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Protein

Lymphocyte-specific protein 1

Gene

LSP1

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

Functioni

May play a role in mediating neutrophil activation and chemotaxis.By similarity

GO - Molecular functioni

  • actin binding Source: ProtInc
  • signal transducer activity Source: InterPro

GO - Biological processi

  • cellular defense response Source: ProtInc
  • chemotaxis Source: Ensembl
  • movement of cell or subcellular component Source: ProtInc
Complete GO annotation...

Enzyme and pathway databases

SignaLinkiP33241.

Names & Taxonomyi

Protein namesi
Recommended name:
Lymphocyte-specific protein 1
Alternative name(s):
47 kDa actin-binding protein
52 kDa phosphoprotein
Short name:
pp52
Lymphocyte-specific antigen WP34
Gene namesi
Name:LSP1
Synonyms:WP34
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:6707. LSP1.

Subcellular locationi

GO - Cellular componenti

  • actin cytoskeleton Source: ProtInc
  • extracellular exosome Source: UniProtKB
  • membrane Source: UniProtKB
  • plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA30472.

Polymorphism and mutation databases

BioMutaiLSP1.
DMDMi462553.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 339339Lymphocyte-specific protein 1PRO_0000084503Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei24 – 241Phosphoserine1 Publication
Modified residuei111 – 1111Phosphoserine1 Publication
Modified residuei175 – 1751PhosphothreonineBy similarity
Modified residuei177 – 1771PhosphoserineBy similarity
Modified residuei188 – 1881Phosphoserine1 Publication
Modified residuei189 – 1891Phosphoserine2 Publications
Modified residuei193 – 1931Phosphoserine1 Publication
Modified residuei252 – 2521Phosphoserine; by MAPKAPK23 Publications
Modified residuei327 – 3271N6-acetyllysine1 Publication

Post-translational modificationi

Phosphorylated by casein kinase II, protein kinase C and MAPKAPK2. Phosphorylation by PKC induces translocation from membrane to cytoplasm. Phosphorylation by MAPKAPK2 may regulate neutrophil chemotaxis (By similarity).By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP33241.
PaxDbiP33241.
PeptideAtlasiP33241.
PRIDEiP33241.

2D gel databases

SWISS-2DPAGEP33241.

PTM databases

PhosphoSiteiP33241.

Expressioni

Tissue specificityi

Activated T-lymphocytes.

Gene expression databases

BgeeiP33241.
CleanExiHS_LSP1.
ExpressionAtlasiP33241. baseline and differential.
GenevisibleiP33241. HS.

Organism-specific databases

HPAiCAB017781.
HPA019693.

Interactioni

Subunit structurei

Binds actin.

Protein-protein interaction databases

BioGridi110224. 9 interactions.
IntActiP33241. 7 interactions.

Structurei

Secondary structure

1
339
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi255 – 2584Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3BH8X-ray1.65C249-258[»]
4NO0X-ray2.70C249-260[»]
4NO2X-ray2.00C249-260[»]
ProteinModelPortaliP33241.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP33241.

Family & Domainsi

Phylogenomic databases

eggNOGiNOG302084.
GeneTreeiENSGT00730000111324.
HOGENOMiHOG000231050.
HOVERGENiHBG001610.
InParanoidiP33241.
KOiK14957.
OMAiRLTAQWS.
OrthoDBiEOG7FNC7W.
PhylomeDBiP33241.
TreeFamiTF336257.

Family and domain databases

InterProiIPR006018. Caldesmon_LSP.
IPR002211. Lymphspecific.
[Graphical view]
PANTHERiPTHR18949. PTHR18949. 1 hit.
PfamiPF02029. Caldesmon. 1 hit.
[Graphical view]
PRINTSiPR01083. LYMPHSPCIFIC.

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P33241-1) [UniParc]FASTAAdd to basket

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

        10         20         30         40         50
MAEASSDPGA EEREELLGPT AQWSVEDEEE AVHEQCQHER DRQLQAQDEE
60 70 80 90 100
GGGHVPERPK QEMLLSLKPS EAPELDEDEG FGDWSQRPEQ RQQHEGAQGA
110 120 130 140 150
LDSGEPPQCR SPEGEQEDRP GLHAYEKEDS DEVHLEELSL SKEGPGPEDT
160 170 180 190 200
VQDNLGAAGA EEEQEEHQKC QQPRTPSPLV LEGTIEQSSP PLSPTTKLID
210 220 230 240 250
RTESLNRSIE KSNSVKKSQP DLPISKIDQW LEQYTQAIET AGRTPKLARQ
260 270 280 290 300
ASIELPSMAV ASTKSRWETG EVQAQSAAKT PSCKDIVAGD MSKKSLWEQK
310 320 330
GGSKTSSTIK STPSGKRYKF VATGHGKYEK VLVEGGPAP
Length:339
Mass (Da):37,192
Last modified:February 1, 1994 - v1
Checksum:iF2A18533500611D9
GO
Isoform 2 (identifier: P33241-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-62: Missing.

