Q9NR12 (PDLI7_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
PDZ and LIM domain protein 7

Alternative name(s):
LIM mineralization protein
Short name=LMP
Protein enigma

Gene names

Name:	PDLIM7
Synonyms:	ENIGMA

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	457 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	May function as a scaffold on which the coordinated assembly of proteins can occur. May play a role as an adapter that, via its PDZ domain, localizes LIM-binding proteins to actin filaments of both skeletal muscle and nonmuscle tissues. Involved in both of the two fundamental mechanisms of bone formation, direct bone formation (e.g. embryonic flat bones mandible and cranium), and endochondral bone formation (e.g. embryonic long bone development). Plays a role during fracture repair. Involved in BMP6 signaling pathway By similarity. Ref.1 Ref.2
Subunit structure	Binds via its LIM zinc-binding 3 domain (LIM 3) to endocytic codes of INSR, but not with those of IGF1R, LDLR, TFRC, or EGFR. Interacts with various PKC isoforms through the LIM zinc-binding domains. Binds to RET in a phosphorylation-independent manner via its LIM zinc-binding domain 2 (LIM 2). Probably part of a complex with SHC and the RET dimer. Interacts with TPM2. Interacts with TBX4 and TBX5 By similarity. Ref.1 Ref.6 Ref.7 Ref.8
Subcellular location	Cytoplasm By similarity. Cytoplasm › cytoskeleton By similarity. Note: Colocalizes with RET to the cell periphery and in some cytoskeletal components. Colocalizes with TPM2 near the Z line in muscle. Co-localizes with TBX4 and TBX5 to actin filaments By similarity. Ref.7
Tissue specificity	Isoform 1 and isoform 2 are expressed ubiquitously, however, isoform 2 predominates in skeletal muscle, isoform 1 is more abundant in lung, spleen, leukocytes and fetal liver. Ref.2
Domain	The LIM zinc-binding 2 (LIM 2) domain interacts with TBX4 By similarity. The LIM zinc-binding 3 (LIM 3) domain provides the structural basis for recognition of tyrosine-containing tight turn structures. This domain is necessary and sufficient for interaction with TBX5 By similarity. Anchored to cell periphery via its N-terminal PDZ domain.
Sequence similarities	Contains 3 LIM zinc-binding domains. Contains 1 PDZ (DHR) domain.
Sequence caution	The sequence AAC37565.1 differs from that shown. Reason: Frameshift at positions 103, 128, 161, 183, 195 and 245.

Ontologies

Keywords
Biological process	Differentiation Osteogenesis
Cellular component	Cytoplasm Cytoskeleton
Coding sequence diversity	Alternative splicing Polymorphism
Domain	LIM domain Repeat
Ligand	Metal-binding Zinc
Molecular function	Developmental protein
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	actin cytoskeleton organization Inferred from electronic annotation. Source: Compara cell differentiation Inferred from electronic annotation. Source: UniProtKB-KW multicellular organismal development Inferred from electronic annotation. Source: UniProtKB-KW ossification Inferred from electronic annotation. Source: UniProtKB-KW positive regulation of osteoblast differentiation Inferred from electronic annotation. Source: Compara receptor-mediated endocytosis Traceable author statement Ref.1. Source: ProtInc
Cellular_component	actin cytoskeleton Inferred from direct assay. Source: HPA cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell focal adhesion Inferred from direct assay. Source: HPA ruffle Inferred from electronic annotation. Source: Compara stress fiber Inferred from electronic annotation. Source: Compara
Molecular_function	zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Hoxa1	P09022	3	EBI-350517,EBI-3957603	From a different organism.
UBQLN4	Q9NRR5	2	EBI-350517,EBI-711226

Alternative products

This entry describes 6 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9NR12-1)

Also known as: LMP-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: Q9NR12-2)

Also known as: LMP-2;

The sequence of this isoform differs from the canonical sequence as follows:
     94-133: ASAPAADPPRYTFAPSVSLNKTARPFGAPPPADSAPQQNG → VQTPDK

Note: Did not induce bone induction.

