O60711 (LPXN_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Leupaxin

Gene names

Name:	LPXN
Synonyms:	LDLP

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

General annotation (Comments)

Function	Transcriptional coactivator for androgen receptor (AR) and serum response factor (SRF). Contributes to the regulation of cell adhesion, spreading and cell migration and acts as a negative regulator in integrin-mediated cell adhesion events. Suppresses the integrin-induced tyrosine phosphorylation of paxillin (PXN). May play a critical role as an adapter protein in the formation of the adhesion zone in osteoclasts. Negatively regulates B-cell antigen receptor (BCR) signaling. Ref.13 Ref.14 Ref.15 Ref.17
Subunit structure	Interacts with PTPN22 By similarity. Interacts with unphosphorylated ITGA4. Interacts with PTK2B/PYK2, PTPN12, AR and SRF. Interacts (via LD motif 3) with LYN and the interaction is induced upon B-cell antigen receptor (BCR) activation. Interacts (via LD motif 3) with PTK2/FAK. Ref.1 Ref.8 Ref.12 Ref.13 Ref.14 Ref.15
Subcellular location	Cytoplasm. Cell junction › focal adhesion. Nucleus. Cytoplasm › perinuclear region By similarity. Cell projection › podosome. Cell membrane. Note: Shuttles between the cytoplasm and nucleus. Recruited to the cell membrane following B-cell antigen receptor (BCR) cross-linking in B-cells. Enhanced focal adhesion kinase activity (PTK2/FAK) attenuates its nuclear accumulation and limits its ability to enhance serum response factor (SRF)-dependent gene transcription. Targeting to focal adhesions is essential for its tyrosine phosphorylation in response to bombesin. Ref.9 Ref.12 Ref.13 Ref.14 Ref.15 Ref.17
Tissue specificity	Macrophages, monocytes and osteoclasts (at protein level). Strongly expressed in cells and tissues of hematopoietic origin. Highest expression in lymphoid tissues such as spleen, lymph node, thymus and appendix and in the vascular smooth muscle. Lower levels in bone marrow and fetal liver. Also expressed in peripheral blood lymphocytes and a number of hematopoietic cell lines. Very low levels found in epithelial cell lines. Expressed in prostate cancer (PCa) cells and its expression intensity is directly linked to PCa progression. Ref.9 Ref.14 Ref.15
Domain	The LIM domain 3 is critical for focal adhesion targeting and the suppression of paxillin (PXN) tyrosine phosphorylation. The LIM domain 3 alone or both LIM domains 3 and 4 can mediate interaction with AR.
Post-translational modification	Phosphorylated on tyrosine residues. Phosphorylation on Tyr-72 is important for its inhibitory function. Bombesin stimulates phosphorylation on Tyr-22, Tyr-62 and Tyr-72. Ref.13 Ref.17
Sequence similarities	Belongs to the paxillin family. Contains 4 LIM zinc-binding domains.

Ontologies

Keywords
Biological process	Cell adhesion Transcription Transcription regulation
Cellular component	Cell junction Cell membrane Cell projection Cytoplasm Membrane Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Domain	LIM domain Repeat
Ligand	Metal-binding Zinc
Molecular function	Activator
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell adhesion Non-traceable author statement Ref.1. Source: ProtInc negative regulation of B cell receptor signaling pathway Inferred from direct assay Ref.13. Source: UniProtKB negative regulation of cell adhesion Inferred from direct assay Ref.17. Source: UniProtKB protein complex assembly Traceable author statement Ref.1. Source: ProtInc regulation of cell adhesion mediated by integrin Inferred from electronic annotation. Source: Compara regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW signal transduction Traceable author statement Ref.1. Source: ProtInc transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cell projection Inferred from electronic annotation. Source: UniProtKB-KW cytoplasm Inferred from direct assay Ref.13Ref.15Ref.14. Source: UniProtKB focal adhesion Inferred from direct assay Ref.15Ref.14Ref.17. Source: UniProtKB nucleus Inferred from direct assay Ref.15Ref.14. Source: UniProtKB perinuclear region of cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from direct assay Ref.13. Source: UniProtKB podosome Inferred from direct assay Ref.9. Source: UniProtKB
Molecular_function	transcription cofactor activity Inferred from direct assay Ref.15Ref.14. Source: UniProtKB zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Hoxa1	P09022	3	EBI-744222,EBI-3957603	From a different organism.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: O60711-1)

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: O60711-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-4: MEEL → MSTLLISSS

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 386

386

Leupaxin

PRO_0000075836

Regions

Domain

150 – 208

59

LIM zinc-binding 1

Domain

209 – 267

59

LIM zinc-binding 2

Domain

268 – 326

59

LIM zinc-binding 3

Domain

327 – 386

60

LIM zinc-binding 4

Motif

3 – 15

13

LD motif 1

Motif

70 – 82

13

LD motif 2

Motif

92 – 103

12

LD motif 3

Amino acid modifications

Modified residue

19

1

Phosphoserine Ref.10

Modified residue

22

1

Phosphotyrosine Ref.17

Modified residue

62

1

Phosphotyrosine Ref.17

Modified residue

72

1

Phosphotyrosine; by LYN Ref.13 Ref.17

Natural variations

Alternative sequence

1 – 4

4

MEEL → MSTLLISSS in isoform 2.

