SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q9NR12

- PDLI7_HUMAN

UniProt

Q9NR12 - PDLI7_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

PDZ and LIM domain protein 7

Gene
PDLIM7, ENIGMA
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.2 Publications

GO - Molecular functioni

  1. protein binding Source: IntAct
  2. zinc ion binding Source: InterPro

GO - Biological processi

  1. actin cytoskeleton organization Source: Ensembl
  2. cell differentiation Source: UniProtKB-KW
  3. multicellular organismal development Source: UniProtKB-KW
  4. ossification Source: UniProtKB-KW
  5. positive regulation of osteoblast differentiation Source: Ensembl
  6. receptor-mediated endocytosis Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Differentiation, Osteogenesis

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
PDZ and LIM domain protein 7
Alternative name(s):
LIM mineralization protein
Short name:
LMP
Protein enigma
Gene namesi
Name:PDLIM7
Synonyms:ENIGMA
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 5

Organism-specific databases

HGNCiHGNC:22958. PDLIM7.

Subcellular locationi

Cytoplasm By similarity. Cytoplasmcytoskeleton By similarity
Note: Colocalizes with RET to the cell periphery and in some cytoskeletal components. Colocalizes with TPM2 near the Z line in muscle. Colocalizes with TBX4 and TBX5 to actin filaments By similarity.1 Publication

GO - Cellular componenti

  1. actin cytoskeleton Source: HPA
  2. cytoplasm Source: UniProtKB-SubCell
  3. focal adhesion Source: HPA
  4. nucleus Source: HPA
  5. ruffle Source: Ensembl
  6. stress fiber Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi15 – 162GF → AA: Loss of binding to TPM2.
Mutagenesisi63 – 631H → A: Loss of binding to TPM2. 1 Publication

Organism-specific databases

PharmGKBiPA128394546.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 457457PDZ and LIM domain protein 7PRO_0000075881Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei247 – 2471Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9NR12.
PaxDbiQ9NR12.
PRIDEiQ9NR12.

PTM databases

PhosphoSiteiQ9NR12.

Expressioni

Tissue specificityi

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.1 Publication

Gene expression databases

ArrayExpressiQ9NR12.
BgeeiQ9NR12.
CleanExiHS_PDLIM7.
GenevestigatoriQ9NR12.

Organism-specific databases

HPAiHPA018794.
HPA048815.

Interactioni

Subunit structurei

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.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Hoxa1P090223EBI-350517,EBI-3957603From a different organism.
UBQLN4Q9NRR52EBI-350517,EBI-711226

Protein-protein interaction databases

BioGridi114682. 42 interactions.
IntActiQ9NR12. 26 interactions.
MINTiMINT-94304.
STRINGi9606.ENSP00000348099.

Structurei

Secondary structure

457
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi1 – 1212
Beta strandi16 – 216
Helixi22 – 243
Beta strandi26 – 338
Helixi38 – 414
Beta strandi49 – 535
Helixi58 – 603
Helixi63 – 719
Beta strandi76 – 849

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2Q3GX-ray1.11A/B1-84[»]
ProteinModelPortaliQ9NR12.
SMRiQ9NR12. Positions 1-84, 278-451.

Miscellaneous databases

EvolutionaryTraceiQ9NR12.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 8585PDZAdd
BLAST
Domaini280 – 33859LIM zinc-binding 1Add
BLAST
Domaini339 – 39860LIM zinc-binding 2Add
BLAST
Domaini399 – 45759LIM zinc-binding 3Add
BLAST

Domaini

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 similaritiesi

Contains 1 PDZ (DHR) domain.

Keywords - Domaini

LIM domain, Repeat

Phylogenomic databases

eggNOGiNOG286537.
HOVERGENiHBG051478.
InParanoidiQ9NR12.
OMAiWPGPTAP.
OrthoDBiEOG7HXCQB.
PhylomeDBiQ9NR12.
TreeFamiTF106408.

Family and domain databases

Gene3Di2.10.110.10. 3 hits.
2.30.42.10. 1 hit.
InterProiIPR001478. PDZ.
IPR001781. Znf_LIM.
[Graphical view]
PfamiPF00412. LIM. 3 hits.
PF00595. PDZ. 1 hit.
[Graphical view]
SMARTiSM00132. LIM. 3 hits.
SM00228. PDZ. 1 hit.
[Graphical view]
SUPFAMiSSF50156. SSF50156. 1 hit.
PROSITEiPS00478. LIM_DOMAIN_1. 2 hits.
PS50023. LIM_DOMAIN_2. 3 hits.
PS50106. PDZ. 1 hit.
[Graphical view]

Sequences (6)i

Sequence statusi: Complete.

This entry describes 6 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9NR12-1) [UniParc]FASTAAdd to Basket

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.

