P48552 (NRIP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Nuclear receptor-interacting protein 1

Alternative name(s):
Nuclear factor RIP140
Receptor-interacting protein 140

Gene names

Name:

NRIP1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1158 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Modulates transcriptional activation by steroid receptors such as NR3C1, NR3C2 and ESR1. Also modulates transcriptional repression by nuclear hormone receptors. Ref.1 Ref.5 Ref.6 Ref.8 Ref.10 Ref.12
Subunit structure	Interacts with RARA and RXRB homodimers and RARA/RXRB heterodimers in the presence of ligand. Interacts with HDAC1 and HDAC3 via its N-terminal domain. Interacts with NR2C1 (sumoylated form and via the ligand-binding domain); the interaction results in promoting the repressor activity of NR2C1 By similarity. Interacts with CTBP1, CTBP2, ESR1, HDAC1, HDAC2, HDAC5, HDAC6, NR2C2, NR3C1, NR3C2, YWHAH, JUN and FOS. Found in a complex with both NR3C1 and YWHAH. Interacts with ZNF366. Ref.1 Ref.4 Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14
Subcellular location	Nucleus. Note: Localized to discrete foci and redistributes to larger nuclear domains upon binding to ligand-bound NR3C1. Ref.1 Ref.7 Ref.9 Ref.12
Domain	Contains 9 Leu-Xaa-Xaa-Leu-Leu (LXXLL) motifs, which have different affinities for nuclear receptors. The C-terminal LTKTNPILYYMLQK motif is required for ligand-dependent interaction with RAAR and RXRB homodimers and heterodimers, for the corepressor activity, and for the formation of an HDAC3 complex with RARA/RXRB By similarity. Contains at least four autonomous repression domains (RD1-4). RD1 functions via a histone deacetylase (HDAC)-independent mechanism, whereas RD2, RD3 and RD4 can function by HDAC-dependent or independent mechanisms, depending on cell type. RD2 is dependent on CTBP binding. Ref.11
Post-translational modification	Acetylation regulates its nuclear translocation and corepressive activity By similarity. Acetylation abolishes interaction with CTBP1. Phosphorylation enhances interaction with YWHAH.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Polymorphism
Domain	Repeat
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	androgen receptor signaling pathway Non-traceable author statement PubMed 15572661. Source: UniProtKB lipid storage Inferred from electronic annotation. Source: Compara negative regulation of transcription from RNA polymerase II promoter Inferred from direct assay Ref.5. Source: UniProtKB ovarian follicle rupture Inferred from electronic annotation. Source: Compara positive regulation of transcription from RNA polymerase II promoter Inferred from direct assay Ref.5Ref.1. Source: UniProtKB transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	histone deacetylase complex Inferred from electronic annotation. Source: Compara nucleus Inferred from direct assay Ref.7Ref.9Ref.1. Source: UniProtKB
Molecular_function	androgen receptor binding Non-traceable author statement PubMed 15572661. Source: UniProtKB transcription coactivator activity Inferred from direct assay Ref.5Ref.8Ref.1. Source: UniProtKB transcription corepressor activity Inferred from direct assay Ref.5. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CEP70	Q8NHQ1	3	EBI-746484,EBI-739624
FHL1	Q13642	6	EBI-746484,EBI-912547
LDOC1	O95751	3	EBI-746484,EBI-740738
ZNF366	Q8N895	2	EBI-746484,EBI-2813661