Isoform 3 (identifier: Q9NR12-3)

Also known as: LMP-3;

The sequence of this isoform differs from the canonical sequence as follows:
     134-153: QPLRPLVPDASKQRLMENTE → CRPLTNSRSDRWSQMPASSG
     154-457: Missing.

Note: Same activity as isoform 1 in bone nodule induction.

Isoform 4 (identifier: Q9NR12-4)

The sequence of this isoform differs from the canonical sequence as follows:
     191-287: SQVPRTEAPA...KTPVCHQCHK → RPYRPQPYQP...PRVPPGGVCV
     288-457: Missing.

Note: No experimental confirmation available.

Isoform 5 (identifier: Q9NR12-5)

The sequence of this isoform differs from the canonical sequence as follows:
     192-457: Missing.

Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay. No experimental confirmation available.

Isoform 6 (identifier: Q9NR12-6)

The sequence of this isoform differs from the canonical sequence as follows:
     191-222: SQVPRTEAPAPASSTPQEPWPGPTAPSPTSRP → REKYVLELQSPRYTRLRDWHHQRSAHVLNVQS
     223-457: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 457

457

PDZ and LIM domain protein 7

PRO_0000075881

Regions

Domain

1 – 85

85

PDZ

Domain

280 – 338

59

LIM zinc-binding 1

Domain

339 – 398

60

LIM zinc-binding 2

Domain

399 – 457

59

LIM zinc-binding 3

Amino acid modifications

Modified residue

247

1

Phosphoserine Ref.9

Natural variations

Alternative sequence

94 – 133

40

ASAPA…PQQNG → VQTPDK in isoform 2.

VSP_016509

Alternative sequence

134 – 153

20

QPLRP…MENTE → CRPLTNSRSDRWSQMPASSG in isoform 3.

VSP_016510

Alternative sequence

154 – 457

304

Missing in isoform 3.

VSP_016513

Alternative sequence

191 – 287

97

SQVPR…HQCHK → RPYRPQPYQPPALGCGPCVC RALCPGQNEHSADPAQPAGH AHAAAEPHLHCAGSCRRGAR RGQQQRQDSRVSPVPQGHPG PLPGGAGPRVPPGGVCV in isoform 4.

VSP_016511

Alternative sequence

191 – 222

32

SQVPR…PTSRP → REKYVLELQSPRYTRLRDWH HQRSAHVLNVQS in isoform 6.

VSP_016512

Alternative sequence

192 – 457

266

Missing in isoform 5.

VSP_016514

Alternative sequence

223 – 457

235

Missing in isoform 6.

VSP_016515

Alternative sequence

288 – 457

170

Missing in isoform 4.

VSP_016516

Natural variant

326

1

A → T.
Corresponds to variant rs2306764 [ dbSNP | Ensembl ].

VAR_050168

Natural variant

450

1

K → N in a breast cancer sample; somatic mutation. Ref.13

VAR_036193

Experimental info

Mutagenesis

15 – 16

2

GF → AA: Loss of binding to TPM2.

Mutagenesis

63

1

H → A: Loss of binding to TPM2. Ref.8

Sequence conflict

138

1

P → Q in BC067806. Ref.4

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

457

Helix Strand Turn

Details...

