nucleotide sequence of a long cDNA clone isolated from human spleen."
    Ohara O., Nagase T., Kikuno R., Okumura K.
    Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Spleen.
  3. "Analysis of the expression pattern of the latent transforming growth factor beta binding protein isoforms in normal and diseased human liver reveals a new splice variant missing the proteinase-sensitive hinge region."
    Michel K., Roth S., Trautwein C., Gong W., Flemming P., Gressner A.M.
    Hepatology 27:1592-1599(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 394-573.
    Tissue: Liver.
  4. "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] OF 514-1303 (ISOFORM 2).
    Tissue: Colon.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 793-1303.
    Tissue: Uterus.
  6. "Specific sequence motif of 8-Cys repeats of TGF-beta binding proteins, LTBPs, creates a hydrophobic interaction surface for binding of small latent TGF-beta."
    Saharinen J., Keski-Oja J.
    Mol. Biol. Cell 11:2691-2704(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TGFB1.
  7. "Latent transforming growth factor-beta binding proteins (LTBPs) --structural extracellular matrix proteins for targeting TGF-beta action."
    Saharinen J., Hyytiainen M., Taipale J., Keski-Oja J.
    Cytokine Growth Factor Rev. 10:99-117(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  8. "The latent transforming growth factor beta binding protein (LTBP) family."
    Oklu R., Hesketh R.
    Biochem. J. 352:601-610(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  9. "Oligodontia is caused by mutation in LTBP3, the gene encoding latent TGF-beta binding protein 3."
    Noor A., Windpassinger C., Vitcu I., Orlic M., Rafiq M.A., Khalid M., Malik M.N., Ayub M., Alman B., Vincent J.B.
    Am. J. Hum. Genet. 84:519-523(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN STHAG6.

Entry informationi

Entry nameiLTBP3_HUMAN
AccessioniPrimary (citable) accession number: Q9NS15
Secondary accession number(s): O15107
, Q96HB9, Q9H7K2, Q9UFN4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 16, 2004
Last sequence update: October 17, 2006
Last modified: September 3, 2014
This is version 127 of the entry and version 4 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 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi