Q13541 (4EBP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Eukaryotic translation initiation factor 4E-binding protein 1
Short name=4E-BP1
Short name=eIF4E-binding protein 1

Alternative name(s):
Phosphorylated heat- and acid-stable protein regulated by insulin 1
Short name=PHAS-I

Gene names

Name:

EIF4EBP1

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	118 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Regulates eIF4E activity by preventing its assembly into the eIF4F complex. Mediates the regulation of protein translation by hormones, growth factors and other stimuli that signal through the MAP kinase and mTORC1 pathways. Ref.1
Subunit structure	Nonphosphorylated EIF4EBP1 competes with EIF4G1/EIF4G3 to interact with EIF4E; insulin stimulated MAP-kinase (MAPK1 and MAPK3) or mTORC1 phosphorylation of EIF4EBP1 causes dissociation of the complex allowing EIF4G1/EIF4G3 to bind and consequent initiation of translation. Interacts with RPTOR. Ref.1 Ref.9 Ref.11 Ref.12
Post-translational modification	Phosphorylated on serine and threonine residues in response to insulin, EGF and PDGF. Phosphorylation at Thr-37, Thr-46, Ser-65 and Thr-70 is regulated by mTORC1. Phosphorylated upon DNA damage, probably by ATM or ATR. Ref.1 Ref.10 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21
Sequence similarities	Belongs to the eIF4E-binding protein family.

Ontologies

Keywords
Biological process	Translation regulation
Molecular function	Protein synthesis inhibitor
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	G1/S transition of mitotic cell cycle Inferred from mutant phenotype. Source: UniProtKB TOR signaling cascade Inferred from direct assay Ref.11. Source: UniProtKB insulin receptor signaling pathway Traceable author statement. Source: Reactome positive regulation of mitotic cell cycle Inferred from mutant phenotype. Source: UniProtKB translation Traceable author statement. Source: Reactome
Cellular component	cytosol Traceable author statement. Source: Reactome
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
EIF4E	P06730	4	EBI-74090,EBI-73440
MTOR	P42345	2	EBI-74090,EBI-359260
Mtor	Q9JLN9	2	EBI-74090,EBI-1571628	From a different organism.
RPTOR	Q8N122	4	EBI-74090,EBI-1567928

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.8

Chain

2 – 118

117

Eukaryotic translation initiation factor 4E-binding protein 1

PRO_0000190513

Amino acid modifications

Modified residue

2

1

N-acetylserine Ref.8 UniProtKB Q62622

Modified residue

10

1

Phosphothreonine Ref.20

Modified residue

34

1

Phosphotyrosine Ref.20

Modified residue

35

1

Phosphoserine Ref.18

Modified residue

36

1

Phosphothreonine Ref.18

Modified residue

37

1

Phosphothreonine; by MTOR Ref.12 Ref.18 Ref.19 Ref.20 Ref.21

Modified residue

41

1

Phosphothreonine Ref.18 Ref.19 Ref.20

Modified residue

44

1

Phosphoserine Ref.20

Modified residue

45

1

Phosphothreonine Ref.20

Modified residue

46

1

Phosphothreonine; by MTOR Ref.12 Ref.14 Ref.18 Ref.19 Ref.20 Ref.21

Modified residue

50

1

Phosphothreonine Ref.18 Ref.19

Modified residue

54

1

Phosphotyrosine Ref.19

Modified residue

65

1

Phosphoserine; by MAPK1, MAPK3 and MTOR Ref.12 Ref.13 Ref.15 Ref.17 Ref.19 UniProtKB Q62622

Modified residue

68

1

Phosphothreonine Ref.17

Modified residue

70

1

Phosphothreonine; by MTOR Ref.12 Ref.15 Ref.18 Ref.19

Modified residue

77

1

Phosphothreonine Ref.19

Modified residue

82

1

Phosphothreonine Ref.18

Modified residue

83

1

Phosphoserine Ref.18 Ref.19

Modified residue

94

1

Phosphoserine Ref.15 Ref.18 Ref.19

Modified residue

101

1

Phosphoserine Ref.15 Ref.18

Modified residue

112

1

Phosphoserine Ref.16

Secondary structure

1

.

.

.

118

Helix Strand Turn

Details...