« Hide

MDSFKVVLEG PAPWGFRLQG GKDFNVPLSI SRLTPGGKAA QAGVAVGDWV    50
LSIDGENAGS LTHIEAQNKI RACGERLSLG LSRAQPVQSK PQKASAPAAD 100
PPRYTFAPSV SLNKTARPFG APPPADSAPQ QNGQPLRPLV PDASKQRLME 150
NTEDWRPRPG TGQSRSFRIL AHLTGTEFMQ DPDEEHLKKS SQVPRTEAPA 200
PASSTPQEPW PGPTAPSPTS RPPWAVDPAF AERYAPDKTS TVLTRHSQPA 250
TPTPLQSRTS IVQAAAGGVP GGGSNNGKTP VCHQCHKVIR GRYLVALGHA 300
YHPEEFVCSQ CGKVLEEGGF FEEKGAIFCP PCYDVRYAPS CAKCKKKITG 350
EIMHALKMTW HVHCFTCAAC KTPIRNRAFY MEEGVPYCER DYEKMFGTKC 400
HGCDFKIDAG DRFLEALGFS WHDTCFVCAI CQINLEGKTF YSKKDRPLCK 450
SHAFSHV 457
Length:457
Mass (Da):49,845
Last modified:October 1, 2000 - v1
Checksum:iAA37F9E8E987D990
GO
Isoform 2 (identifier: Q9NR12-2) [UniParc]FASTAAdd to Basket

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.

Show »
Length:423
Mass (Da):46,510
Checksum:i486E854CABB4D494
GO
Isoform 3 (identifier: Q9NR12-3) [UniParc]FASTAAdd to Basket

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.

Show »
Length:153
Mass (Da):16,034
Checksum:i257AD5C3CD61F6F1
GO
Isoform 4 (identifier: Q9NR12-4) [UniParc]FASTAAdd to Basket

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.

Show »
Length:287
Mass (Da):30,411
Checksum:i7B30CF3E6197899C
GO
Isoform 5 (identifier: Q9NR12-5) [UniParc]FASTAAdd to Basket

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.

Show »
Length:191
Mass (Da):20,514
Checksum:iB9B6B99E12B23B25
GO
Isoform 6 (identifier: Q9NR12-6) [UniParc]FASTAAdd to Basket

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

Note: No experimental confirmation available.

Show »
Length:222
Mass (Da):24,413
Checksum:iADF21719E4928621
GO

Sequence cautioni

The sequence AAC37565.1 differs from that shown. Reason: Frameshift at positions 103, 128, 161, 183, 195 and 245.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti326 – 3261A → T.
Corresponds to variant rs2306764 [ dbSNP | Ensembl ].
VAR_050168
Natural varianti450 – 4501K → N in a breast cancer sample; somatic mutation. 1 Publication
VAR_036193

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei94 – 13340ASAPA…PQQNG → VQTPDK in isoform 2. VSP_016509Add
BLAST
Alternative sequencei134 – 15320QPLRP…MENTE → CRPLTNSRSDRWSQMPASSG in isoform 3. VSP_016510Add
BLAST
Alternative sequencei154 – 457304Missing in isoform 3. VSP_016513Add
BLAST
Alternative sequencei191 – 28797SQVPR…HQCHK → RPYRPQPYQPPALGCGPCVC RALCPGQNEHSADPAQPAGH AHAAAEPHLHCAGSCRRGAR RGQQQRQDSRVSPVPQGHPG PLPGGAGPRVPPGGVCV in isoform 4. VSP_016511Add
BLAST
Alternative sequencei191 – 22232SQVPR…PTSRP → REKYVLELQSPRYTRLRDWH HQRSAHVLNVQS in isoform 6. VSP_016512Add
BLAST
Alternative sequencei192 – 457266Missing in isoform 5. VSP_016514Add
BLAST
Alternative sequencei223 – 457235Missing in isoform 6. VSP_016515Add
BLAST
Alternative sequencei288 – 457170Missing in isoform 4. VSP_016516Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti138 – 1381P → Q in BC067806. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS4422.1. [Q9NR12-1]
CCDS4423.1. [Q9NR12-2]
CCDS4424.1. [Q9NR12-6]
PIRiA55050.
RefSeqiNP_005442.2. NM_005451.4. [Q9NR12-1]
NP_976227.1. NM_203352.2. [Q9NR12-2]
NP_998801.1. NM_213636.2. [Q9NR12-6]
UniGeneiHs.533040.
Hs.736984.