Beta strand

1 – 12

12

Beta strand

16 – 21

6

Helix

22 – 24

3

Beta strand

26 – 33

8

Helix

38 – 41

4

Beta strand

49 – 53

5

Helix

58 – 60

3

Helix

63 – 71

9

Beta strand

76 – 84

9

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (LMP-1) [UniParc]. Last modified October 1, 2000. Version 1. Checksum: AA37F9E8E987D990	FASTA	457	49,845
	10 20 30 40 50 60 MDSFKVVLEG PAPWGFRLQG GKDFNVPLSI SRLTPGGKAA QAGVAVGDWV LSIDGENAGS 70 80 90 100 110 120 LTHIEAQNKI RACGERLSLG LSRAQPVQSK PQKASAPAAD PPRYTFAPSV SLNKTARPFG 130 140 150 160 170 180 APPPADSAPQ QNGQPLRPLV PDASKQRLME NTEDWRPRPG TGQSRSFRIL AHLTGTEFMQ 190 200 210 220 230 240 DPDEEHLKKS SQVPRTEAPA PASSTPQEPW PGPTAPSPTS RPPWAVDPAF AERYAPDKTS 250 260 270 280 290 300 TVLTRHSQPA TPTPLQSRTS IVQAAAGGVP GGGSNNGKTP VCHQCHKVIR GRYLVALGHA 310 320 330 340 350 360 YHPEEFVCSQ CGKVLEEGGF FEEKGAIFCP PCYDVRYAPS CAKCKKKITG EIMHALKMTW 370 380 390 400 410 420 HVHCFTCAAC KTPIRNRAFY MEEGVPYCER DYEKMFGTKC HGCDFKIDAG DRFLEALGFS 430 440 450 WHDTCFVCAI CQINLEGKTF YSKKDRPLCK SHAFSHV
	Isoform 2 (LMP-2) [UniParc]. Checksum: 486E854CABB4D494	FASTA	423	46,510
	10 20 30 40 50 60 MDSFKVVLEG PAPWGFRLQG GKDFNVPLSI SRLTPGGKAA QAGVAVGDWV LSIDGENAGS 70 80 90 100 110 120 LTHIEAQNKI RACGERLSLG LSRAQPVQSK PQKVQTPDKQ PLRPLVPDAS KQRLMENTED 130 140 150 160 170 180 WRPRPGTGQS RSFRILAHLT GTEFMQDPDE EHLKKSSQVP RTEAPAPASS TPQEPWPGPT 190 200 210 220 230 240 APSPTSRPPW AVDPAFAERY APDKTSTVLT RHSQPATPTP LQSRTSIVQA AAGGVPGGGS 250 260 270 280 290 300 NNGKTPVCHQ CHKVIRGRYL VALGHAYHPE EFVCSQCGKV LEEGGFFEEK GAIFCPPCYD 310 320 330 340 350 360 VRYAPSCAKC KKKITGEIMH ALKMTWHVHC FTCAACKTPI RNRAFYMEEG VPYCERDYEK 370 380 390 400 410 420 MFGTKCHGCD FKIDAGDRFL EALGFSWHDT CFVCAICQIN LEGKTFYSKK DRPLCKSHAF SHV
	Isoform 3 (LMP-3) [UniParc]. Checksum: 257AD5C3CD61F6F1	FASTA	153	16,034
	10 20 30 40 50 60 MDSFKVVLEG PAPWGFRLQG GKDFNVPLSI SRLTPGGKAA QAGVAVGDWV LSIDGENAGS 70 80 90 100 110 120 LTHIEAQNKI RACGERLSLG LSRAQPVQSK PQKASAPAAD PPRYTFAPSV SLNKTARPFG 130 140 150 APPPADSAPQ QNGCRPLTNS RSDRWSQMPA SSG
	Isoform 4 [UniParc]. Checksum: 7B30CF3E6197899C	FASTA	287	30,411
	10 20 30 40 50 60 MDSFKVVLEG PAPWGFRLQG GKDFNVPLSI SRLTPGGKAA QAGVAVGDWV LSIDGENAGS 70 80 90 100 110 120 LTHIEAQNKI RACGERLSLG LSRAQPVQSK PQKASAPAAD PPRYTFAPSV SLNKTARPFG 130 140 150 160 170 180 APPPADSAPQ QNGQPLRPLV PDASKQRLME NTEDWRPRPG TGQSRSFRIL AHLTGTEFMQ 190 200 210 220 230 240 DPDEEHLKKS RPYRPQPYQP PALGCGPCVC RALCPGQNEH SADPAQPAGH AHAAAEPHLH 250 260 270 280 CAGSCRRGAR RGQQQRQDSR VSPVPQGHPG PLPGGAGPRV PPGGVCV
	Isoform 5 [UniParc]. Checksum: B9B6B99E12B23B25	FASTA	191	20,514
	10 20 30 40 50 60 MDSFKVVLEG PAPWGFRLQG GKDFNVPLSI SRLTPGGKAA QAGVAVGDWV LSIDGENAGS 70 80 90 100 110 120 LTHIEAQNKI RACGERLSLG LSRAQPVQSK PQKASAPAAD PPRYTFAPSV SLNKTARPFG 130 140 150 160 170 180 APPPADSAPQ QNGQPLRPLV PDASKQRLME NTEDWRPRPG TGQSRSFRIL AHLTGTEFMQ 190 DPDEEHLKKS S