Helix

56 – 61

6

Sequences

	Sequence		Length	Mass (Da)
	Q13541 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 1682A6BA74132966	FASTA	118	12,580
	10 20 30 40 50 60 MSGGSSCSQT PSRAIPATRR VVLGDGVQLP PGDYSTTPGG TLFSTTPGGT RIIYDRKFLM 70 80 90 100 110 ECRNSPVTKT PPRDLPTIPG VTSPSSDEPP MEASQSHLRN SPEDKRAGGE ESQFEMDI

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Insulin-dependent stimulation of protein synthesis by phosphorylation of a regulator of 5'-cap function." Pause A., Belsham G.J., Gingras A.-C., Donze O., Lin T.-A., Lawrence J.C. Jr., Sonenberg N. Nature 371:762-767(1994) [PubMed: 7935836] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH EIF4E, PHOSPHORYLATION. Tissue: Placenta.
[2]	"Identification of multiple genes and immunogenic epitopes of pancreatic cancer cells." Ito M., Shichijo S., Tsuda N., Ochi M., Harashima N., Saito N., Itoh K. Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[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].
[4]	"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)." Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B. Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain.
[6]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases 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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Colon and Lung.
[8]	"Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides." Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J. Nat. Biotechnol. 21:566-569(2003) [PubMed: 12665801] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-13, ACETYLATION AT SER-2. Tissue: Platelet.
[9]	"Repression of cap-dependent translation by 4E-binding protein 1: competition with p220 for binding to eukaryotic initiation factor-4E." Haghighat A., Mader S., Pause A., Sonenberg N. EMBO J. 14:5701-5709(1995) [PubMed: 8521827] [Abstract] Cited for: INTERACTION WITH EIF4E AND EIF4G.
[10]	"RAFT1 phosphorylation of the translational regulators p70 S6 kinase and 4E-BP1." Burnett P.E., Barrow R.K., Cohen N.A., Snyder S.H., Sabatini D.M. Proc. Natl. Acad. Sci. U.S.A. 95:1432-1437(1998) [PubMed: 9465032] [Abstract] Cited for: PHOSPHORYLATION BY MTOR.
[11]	"Raptor, a binding partner of target of rapamycin (TOR), mediates TOR action." Hara K., Maruki Y., Long X., Yoshino K., Oshiro N., Hidayat S., Tokunaga C., Avruch J., Yonezawa K. Cell 110:177-189(2002) [PubMed: 12150926] [Abstract] Cited for: INTERACTION WITH RPTOR.
[12]	"TOS motif-mediated raptor binding regulates 4E-BP1 multisite phosphorylation and function." Schalm S.S., Fingar D.C., Sabatini D.M., Blenis J. Curr. Biol. 13:797-806(2003) [PubMed: 12747827] [Abstract] Cited for: INTERACTION WITH RPTOR, PHOSPHORYLATION AT THR-37; THR-46; SER-65 AND THR-70 BY MTOR.
[13]	"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: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[14]	"Toward a global characterization of the phosphoproteome in prostate cancer cells: identification of phosphoproteins in the LNCaP cell line." Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S. Electrophoresis 28:2027-2034(2007) [PubMed: 17487921] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-46, MASS SPECTROMETRY. Tissue: Prostate cancer.
[15]	"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry." Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A. Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007) [PubMed: 17287340] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65; THR-70; SER-94 AND SER-101, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[16]	"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage." Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J. Science 316:1160-1166(2007) [PubMed: 17525332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-112, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[17]	"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column." Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y. Anal. Sci. 24:161-166(2008) [PubMed: 18187866] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65 AND THR-68, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[18]	"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis." Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III J. Proteome Res. 7:1346-1351(2008) [PubMed: 18220336] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-35; THR-36; THR-37; THR-41; THR-46; THR-50; THR-70; THR-82; SER-83; SER-94 AND SER-101, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[19]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-37; THR-41; THR-46; THR-50; TYR-54; SER-65; THR-70; THR-77; SER-83 AND SER-94, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[20]	"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach." Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S. Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-10; TYR-34; THR-37; THR-41; SER-44; THR-45 AND THR-46, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[21]	"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: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-37 AND THR-46, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[22]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[23]	"The interaction of eIF4E with 4E-BP1 is an induced fit to a completely disordered protein." Fletcher C.M., Wagner G. Protein Sci. 7:1639-1642(1998) [PubMed: 9684899] [Abstract] Cited for: STRUCTURE BY NMR OF 4-118.
[24]	"Structural basis for mRNA cap-binding regulation of eukaryotic initiation factor 4E by 4E-binding protein, studied by spectroscopic, X-ray crystal structural, and molecular dynamics simulation methods." Tomoo K., Matsushita Y., Fujisaki H., Abiko F., Shen X., Taniguchi T., Miyagawa H., Kitamura K., Miura K., Ishida T. Biochim. Biophys. Acta 1753:191-208(2005) [PubMed: 16271312] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 36-70 IN COMPLEX WITH EIF4E AND MRNA CAP ANALOG.
[25]	"Structures of the human eIF4E homologous protein, h4EHP, in its m7GTP-bound and unliganded forms." Rosettani P., Knapp S., Vismara M.-G., Rusconi L., Cameron A.D. J. Mol. Biol. 368:691-705(2007) [PubMed: 17368478] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 51-67 IN COMPLEX WITH EIF4E2 AND MRNA CAP ANALOG.
[26]	"Crystallographic and mass spectrometric characterisation of eIF4E with N7-alkylated cap derivatives." Brown C.J., McNae I., Fischer P.M., Walkinshaw M.D. J. Mol. Biol. 372:7-15(2007) [PubMed: 17631896] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 51-64 IN COMPLEX WITH EIF4E AND MRNA CAP ANALOG.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