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1158

1158

Nuclear receptor-interacting protein 1

PRO_0000057951

Regions

Region

1 – 415

415

Interaction with ZNF366

Region

78 – 333

256

Repression domain 1

Region

410 – 700

291

Repression domain 2

Region

431 – 472

42

Required for targeting to small nuclear foci

Region

735 – 885

151

Repression domain 3

Region

753 – 1158

406

Interaction with ZNF366

Region

1118 – 1158

41

Repression domain 4

Motif

21 – 25

5

LXXLL motif 1

Motif

133 – 137

5

LXXLL motif 2

Motif

185 – 189

5

LXXLL motif 3

Motif

266 – 270

5

LXXLL motif 4

Motif

380 – 384

5

LXXLL motif 5

Motif

440 – 446

7

CTBP-binding; principal site

Motif

500 – 504

5

LXXLL motif 6

Motif

565 – 569

5

CTBP-binding

Motif

599 – 603

5

CTBP-binding Potential

Motif

713 – 717

5

LXXLL motif 7

Motif

819 – 823

5

LXXLL motif 8

Motif

936 – 940

5

LXXLL motif 9

Motif

946 – 950

5

CTBP-binding

Motif

1061 – 1074

14

Ligand-dependent nuclear receptor binding By similarity

Amino acid modifications

Modified residue

104

1

Phosphoserine By similarity

Modified residue

111

1

N6-acetyllysine By similarity

Modified residue

158

1

N6-acetyllysine By similarity

Modified residue

207

1

Phosphothreonine By similarity

Modified residue

286

1

N6-acetyllysine By similarity

Modified residue

310

1

N6-acetyllysine By similarity

Modified residue

356

1

Phosphoserine By similarity

Modified residue

378

1

Phosphoserine By similarity

Modified residue

446

1

N6-acetyllysine Ref.6

Modified residue

481

1

N6-acetyllysine By similarity

Modified residue

487

1

Phosphoserine By similarity

Modified residue

518

1

Phosphoserine By similarity

Modified residue

528

1

N6-acetyllysine By similarity

Modified residue

542

1

Phosphoserine By similarity

Modified residue

606

1

N6-acetyllysine By similarity

Modified residue

671

1

Phosphoserine By similarity

Modified residue

931

1

N6-acetyllysine By similarity

Modified residue

1001

1

Phosphoserine By similarity

Natural variations

Natural variant

37

1

V → I.
Corresponds to variant rs9941840 [ dbSNP | Ensembl ].

VAR_051241

Natural variant

221

1

H → R. Ref.16

VAR_023706

Natural variant

315

1

Y → F.
Corresponds to variant rs2228507 [ dbSNP | Ensembl ].

VAR_034142

Natural variant

441

1

I → V. Ref.16

VAR_023707

Natural variant

448

1

R → G Common polymorphism. Ref.1 Ref.16
Corresponds to variant rs2229742 [ dbSNP | Ensembl ].

VAR_023708

Natural variant

567

1

N → S.
Corresponds to variant rs9975169 [ dbSNP | Ensembl ].

VAR_051242

Natural variant

803

1

S → L. Ref.16

VAR_023709

Natural variant

1079

1

V → F. Ref.16

VAR_023710

Experimental info

Mutagenesis

440 – 443

4

PIDL → AAAA: Abolishes interaction with CTBP1. Ref.6

Mutagenesis

440 – 442

3

PID → AIA: Abolishes interaction with CTBP1 and attenuates nuclear hormone receptor-dependent transcription repression.

Mutagenesis

442 – 443

2

DL → AA: Reduces, but does not completely abolish, interaction with CTBP. Reduces transcriptional repression. Ref.12

Mutagenesis

442 – 443

2

DL → AS: Disrupts interaction with CTBP1, and CTBP2 to a lesser extent. Disrupts transcriptional repression; when associated with 567-AS-568. Ref.12

Mutagenesis

446

1

K → Q: Disrupts interaction with CTBP1. Decreases lysine acetylation. Disrupts nuclear hormone receptor-dependent transcription repression. Ref.6

Mutagenesis

446

1

K → R: Does not disrupt nuclear hormone receptor-dependent transcription repression. Ref.6

Mutagenesis

567 – 568

2

NL → AA: Disrupts transcriptional repression. Ref.11 Ref.12

Mutagenesis

567 – 568

2

NL → AS: Disrupts interaction with CTBP1 and CTBP2. Disrupts transcriptional repression; when associated with 442-AS-443. Ref.11 Ref.12

Mutagenesis

599 – 603

5

SMDLT → PIAAS: Does not further disrupt transcriptional repression; when associated with 442-AA-443 and 567-AA-568.

Mutagenesis

948 – 949

2

DL → AA: Abolishes CTBP binding but retains transcriptional repressor activity. Ref.11

Sequence conflict

124

1

P → R in CAA59108. Ref.1

Sequence conflict

721 – 726

6

NKGKSE → TKGRVK in CAA59108. Ref.1

Sequence conflict

954

1

S → I in AAH40361. Ref.3

Sequence conflict

1080

1

T → A in CAA59108. Ref.1

Secondary structure

1

.