Genome annotation databases

EnsembliENST00000355572; ENSP00000347776; ENSG00000196923. [Q9NR12-6]
ENST00000355841; ENSP00000348099; ENSG00000196923. [Q9NR12-1]
ENST00000356618; ENSP00000349030; ENSG00000196923. [Q9NR12-4]
ENST00000359895; ENSP00000352964; ENSG00000196923. [Q9NR12-2]
ENST00000393551; ENSP00000377182; ENSG00000196923. [Q9NR12-4]
ENST00000486828; ENSP00000439157; ENSG00000196923. [Q9NR12-5]
ENST00000493815; ENSP00000431236; ENSG00000196923. [Q9NR12-3]
GeneIDi9260.
KEGGihsa:9260.
UCSCiuc003mha.1. human. [Q9NR12-1]
uc003mhb.1. human. [Q9NR12-2]
uc003mhf.3. human. [Q9NR12-4]
uc003mhg.1. human. [Q9NR12-6]

Polymorphism databases

DMDMi74752914.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS4422.1. [Q9NR12-1 ]
CCDS4423.1. [Q9NR12-2 ]
CCDS4424.1. [Q9NR12-6 ]
PIRi A55050.
RefSeqi NP_005442.2. NM_005451.4. [Q9NR12-1 ]
NP_976227.1. NM_203352.2. [Q9NR12-2 ]
NP_998801.1. NM_213636.2. [Q9NR12-6 ]
UniGenei Hs.533040.
Hs.736984.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2Q3G X-ray 1.11 A/B 1-84 [» ]
ProteinModelPortali Q9NR12.
SMRi Q9NR12. Positions 1-84, 278-451.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 114682. 42 interactions.
IntActi Q9NR12. 26 interactions.
MINTi MINT-94304.
STRINGi 9606.ENSP00000348099.

PTM databases

PhosphoSitei Q9NR12.

Polymorphism databases

DMDMi 74752914.

Proteomic databases

MaxQBi Q9NR12.
PaxDbi Q9NR12.
PRIDEi Q9NR12.

Protocols and materials databases

DNASUi 9260.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000355572 ; ENSP00000347776 ; ENSG00000196923 . [Q9NR12-6 ]
ENST00000355841 ; ENSP00000348099 ; ENSG00000196923 . [Q9NR12-1 ]
ENST00000356618 ; ENSP00000349030 ; ENSG00000196923 . [Q9NR12-4 ]
ENST00000359895 ; ENSP00000352964 ; ENSG00000196923 . [Q9NR12-2 ]
ENST00000393551 ; ENSP00000377182 ; ENSG00000196923 . [Q9NR12-4 ]
ENST00000486828 ; ENSP00000439157 ; ENSG00000196923 . [Q9NR12-5 ]
ENST00000493815 ; ENSP00000431236 ; ENSG00000196923 . [Q9NR12-3 ]
GeneIDi 9260.
KEGGi hsa:9260.
UCSCi uc003mha.1. human. [Q9NR12-1 ]
uc003mhb.1. human. [Q9NR12-2 ]
uc003mhf.3. human. [Q9NR12-4 ]
uc003mhg.1. human. [Q9NR12-6 ]

Organism-specific databases

CTDi 9260.
GeneCardsi GC05M176912.
HGNCi HGNC:22958. PDLIM7.
HPAi HPA018794.
HPA048815.
MIMi 605903. gene.
neXtProti NX_Q9NR12.
PharmGKBi PA128394546.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG286537.
HOVERGENi HBG051478.
InParanoidi Q9NR12.
OMAi WPGPTAP.
OrthoDBi EOG7HXCQB.
PhylomeDBi Q9NR12.
TreeFami TF106408.

Miscellaneous databases

ChiTaRSi PDLIM7. human.
EvolutionaryTracei Q9NR12.
GeneWikii PDLIM7.
GenomeRNAii 9260.
NextBioi 34707.
PROi Q9NR12.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9NR12.
Bgeei Q9NR12.
CleanExi HS_PDLIM7.
Genevestigatori Q9NR12.

Family and domain databases

Gene3Di 2.10.110.10. 3 hits.
2.30.42.10. 1 hit.
InterProi IPR001478. PDZ.
IPR001781. Znf_LIM.
[Graphical view ]
Pfami PF00412. LIM. 3 hits.
PF00595. PDZ. 1 hit.
[Graphical view ]
SMARTi SM00132. LIM. 3 hits.
SM00228. PDZ. 1 hit.
[Graphical view ]
SUPFAMi SSF50156. SSF50156. 1 hit.
PROSITEi PS00478. LIM_DOMAIN_1. 2 hits.
PS50023. LIM_DOMAIN_2. 3 hits.
PS50106. PDZ. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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, IDENTIFICATION BY 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. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-247, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "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.
  14. Cited for: VARIANT [LARGE SCALE ANALYSIS] ASN-450.

Entry informationi

Entry nameiPDLI7_HUMAN
AccessioniPrimary (citable) accession number: Q9NR12
Secondary accession number(s): Q14250
, Q5XG82, Q6NVZ5, Q96C91, Q9BXB8, Q9BXB9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 6, 2005
Last sequence update: October 1, 2000
Last modified: July 9, 2014
This is version 120 of the entry and version 1 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 5
    Human chromosome 5: 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