VSP_042655

Natural variant

148

1

P → T.
Corresponds to variant rs12271558 [ dbSNP | Ensembl ].

VAR_050152

Experimental info

Sequence conflict

2

1

E → D in CAG38768. Ref.3

Sequence conflict

14

1

S → T in BAD96885. Ref.4

Sequence conflict

100

1

L → M in CAG38768. Ref.3

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

386

Helix Strand Turn

Details...

Turn

271 – 273

3

Beta strand

282 – 284

3

Beta strand

287 – 289

3

Turn

291 – 293

3

Beta strand

297 – 299

3

Beta strand

309 – 313

5

Helix

318 – 325

8

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified August 1, 1998. Version 1. Checksum: C8D2BE61FAB11F3A	FASTA	386	43,332
	10 20 30 40 50 60 MEELDALLEE LERSTLQDSD EYSNPAPLPL DQHSRKETNL DETSEILSIQ DNTSPLPAQL 70 80 90 100 110 120 VYTTNIQELN VYSEAQEPKE SPPPSKTSAA AQLDELMAHL TEMQAKVAVR ADAGKKHLPD 130 140 150 160 170 180 KQDHKASLDS MLGGLEQELQ DLGIATVPKG HCASCQKPIA GKVIHALGQS WHPEHFVCTH 190 200 210 220 230 240 CKEEIGSSPF FERSGLAYCP NDYHQLFSPR CAYCAAPILD KVLTAMNQTW HPEHFFCSHC 250 260 270 280 290 300 GEVFGAEGFH EKDKKPYCRK DFLAMFSPKC GGCNRPVLEN YLSAMDTVWH PECFVCGDCF 310 320 330 340 350 360 TSFSTGSFFE LDGRPFCELH YHHRRGTLCH GCGQPITGRC ISAMGYKFHP EHFVCAFCLT 370 380 QLSKGIFREQ NDKTYCQPCF NKLFPL
	Isoform 2 [UniParc]. Checksum: A8F1FFD11D4DB7BD	FASTA	391	43,750
	10 20 30 40 50 60 MSTLLISSSD ALLEELERST LQDSDEYSNP APLPLDQHSR KETNLDETSE ILSIQDNTSP 70 80 90 100 110 120 LPAQLVYTTN IQELNVYSEA QEPKESPPPS KTSAAAQLDE LMAHLTEMQA KVAVRADAGK 130 140 150 160 170 180 KHLPDKQDHK ASLDSMLGGL EQELQDLGIA TVPKGHCASC QKPIAGKVIH ALGQSWHPEH 190 200 210 220 230 240 FVCTHCKEEI GSSPFFERSG LAYCPNDYHQ LFSPRCAYCA APILDKVLTA MNQTWHPEHF 250 260 270 280 290 300 FCSHCGEVFG AEGFHEKDKK PYCRKDFLAM FSPKCGGCNR PVLENYLSAM DTVWHPECFV 310 320 330 340 350 360 CGDCFTSFST GSFFELDGRP FCELHYHHRR GTLCHGCGQP ITGRCISAMG YKFHPEHFVC 370 380 390 AFCLTQLSKG IFREQNDKTY CQPCFNKLFP L