	Isoform 6 [UniParc]. Checksum: ADF21719E4928621	FASTA	222	24,413
	10 20 30 40 50 60 MDSFKVVLEG PAPWGFRLQG GKDFNVPLSI SRLTPGGKAA QAGVAVGDWV LSIDGENAGS 70 80 90 100 110 120 LTHIEAQNKI RACGERLSLG LSRAQPVQSK PQKASAPAAD PPRYTFAPSV SLNKTARPFG 130 140 150 160 170 180 APPPADSAPQ QNGQPLRPLV PDASKQRLME NTEDWRPRPG TGQSRSFRIL AHLTGTEFMQ 190 200 210 220 DPDEEHLKKS REKYVLELQS PRYTRLRDWH HQRSAHVLNV QS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"LIM domain recognition of a tyrosine-containing tight turn." Wu R.-Y., Gill G.N. J. Biol. Chem. 269:25085-25090(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, INTERACTION WITH INSR.
[2]	"Overexpressed LIM mineralization proteins do not require LIM domains to induce bone." Liu Y., Hair G.A., Boden S.D., Viggeswarapu M., Titus L. J. Bone Miner. Res. 17:406-414(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), FUNCTION, TISSUE SPECIFICITY, ALTERNATIVE SPLICING. Tissue: Heart.
[3]	"Enigma sequence and interaction with Ret." Borrello M.G., Billaud M., Mercalli E., Ghizzoni S., Bidaud C. Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Neuroepithelium.
[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] (ISOFORMS 1; 4; 5 AND 6). Tissue: Brain, Kidney, Mammary gland and Uterus.
[5]	Bienvenut W.V., Claeys D. Submitted (NOV-2005) to UniProtKB Cited for: PROTEIN SEQUENCE OF 6-17; 94-103 AND 246-258, MASS SPECTROMETRY. Tissue: Platelet.
[6]	"Protein-protein interaction of zinc finger LIM domains with protein kinase C." Kuroda S., Tokunaga C., Kiyohara Y., Higuchi O., Konishi H., Mizuno K., Gill G.N., Kikkawa U. J. Biol. Chem. 271:31029-31032(1996) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PKC.
[7]	"Shc and Enigma are both required for mitogenic signaling by Ret/ptc2." Durick K., Gill G.N., Taylor S.S. Mol. Cell. Biol. 18:2298-2308(1998) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, INTERACTION WITH RET AND SHC1.
[8]	"The PDZ domain of the LIM protein enigma binds to beta-tropomyosin." Guy P.M., Kenny D.A., Gill G.N. Mol. Biol. Cell 10:1973-1984(1999) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH TPM2, MUTAGENESIS OF 15-GLY-PHE-16 AND HIS-63.
[9]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-247, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[11]	"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] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]	"Structure of the PDZ domain of human PDLIM7 bound to a C-terminal extension from human beta-tropomyosin." Structural genomics consortium (SGC) Submitted (FEB-2009) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (1.11 ANGSTROMS) OF 1-84.
[13]	"The consensus coding sequences of human breast and colorectal cancers." Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E. Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] ASN-450.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