L36055 mRNA. Translation: AAA62269.1.
AB044548 mRNA. Translation: BAB18650.1.
BT007162 mRNA. Translation: AAP35826.1.
CR456769 mRNA. Translation: CAG33050.1.
AK312011 mRNA. Translation: BAG34949.1.
CH471080 Genomic DNA. Translation: EAW63341.1.
CH471080 Genomic DNA. Translation: EAW63342.1.
BC004459 mRNA. Translation: AAH04459.1.
BC058073 mRNA. Translation: AAH58073.1.

IPI

IPI00002569.

PIR

S50866.

RefSeq

NP_004086.1. NM_004095.3.

UniGene

Hs.411641.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1WKW	X-ray	2.10	B	47-66	[»]
2JGB	X-ray	1.70	B	51-67	[»]
2JGC	X-ray	2.40	B	51-67	[»]
2V8W	X-ray	2.30	B/F	51-64	[»]
2V8X	X-ray	2.30	B/F	51-64	[»]
2V8Y	X-ray	2.10	B/F	51-64	[»]
3HXG	X-ray	2.10	C	51-67	[»]
3HXI	X-ray	1.80	C	51-67	[»]
3M93	X-ray	2.90	C	51-67	[»]
3M94	X-ray	2.05	C	51-67	[»]
3U7X	X-ray	2.10	C/D	47-66	[»]

ProteinModelPortal

Q13541.

DisProt

DP00028.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-30944N.

IntAct

Q13541. 10 interactions.

MINT

MINT-210160.

STRING

Q13541.

PTM databases

PhosphoSite

Q13541.

Polymorphism databases

DMDM

34921508.

Proteomic databases

PeptideAtlas

Q13541.

PRIDE

Q13541.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000338825; ENSP00000340691; ENSG00000187840.

GeneID

1978.

KEGG

hsa:1978.

UCSC

uc003xks.1. human.

Organism-specific databases

CTD

1978.

GeneCards

GC08P037888.

H-InvDB

HIX0004694.

HGNC

HGNC:3288. EIF4EBP1.

HPA

CAB005032.
CAB005039.
HPA023501.

MIM

602223. gene.

neXtProt

NX_Q13541.

PharmGKB

PA27715.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG19978.

GeneTree

ENSGT00390000013843.

HOGENOM

HBG714775.

HOVERGEN

HBG050425.

InParanoid

Q13541.

OMA

DKPAGGE.

OrthoDB

EOG40P486.

PhylomeDB

Q13541.

Enzyme and pathway databases

Pathway_Interaction_DB

insulin_pathway. Insulin Pathway.
mtor_4pathway. mTOR signaling pathway.
p38alphabetadownstreampathway. Signaling mediated by p38-alpha and p38-beta.

Reactome

REACT_111102. Signal Transduction.
REACT_17015. Metabolism of proteins.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpress

Q13541.

Bgee

Q13541.

CleanEx

HS_EIF4EBP1.

Genevestigator

Q13541.

GermOnline

ENSG00000187840. Homo sapiens.

Family and domain databases

InterPro

IPR008606. EIF4EBP.
[Graphical view]

KO

K07205.

PANTHER

PTHR12669. EIF4EBP. 1 hit.

Pfam

PF05456. eIF_4EBP. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

8003.

PMAP-CutDB

Q13541.

SOURCE

Search...

Entry information

Entry name

4EBP1_HUMAN

Accession

Primary (citable) accession number: Q13541
Secondary accession number(s): B2R502, D3DSW8, Q6IBN3

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 19, 2003
Last sequence update:	January 23, 2007
Last modified:	January 25, 2012
This is version 108 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.