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Protein

Phosphatidylethanolamine-binding protein 1

Gene

PEBP1

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

Functioni

Binds ATP, opioids and phosphatidylethanolamine. Has lower affinity for phosphatidylinositol and phosphatidylcholine. Serine protease inhibitor which inhibits thrombin, neuropsin and chymotrypsin but not trypsin, tissue type plasminogen activator and elastase (By similarity). Inhibits the kinase activity of RAF1 by inhibiting its activation and by dissociating the RAF1/MEK complex and acting as a competitive inhibitor of MEK phosphorylation.By similarity1 Publication
HCNP may be involved in the function of the presynaptic cholinergic neurons of the central nervous system. HCNP increases the production of choline acetyltransferase but not acetylcholinesterase. Seems to be mediated by a specific receptor (By similarity).By similarity

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • enzyme binding Source: UniProtKB
  • phosphatidylethanolamine binding Source: ProtInc
  • poly(A) RNA binding Source: UniProtKB
  • protein kinase binding Source: UniProtKB
  • serine-type endopeptidase inhibitor activity Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Protease inhibitor, Serine protease inhibitor

Keywords - Ligandi

ATP-binding, Lipid-binding, Nucleotide-binding

Enzyme and pathway databases

SignaLinkiP30086.

Protein family/group databases

MEROPSiI51.002.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphatidylethanolamine-binding protein 1
Short name:
PEBP-1
Alternative name(s):
HCNPpp
Neuropolypeptide h3
Prostatic-binding protein
Raf kinase inhibitor protein
Short name:
RKIP
Cleaved into the following chain:
Gene namesi
Name:PEBP1
Synonyms:PBP, PEBP
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:8630. PEBP1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB-SubCell
  • extracellular exosome Source: UniProtKB
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA32968.

Polymorphism and mutation databases

BioMutaiPEBP1.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 187186Phosphatidylethanolamine-binding protein 1PRO_0000023271Add
BLAST
Peptidei2 – 1211Hippocampal cholinergic neurostimulating peptidePRO_0000023272Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei6 – 61Phosphoserine1 Publication
Modified residuei42 – 421Phosphothreonine1 Publication
Modified residuei52 – 521Phosphoserine5 Publications
Modified residuei54 – 541Phosphoserine1 Publication
Modified residuei98 – 981Phosphoserine1 Publication
Modified residuei153 – 1531Phosphoserine1 Publication

Keywords - PTMi

Disulfide bond, Phosphoprotein

Proteomic databases

MaxQBiP30086.
PaxDbiP30086.
PeptideAtlasiP30086.
PRIDEiP30086.

2D gel databases

DOSAC-COBS-2DPAGEP30086.
OGPiP30086.
REPRODUCTION-2DPAGEIPI00219446.
P30086.
SWISS-2DPAGEP30086.
UCD-2DPAGEP30086.

PTM databases

PhosphoSiteiP30086.

Expressioni

Gene expression databases

BgeeiP30086.
CleanExiHS_PEBP1.
ExpressionAtlasiP30086. baseline and differential.
GenevisibleiP30086. HS.

Organism-specific databases

HPAiCAB009906.
CAB013493.
HPA008819.

Interactioni

Subunit structurei

Has a tendency to form dimers by disulfide cross-linking (By similarity). Interacts with RAF1 and this interaction is enhanced if RAF1 is phosphorylated on residues 'Ser-338', 'Ser-339', 'Tyr-340' and 'Tyr-341'. Interacts with ALOX15; in response to IL13/interleukin-13, prevents the interaction of PEBP1 with RAF1 to activate the ERK signaling cascade.By similarity3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
RAF1P040497EBI-716384,EBI-365996

Protein-protein interaction databases

BioGridi111076. 19 interactions.
DIPiDIP-44269N.
IntActiP30086. 8 interactions.
MINTiMINT-5002544.
STRINGi9606.ENSP00000261313.

Structurei

Secondary structure

1
187
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi5 – 73Combined sources
Turni8 – 125Combined sources
Helixi14 – 163Combined sources
Beta strandi22 – 243Combined sources
Beta strandi26 – 283Combined sources
Beta strandi32 – 343Combined sources
Turni43 – 464Combined sources
Beta strandi51 – 544Combined sources
Beta strandi62 – 7110Combined sources
Beta strandi76 – 783Combined sources
Beta strandi84 – 9310Combined sources
Helixi97 – 993Combined sources
Beta strandi100 – 1045Combined sources
Beta strandi118 – 12912Combined sources
Beta strandi140 – 1423Combined sources
Turni144 – 1463Combined sources
Helixi151 – 1577Combined sources
Beta strandi164 – 1718Combined sources
Helixi177 – 1837Combined sources
Turni184 – 1863Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BD9X-ray2.05A/B1-187[»]
1BEHX-ray1.75A/B1-187[»]
2L7WNMR-A1-187[»]
2QYQX-ray1.95A1-187[»]
ProteinModelPortaliP30086.
SMRiP30086. Positions 3-186.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP30086.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni93 – 13442Interaction with RAF1Add
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1881.
GeneTreeiENSGT00740000115401.
HOGENOMiHOG000237655.
HOVERGENiHBG008165.
InParanoidiP30086.
OMAiDKPLKCD.
OrthoDBiEOG7P02K3.
PhylomeDBiP30086.
TreeFamiTF315074.