L35240 Genomic DNA. Translation: AAC37565.1. Frameshift.
AF345904 mRNA. Translation: AAK30567.1.
AF345905 mRNA. Translation: AAK30568.1.
AF345906 mRNA. Translation: AAK30569.1.
AF265209 mRNA. Translation: AAF76152.1.
BC001093 mRNA. Translation: AAH01093.1.
BC014521 mRNA. Translation: AAH14521.1.
BC067806 mRNA. No translation available.
BC084575 mRNA. Translation: AAH84575.1.

IPI

IPI00023122.
IPI00023560.
IPI00030835.
IPI00060308.
IPI00478185.
IPI00655883.

PIR

A55050.

RefSeq

NP_005442.2. NM_005451.3.
NP_976227.1. NM_203352.1.
NP_998801.1. NM_213636.1.

UniGene

Hs.533040.
Hs.736984.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2Q3G	X-ray	1.11	A/B	1-84	[»]

ProteinModelPortal

Q9NR12.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9NR12. 22 interactions.

MINT

MINT-94304.

STRING

9606.ENSP00000348099.

PTM databases

PhosphoSite

Q9NR12.

Polymorphism databases

DMDM

74752914.

Proteomic databases

PaxDb

Q9NR12.

PRIDE

Q9NR12.

Protocols and materials databases

DNASU

9260.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000355572; ENSP00000347776; ENSG00000196923.
ENST00000355841; ENSP00000348099; ENSG00000196923.
ENST00000356618; ENSP00000349030; ENSG00000196923.
ENST00000359895; ENSP00000352964; ENSG00000196923.
ENST00000393551; ENSP00000377182; ENSG00000196923.
ENST00000486828; ENSP00000439157; ENSG00000196923.
ENST00000493815; ENSP00000431236; ENSG00000196923.

GeneID

9260.

KEGG

hsa:9260.

UCSC

uc003mha.1. human.
uc003mhb.1. human.
uc003mhf.3. human.
uc003mhg.1. human.

Organism-specific databases

CTD

9260.

GeneCards

GC05M176912.

HGNC

HGNC:22958. PDLIM7.

HPA

HPA018794.

MIM

605903. gene.

neXtProt

NX_Q9NR12.

PharmGKB

PA128394546.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG286537.

HOVERGEN

HBG051478.

InParanoid

Q9NR12.

OMA

ATPTPMQ.

PhylomeDB

Q9NR12.

Enzyme and pathway databases

Pathway_Interaction_DB

ret_pathway. Signaling events regulated by Ret tyrosine kinase.

Gene expression databases

ArrayExpress

Q9NR12.

Bgee

Q9NR12.

CleanEx

HS_PDLIM7.

Genevestigator

Q9NR12.

GermOnline

ENSG00000196923. Homo sapiens.

Family and domain databases

Gene3D

2.10.110.10. 3 hits.

InterPro

IPR001478. PDZ.
IPR001781. Znf_LIM.
[Graphical view]

Pfam

PF00412. LIM. 3 hits.
PF00595. PDZ. 1 hit.
[Graphical view]

SMART

SM00132. LIM. 3 hits.
SM00228. PDZ. 1 hit.
[Graphical view]

SUPFAM

SSF50156. PDZ. 1 hit.

PROSITE

PS00478. LIM_DOMAIN_1. 2 hits.
PS50023. LIM_DOMAIN_2. 3 hits.
PS50106. PDZ. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

PDLIM7. human.

EvolutionaryTrace

Q9NR12.

GenomeRNAi

9260.

NextBio

34707.

SOURCE

Search...

Entry information

Entry name

PDLI7_HUMAN

Accession

Primary (citable) accession number: Q9NR12
Secondary accession number(s): Q14250 , Q5XG82, Q6NVZ5, Q96C91, Q9BXB8, Q9BXB9

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 6, 2005
Last sequence update:	October 1, 2000
Last modified:	May 29, 2013
This is version 108 of the entry and version 1 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.