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Leupaxin is a novel LIM domain protein that forms a complex with PYK2." Lipsky B.P., Beals C.R., Staunton D.E. J. Biol. Chem. 273:11709-11713(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH PTK2B/PYK2, CHARACTERIZATION. Tissue: Spleen.
[2]	"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] (ISOFORMS 1 AND 2). Tissue: Small intestine and Spleen.
[3]	"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] (ISOFORM 1).
[4]	Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S. Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Lung.
[5]	"Human chromosome 11 DNA sequence and analysis including novel gene identification." Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G. , Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S., Sakaki Y. Nature 440:497-500(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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 (JUL-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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: B-cell.
[8]	"Binding of paxillin to alpha4 integrins modifies integrin-dependent biological responses." Liu S., Thomas S.M., Woodside D.G., Rose D.M., Kiosses W.B., Pfaff M., Ginsberg M.H. Nature 402:676-681(1999) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH ITGA4.
[9]	"Leupaxin is a critical adaptor protein in the adhesion zone of the osteoclast." Gupta A., Lee B.S., Khadeer M.A., Tang Z., Chellaiah M., Abu-Amer Y., Goldknopf J., Hruska K.A. J. Bone Miner. Res. 18:669-685(2003) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[10]	"Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry." Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M., Peters E.C. Anal. Chem. 76:2763-2772(2004) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[11]	"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells." Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J. Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]	"Interaction of Pyk2 and PTP-PEST with leupaxin in prostate cancer cells." Sahu S.N., Nunez S., Bai G., Gupta A. Am. J. Physiol. 292:C2288-C2296(2007) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PTK2B/PYK2 AND PTPN12, SUBCELLULAR LOCATION.
[13]	"Leupaxin negatively regulates B cell receptor signaling." Chew V., Lam K.P. J. Biol. Chem. 282:27181-27191(2007) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT TYR-72 BY LYN, INTERACTION WITH LYN.
[14]	"The LIM protein leupaxin is enriched in smooth muscle and functions as an serum response factor cofactor to induce smooth muscle cell gene transcription." Sundberg-Smith L.J., DiMichele L.A., Sayers R.L., Mack C.P., Taylor J.M. Circ. Res. 102:1502-1511(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH PTK2/FAK AND SRF.
[15]	"Leupaxin, a novel coactivator of the androgen receptor, is expressed in prostate cancer and plays a role in adhesion and invasion of prostate carcinoma cells." Kaulfuss S., Grzmil M., Hemmerlein B., Thelen P., Schweyer S., Neesen J., Bubendorf L., Glass A.G., Jarry H., Auber B., Burfeind P. Mol. Endocrinol. 22:1606-1621(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH AR.
[16]	"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Leukemic T-cell.
[17]	"Leupaxin is similar to paxillin in focal adhesion targeting and tyrosine phosphorylation but has distinct roles in cell adhesion and spreading." Chen P.W., Kroog G.S. Cell Adh. Migr. 4:527-540(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT TYR-22; TYR-62 AND TYR-72.
[18]	"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].
[19]	"Solution structure of the LIM domain of human leupaxin." RIKEN structural genomics initiative (RSGI) Submitted (JAN-2006) to the PDB data bank Cited for: STRUCTURE BY NMR OF 260-326.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF062075 mRNA. Translation: AAC16014.1.
AK300955 mRNA. Translation: BAG62583.1.
AK313306 mRNA. Translation: BAG36111.1.
CR536531 mRNA. Translation: CAG38768.1.
AK223165 mRNA. Translation: BAD96885.1.
AP001350 Genomic DNA. No translation available.
AP003557 Genomic DNA. No translation available.
CH471076 Genomic DNA. Translation: EAW73808.1.
BC019035 mRNA. Translation: AAH19035.1.

IPI

IPI00299066.
IPI00871430.

RefSeq

NP_001137467.1. NM_001143995.1.
NP_004802.1. NM_004811.2.

UniGene

Hs.125474.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1X3H	NMR	-	A	260-326	[»]

ProteinModelPortal

O60711.

ModBase

Search...

Protein-protein interaction databases

IntAct

O60711. 18 interactions.

MINT

MINT-1449182.

STRING

9606.ENSP00000263845.

PTM databases

PhosphoSite

O60711.

Proteomic databases

PaxDb

O60711.

PeptideAtlas

O60711.

PRIDE

O60711.

Protocols and materials databases

DNASU

9404.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000395074; ENSP00000378512; ENSG00000110031.
ENST00000528954; ENSP00000431284; ENSG00000110031.

GeneID

9404.

KEGG

hsa:9404.

UCSC

uc001nmw.3. human.
uc010rkj.2. human.

Organism-specific databases

CTD

9404.

GeneCards

GC11M058294.

HGNC

HGNC:14061. LPXN.

HPA

CAB046478.
HPA043741.

MIM

605390. gene.

neXtProt

NX_O60711.

PharmGKB

PA30441.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG267887.

HOGENOM

HOG000018764.

HOVERGEN

HBG001512.

InParanoid

O60711.

OMA

GFHEKDK.

OrthoDB

EOG4TMR25.

PhylomeDB

O60711.

Enzyme and pathway databases

SignaLink

O60711.

Gene expression databases

ArrayExpress

O60711.

Bgee

O60711.

CleanEx

HS_LPXN.

Genevestigator

O60711.

GermOnline

ENSG00000110031. Homo sapiens.

Family and domain databases

Gene3D

2.10.110.10. 4 hits.

InterPro

IPR017305. Leupaxin.
IPR001781. Znf_LIM.
[Graphical view]

Pfam

PF00412. LIM. 4 hits.
[Graphical view]

PIRSF

PIRSF037881. Leupaxin. 1 hit.

SMART

SM00132. LIM. 4 hits.
[Graphical view]

PROSITE

PS00478. LIM_DOMAIN_1. 4 hits.
PS50023. LIM_DOMAIN_2. 4 hits.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

O60711.

GenomeRNAi

9404.

NextBio

35232.

SOURCE

Search...

Entry information

Entry name

LPXN_HUMAN

Accession

Primary (citable) accession number: O60711
Secondary accession number(s): B2R8B4 , B4DV71, Q53FW6, Q6FI07

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	August 1, 1998
Last modified:	May 29, 2013
This is version 121 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.