Family and domain databases

Gene3Di3.90.280.10. 1 hit.
InterProiIPR001858. Phosphotidylethanolamine-bd_CS.
IPR008914. PtdEtn-bd_prot_PEBP.
[Graphical view]
PfamiPF01161. PBP. 1 hit.
[Graphical view]
SUPFAMiSSF49777. SSF49777. 1 hit.
PROSITEiPS01220. PBP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P30086-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPVDLSKWSG PLSLQEVDEQ PQHPLHVTYA GAAVDELGKV LTPTQVKNRP
60 70 80 90 100
TSISWDGLDS GKLYTLVLTD PDAPSRKDPK YREWHHFLVV NMKGNDISSG
110 120 130 140 150
TVLSDYVGSG PPKGTGLHRY VWLVYEQDRP LKCDEPILSN RSGDHRGKFK
160 170 180
VASFRKKYEL RAPVAGTCYQ AEWDDYVPKL YEQLSGK
Length:187
Mass (Da):21,057
Last modified:January 23, 2007 - v3
Checksum:iF1E9F17E2CD11C36
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti8 – 81W → K (PubMed:7637590).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti9 – 91S → N.
VAR_006048

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D16111 mRNA. Translation: BAA03684.1.
X75252 mRNA. Translation: CAA53031.1.
X85033 mRNA. Translation: CAA59404.1.
AK311927 mRNA. Translation: BAG34868.1.
CH471054 Genomic DNA. Translation: EAW98122.1.
BC008714 mRNA. Translation: AAH08714.1.
BC017396 mRNA. Translation: AAH17396.1.
BC031102 mRNA. Translation: AAH31102.1.
S76773 mRNA. Translation: AAD14234.1.
CCDSiCCDS9187.1.
PIRiI53745.
RefSeqiNP_002558.1. NM_002567.2.
UniGeneiHs.433863.

Genome annotation databases

EnsembliENST00000261313; ENSP00000261313; ENSG00000089220.
GeneIDi5037.
KEGGihsa:5037.
UCSCiuc001twu.1. human.

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D16111 mRNA. Translation: BAA03684.1.
X75252 mRNA. Translation: CAA53031.1.
X85033 mRNA. Translation: CAA59404.1.
AK311927 mRNA. Translation: BAG34868.1.
CH471054 Genomic DNA. Translation: EAW98122.1.
BC008714 mRNA. Translation: AAH08714.1.
BC017396 mRNA. Translation: AAH17396.1.
BC031102 mRNA. Translation: AAH31102.1.
S76773 mRNA. Translation: AAD14234.1.
CCDSiCCDS9187.1.
PIRiI53745.
RefSeqiNP_002558.1. NM_002567.2.
UniGeneiHs.433863.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BD9X-ray2.05A/B1-187[»]
1BEHX-ray1.75A/B1-187[»]
2L7WNMR-A1-187[»]
2QYQX-ray1.95A1-187[»]
ProteinModelPortaliP30086.
SMRiP30086. Positions 3-186.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111076. 19 interactions.
DIPiDIP-44269N.
IntActiP30086. 8 interactions.
MINTiMINT-5002544.
STRINGi9606.ENSP00000261313.

Protein family/group databases

MEROPSiI51.002.

PTM databases

PhosphoSiteiP30086.

Polymorphism and mutation databases

BioMutaiPEBP1.

2D gel databases

DOSAC-COBS-2DPAGEP30086.
OGPiP30086.
REPRODUCTION-2DPAGEIPI00219446.
P30086.
SWISS-2DPAGEP30086.
UCD-2DPAGEP30086.

Proteomic databases

MaxQBiP30086.
PaxDbiP30086.
PeptideAtlasiP30086.
PRIDEiP30086.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000261313; ENSP00000261313; ENSG00000089220.
GeneIDi5037.
KEGGihsa:5037.
UCSCiuc001twu.1. human.