.

.

1158

Helix Strand Turn

Details...

Helix

379 – 385

7

Sequences

	Sequence		Length	Mass (Da)
	P48552 [UniParc]. Last modified December 1, 2000. Version 2. Checksum: 81FC424968E9A5F6	FASTA	1,158	126,942
	10 20 30 40 50 60 MTHGEELGSD VHQDSIVLTY LEGLLMHQAA GGSGTAVDKK SAGHNEEDQN FNISGSAFPT 70 80 90 100 110 120 CQSNGPVLNT HTYQGSGMLH LKKARLLQSS EDWNAAKRKR LSDSIMNLNV KKEALLAGMV 130 140 150 160 170 180 DSVPKGKQDS TLLASLLQSF SSRLQTVALS QQIRQSLKEQ GYALSHDSLK VEKDLRCYGV 190 200 210 220 230 240 ASSHLKTLLK KSKVKDQKPD TNLPDVTKNL IRDRFAESPH HVGQSGTKVM SEPLSCAARL 250 260 270 280 290 300 QAVASMVEKR ASPATSPKPS VACSQLALLL SSEAHLQQYS REHALKTQNA NQAASERLAA 310 320 330 340 350 360 MARLQENGQK DVGSYQLPKG MSSHLNGQAR TSSSKLMASK SSATVFQNPM GIIPSSPKNA 370 380 390 400 410 420 GYKNSLERNN IKQAANNSLL LHLLKSQTIP KPMNGHSHSE RGSIFEESST PTTIDEYSDN 430 440 450 460 470 480 NPSFTDDSSG DESSYSNCVP IDLSCKHRTE KSESDQPVSL DNFTQSLLNT WDPKVPDVDI 490 500 510 520 530 540 KEDQDTSKNS KLNSHQKVTL LQLLLGHKNE ENVEKNTSPQ GVHNDVSKFN TQNYARTSVI 550 560 570 580 590 600 ESPSTNRTTP VSTPPLLTSS KAGSPINLSQ HSLVIKWNSP PYVCSTQSEK LTNTASNHSM 610 620 630 640 650 660 DLTKSKDPPG EKPAQNEGAQ NSATFSASKL LQNLAQCGMQ SSMSVEEQRP SKQLLTGNTD 670 680 690 700 710 720 KPIGMIDRLN SPLLSNKTNA VEENKAFSSQ PTGPEPGLSG SEIENLLERR TVLQLLLGNP 730 740 750 760 770 780 NKGKSEKKEK TPLRDESTQE HSERALSEQI LMVKIKSEPC DDLQIPNTNV HLSHDAKSAP 790 800 810 820 830 840 FLGMAPAVQR SAPALPVSED FKSEPVSPQD FSFSKNGLLS RLLRQNQDSY LADDSDRSHR 850 860 870 880 890 900 NNEMALLESK NLCMVPKKRK LYTEPLENPF KKMKNNIVDA ANNHSAPEVL YGSLLNQEEL 910 920 930 940 950 960 KFSRNDLEFK YPAGHGSASE SEHRSWARES KSFNVLKQLL LSENCVRDLS PHRSNSVADS 970 980 990 1000 1010 1020 KKKGHKNNVT NSKPEFSISS LNGLMYSSTQ PSSCMDNRTF SYPGVVKTPV SPTFPEHLGC 1030 1040 1050 1060 1070 1080 AGSRPESGLL NGCSMPSEKG PIKWVITDAE KNEYEKDSPR LTKTNPILYY MLQKGGNSVT 1090 1100 1110 1120 1130 1140 SRETQDKDIW REASSAESVS QVTAKEELLP TAETKASFFN LRSPYNSHMG NNASRPHSAN 1150 GEVYGLLGSV LTIKKESE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nuclear factor RIP140 modulates transcriptional activation by the estrogen receptor." Cavailles V., Dauvois S., L'Horset F., Lopez G., Hoare S., Kushner P.J., Parker M.G. EMBO J. 14:3741-3751(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH ESR1, SUBCELLULAR LOCATION, VARIANT GLY-448. Tissue: Mammary gland.
[2]	"The DNA sequence of human chromosome 21." Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T., Park H.-S., Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y., Soeda E., Ohki M., Takagi T., Sakaki Y., Taudien S., Blechschmidt K., Polley A. , Menzel U., Delabar J., Kumpf K., Lehmann R., Patterson D., Reichwald K., Rump A., Schillhabel M., Schudy A., Zimmermann W., Rosenthal A., Kudoh J., Shibuya K., Kawasaki K., Asakawa S., Shintani A., Sasaki T., Nagamine K., Mitsuyama S., Antonarakis S.E., Minoshima S., Shimizu N., Nordsiek G., Hornischer K., Brandt P., Scharfe M., Schoen O., Desario A., Reichelt J., Kauer G., Bloecker H., Ramser J., Beck A., Klages S., Hennig S., Riesselmann L., Dagand E., Wehrmeyer S., Borzym K., Gardiner K., Nizetic D., Francis F., Lehrach H., Reinhardt R., Yaspo M.-L. Nature 405:311-319(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	"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: Skin.
[4]	"Regulation of peroxisome proliferator-activated receptor alpha-induced transactivation by the nuclear orphan receptor TAK1/TR4." Yan Z.H., Karam W.G., Staudinger J.L., Medvedev A., Ghanayem B.I., Jetten A.M. J. Biol. Chem. 273:10948-10957(1998) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH NR2C2.
[5]	"Receptor interacting protein RIP140 inhibits both positive and negative gene regulation by glucocorticoids." Subramaniam N., Treuter E., Okret S. J. Biol. Chem. 274:18121-18127(1999) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH NR3C1.