Organism-specific databases

CTDi5037.
GeneCardsiGC12P118573.
HGNCiHGNC:8630. PEBP1.
HPAiCAB009906.
CAB013493.
HPA008819.
MIMi604591. gene.
neXtProtiNX_P30086.
PharmGKBiPA32968.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG1881.
GeneTreeiENSGT00740000115401.
HOGENOMiHOG000237655.
HOVERGENiHBG008165.
InParanoidiP30086.
OMAiDKPLKCD.
OrthoDBiEOG7P02K3.
PhylomeDBiP30086.
TreeFamiTF315074.

Enzyme and pathway databases

SignaLinkiP30086.

Miscellaneous databases

ChiTaRSiPEBP1. human.
EvolutionaryTraceiP30086.
GeneWikiiPhosphatidylethanolamine_binding_protein_1.
GenomeRNAii5037.
NextBioi19408.
PROiP30086.
SOURCEiSearch...

Gene expression databases

BgeeiP30086.
CleanExiHS_PEBP1.
ExpressionAtlasiP30086. baseline and differential.
GenevisibleiP30086. HS.

Family and domain databases

Gene3Di3.90.280.10. 1 hit.
InterProiIPR001858. Phosphotidylethanolamine-bd_CS.
IPR008914. PtdEtn-bd_prot_PEBP.
[Graphical view]
PfamiPF01161. PBP. 1 hit.
[Graphical view]
SUPFAMiSSF49777. SSF49777. 1 hit.
PROSITEiPS01220. PBP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A human cDNA sequence homologue of bovine phosphatidylethanolamine-binding protein."
    Hori N., Keon-Sang C., Murakawa K., Matoba R., Fukushima A., Okubo K., Matsubara K.
    Gene 140:293-294(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Sequence homology of rat and human HCNP precursor proteins, bovine phosphatidylethanolamine-binding protein and rat 23-kDa protein associated with the opioid-binding protein."
    Tohdoh N., Tojo S., Agui H., Ojika K.
    Brain Res. Mol. Brain Res. 30:381-384(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Placenta.
  3. Hall L.
    Submitted (FEB-1995) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain.
  4. "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].
    Tissue: Cerebellum.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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].
    Tissue: Brain, Hypothalamus and Lung.
  7. "Human liver protein map: a reference database established by microsequencing and gel comparison."
    Hochstrasser D.F., Frutiger S., Paquet N., Bairoch A., Ravier F., Pasquali C., Sanchez J.-C., Tissot J.-D., Bjellqvist B., Vargas R., Appel R.D., Hughes G.J.
    Electrophoresis 13:992-1001(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-11.
    Tissue: Liver.
  8. Lubec G., Vishwanath V., Chen W.-Q., Sun Y.
    Submitted (DEC-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 8-39; 48-77; 81-113; 120-141 AND 162-187, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
  9. "Amino acid sequence of the Homo sapiens brain 21-23-kDa protein (neuropolypeptide h3), comparison with its counterparts from Rattus norvegicus and Bos taurus species, and expression of its mRNA in different tissues."
    Seddiqi N., Bollengier F., Alliel P.M., Perin J.-P., Bonnet F., Bucquoy S., Jolles P., Schoentgen F.
    J. Mol. Evol. 39:655-660(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 48-187.
    Tissue: Brain.
  10. Cited for: CHARACTERIZATION OF HCNP.
  11. Cited for: INTERACTION WITH RAF-1.
  12. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. "The RKIP (Raf-1 Kinase Inhibitor Protein) conserved pocket binds to the phosphorylated N-region of Raf-1 and inhibits the Raf-1-mediated activated phosphorylation of MEK."
    Rath O., Park S., Tang H.H., Banfield M.J., Brady R.L., Lee Y.C., Dignam J.D., Sedivy J.M., Kolch W., Yeung K.C.
    Cell. Signal. 20:935-941(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH RAF1.
  14. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-42 AND SER-52, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  16. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "15-Lipoxygenase 1 interacts with phosphatidylethanolamine-binding protein to regulate MAPK signaling in human airway epithelial cells."
    Zhao J., O'Donnell V.B., Balzar S., St Croix C.M., Trudeau J.B., Wenzel S.E.
    Proc. Natl. Acad. Sci. U.S.A. 108:14246-14251(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ALOX15.
  19. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  20. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  21. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6; SER-52; SER-54; SER-98 AND SER-153, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  22. "Function from structure? The crystal structure of human phosphatidylethanolamine-binding protein suggests a role in membrane signal transduction."
    Banfield M.J., Barker J.J., Perry A.C., Brady R.L.
    Structure 6:1245-1254(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS).

Entry informationi

Entry nameiPEBP1_HUMAN
AccessioniPrimary (citable) accession number: P30086
Secondary accession number(s): B2R4S1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: January 23, 2007
Last modified: June 24, 2015
This is version 163 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

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. 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.