[6]	"Acetylation of nuclear hormone receptor-interacting protein RIP140 regulates binding of the transcriptional corepressor CtBP." Vo N., Fjeld C., Goodman R.H. Mol. Cell. Biol. 21:6181-6188(2001) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH CTBP1, MUTAGENESIS OF 440-PRO--LEU-443 AND LYS-446, ACETYLATION AT LYS-446.
[7]	"Regulation of glucocorticoid receptor activity by 14-3-3-dependent intracellular relocalization of the corepressor RIP140." Zilliacus J., Holter E., Wakui H., Tazawa H., Treuter E., Gustafsson J.-A. Mol. Endocrinol. 15:501-511(2001) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH NR3C1 AND YWHAH, IDENTIFICATION IN A COMPLEX WITH NR3C1 AND YWHAH, SUBCELLULAR LOCATION.
[8]	"A new human MR splice variant is a ligand-independent transactivator modulating corticosteroid action." Zennaro M.-C., Souque A., Viengchareun S., Poisson E., Lombes M. Mol. Endocrinol. 15:1586-1598(2001) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH NR3C2.
[9]	"Regulation of subnuclear localization is associated with a mechanism for nuclear receptor corepression by RIP140." Tazawa H., Osman W., Shoji Y., Treuter E., Gustafsson J.-A., Zilliacus J. Mol. Cell. Biol. 23:4187-4198(2003) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH NR3C1, SUBCELLULAR LOCATION.
[10]	"Receptor-interacting protein 140 binds c-Jun and inhibits estradiol-induced activator protein-1 activity by reversing glucocorticoid receptor-interacting protein 1 effect." Teyssier C., Belguise K., Galtier F., Cavailles V., Chalbos D. Mol. Endocrinol. 17:287-299(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH ESR1; FOS AND JUN.
[11]	"Characterization of four autonomous repression domains in the corepressor receptor interacting protein 140." Christian M., Tullet J.M.A., Parker M.G. J. Biol. Chem. 279:15645-15651(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH CTBP1 AND CTBP2, MUTAGENESIS OF 442-ASP--LEU-443; 567-ASN--LEU-568 AND 948-ASP--LEU-949, IDENTIFICATION OF REPRESSION DOMAINS.
[12]	"Multiple domains of the receptor-interacting protein 140 contribute to transcription inhibition." Castet A., Boulahtouf A., Versini G., Bonnet S., Augereau P., Vignon F., Khochbin S., Jalaguier S., Cavailles V. Nucleic Acids Res. 32:1957-1966(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH CTBP1; CTBP2; HDAC1; HDAC2; HDAC5 AND HDAC6, MUTAGENESIS OF 442-ASP--LEU-443 AND 567-ASN--LEU-568, SUBCELLULAR LOCATION.
[13]	"Modulation of testicular receptor 4 activity by mitogen-activated protein kinase-mediated phosphorylation." Huq M.D., Gupta P., Tsai N.P., Wei L.N. Mol. Cell. Proteomics 5:2072-2082(2006) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH NR2C2.
[14]	"ZNF366 is an estrogen receptor corepressor that acts through CtBP and histone deacetylases." Lopez-Garcia J., Periyasamy M., Thomas R.S., Christian M., Leao M., Jat P., Kindle K.B., Heery D.M., Parker M.G., Buluwela L., Kamalati T., Ali S. Nucleic Acids Res. 34:6126-6136(2006) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH ZNF366.
[15]	"X-ray crystal structures of the estrogen-related receptor-gamma ligand binding domain in three functional states reveal the molecular basis of small molecule regulation." Wang L., Zuercher W.J., Consler T.G., Lambert M.H., Miller A.B., Orband-Miller L.A., McKee D.D., Willson T.M., Nolte R.T. J. Biol. Chem. 281:37773-37781(2006) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 366-390 IN COMPLEX WITH ESRRG.
[16]	"Preliminary molecular genetic analysis of the receptor interacting protein 140 (RIP140) in women affected by endometriosis." Caballero V., Ruiz R., Sainz J.A., Cruz M., Lopez-Nevot M.A., Galan J.J., Real L.M., de Castro F., Lopez-Villaverde V., Ruiz A. J. Exp. Clin. Assist. Reprod. 2:11-11(2005) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS ARG-221; VAL-441; GLY-448; LEU-803 AND PHE-1079.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X84373 mRNA. Translation: CAA59108.1.
AF248484 Genomic DNA. Translation: AAF62185.1.
AF127577 Genomic DNA. Translation: AAF35255.1.
AL163207 Genomic DNA. Translation: CAB90396.1.
BC040361 mRNA. Translation: AAH40361.1.

IPI

IPI00010196.

PIR

S57348.

RefSeq

NP_003480.2. NM_003489.3.

UniGene

Hs.155017.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2GPO	X-ray	1.95	C	366-390	[»]
2GPP	X-ray	2.60	C/D	366-390	[»]

ProteinModelPortal

P48552.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-5964N.

IntAct

P48552. 13 interactions.

MINT

MINT-192711.

STRING

9606.ENSP00000327213.

PTM databases

PhosphoSite

P48552.

Polymorphism databases

DMDM

9988061.

Proteomic databases

PaxDb

P48552.

PRIDE

P48552.

Protocols and materials databases

DNASU

8204.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000318948; ENSP00000327213; ENSG00000180530.
ENST00000400199; ENSP00000383060; ENSG00000180530.
ENST00000400202; ENSP00000383063; ENSG00000180530.

GeneID

8204.

KEGG

hsa:8204.

UCSC

uc002yjx.2. human.

Organism-specific databases

CTD

8204.

GeneCards

GC21M016333.

H-InvDB

HIX0027827.

HGNC

HGNC:8001. NRIP1.

HPA

HPA046571.

MIM

602490. gene.

neXtProt

NX_P48552.

PharmGKB

PA31780.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG47583.

HOGENOM

HOG000236277.

HOVERGEN

HBG052667.

InParanoid

P48552.

OMA

MTHGEEL.

OrthoDB

EOG4H72BC.

PhylomeDB

P48552.

Enzyme and pathway databases

Pathway_Interaction_DB

ar_pathway. Coregulation of Androgen receptor activity.
hnf3apathway. FOXA1 transcription factor network.
retinoic_acid_pathway. Retinoic acid receptors-mediated signaling.

Gene expression databases

ArrayExpress

P48552.

Bgee

P48552.

CleanEx

HS_NRIP1.

Genevestigator

P48552.

GermOnline

ENSG00000180530. Homo sapiens.

Family and domain databases

InterPro

IPR026649. NRIP1.
[Graphical view]

PANTHER

PTHR15088. PTHR15088. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

P48552.

GenomeRNAi

8204.

NextBio

30914.

SOURCE

Search...

Entry information

Entry name

NRIP1_HUMAN

Accession

Primary (citable) accession number: P48552
Secondary accession number(s): Q8IWE8

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1996
Last sequence update:	December 1, 2000
Last modified:	May 1, 2013
This is version 115 of the entry and version 2 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.