Note: No experimental confirmation available.
Show »
Length:277
Mass (Da):30,213
Checksum:iDA869746FA7B7C6D
GO
Isoform 3 (identifier: P33241-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-18: MAEASSDPGAEEREELLG → MAPIWSPPGR...SGPSTNCSPR

Note: No experimental confirmation available.Curated
Show »
Length:467
Mass (Da):50,389
Checksum:iA3F09D8EECD570D6
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti15 – 151Missing in AAB29545 (PubMed:8274738).Curated
Sequence conflicti24 – 241S → T in CAA38971 (PubMed:2174784).Curated
Sequence conflicti100 – 1012Missing in AAB29545 (PubMed:8274738).Curated
Sequence conflicti148 – 1481E → D in BAG52478 (PubMed:14702039).Curated
Isoform 3 (identifier: P33241-3)
Sequence conflicti31 – 311G → Q in BAG52478 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti100 – 1001A → T.3 Publications
Corresponds to variant rs621679 [ dbSNP | Ensembl ].
VAR_011867
Natural varianti108 – 1081Q → L.
Corresponds to variant rs11545725 [ dbSNP | Ensembl ].
VAR_061680
Natural varianti229 – 2291Q → K.
Corresponds to variant rs1803928 [ dbSNP | Ensembl ].
VAR_011868

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 6262Missing in isoform 2. 1 PublicationVSP_045655Add
BLAST
Alternative sequencei1 – 1818MAEAS…EELLG → MAPIWSPPGRVSGCHLSSGP APGSAVGPWLGTPHPSLPLP LAPHKPPPPGLPGSAGQTSL PAQRECVFPGDAAVHQELCG LGFEECLGSIPQAHQCYLTN GPKRRKCSPRRRGRAPAWLC GGSPPCHQGLGHEHPSSGPS TNCSPR in isoform 3. 1 PublicationVSP_045983Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M33552 mRNA. Translation: AAA59534.1.
X55188 mRNA. Translation: CAA38971.1.
S67783 mRNA. Translation: AAB29545.1.
CR541728 mRNA. Translation: CAG46529.1.
CR541754 mRNA. Translation: CAG46554.1.
AK056576 mRNA. Translation: BAG51753.1.
AK092071 mRNA. Translation: BAG52478.1.
AK222733 mRNA. Translation: BAD96453.1.
AC051649 Genomic DNA. No translation available.
BC001785 mRNA. Translation: AAH01785.1.
CCDSiCCDS31334.1. [P33241-1]
CCDS31335.1. [P33241-2]
CCDS58110.1. [P33241-3]
PIRiA43542.
RefSeqiNP_001013271.1. NM_001013253.1. [P33241-2]
NP_001013272.1. NM_001013254.1. [P33241-2]
NP_001013273.1. NM_001013255.1. [P33241-2]
NP_001229861.1. NM_001242932.1. [P33241-3]
NP_001275934.1. NM_001289005.1. [P33241-2]
NP_002330.1. NM_002339.2. [P33241-1]
UniGeneiHs.56729.

Genome annotation databases

EnsembliENST00000311604; ENSP00000308383; ENSG00000130592. [P33241-1]
ENST00000381775; ENSP00000371194; ENSG00000130592. [P33241-3]
ENST00000405957; ENSP00000383932; ENSG00000130592. [P33241-2]
ENST00000406638; ENSP00000384022; ENSG00000130592. [P33241-2]
ENST00000612798; ENSP00000484140; ENSG00000130592. [P33241-2]
GeneIDi4046.
KEGGihsa:4046.
UCSCiuc001lui.3. human. [P33241-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M33552 mRNA. Translation: AAA59534.1.
X55188 mRNA. Translation: CAA38971.1.
S67783 mRNA. Translation: AAB29545.1.
CR541728 mRNA. Translation: CAG46529.1.
CR541754 mRNA. Translation: CAG46554.1.
AK056576 mRNA. Translation: BAG51753.1.
AK092071 mRNA. Translation: BAG52478.1.
AK222733 mRNA. Translation: BAD96453.1.
AC051649 Genomic DNA. No translation available.
BC001785 mRNA. Translation: AAH01785.1.
CCDSiCCDS31334.1. [P33241-1]
CCDS31335.1. [P33241-2]
CCDS58110.1. [P33241-3]
PIRiA43542.
RefSeqiNP_001013271.1. NM_001013253.1. [P33241-2]
NP_001013272.1. NM_001013254.1. [P33241-2]
NP_001013273.1. NM_001013255.1. [P33241-2]
NP_001229861.1. NM_001242932.1. [P33241-3]
NP_001275934.1. NM_001289005.1. [P33241-2]
NP_002330.1. NM_002339.2. [P33241-1]
UniGeneiHs.56729.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3BH8X-ray1.65C249-258[»]
4NO0X-ray2.70C249-260[»]
4NO2X-ray2.00C249-260[»]
ProteinModelPortaliP33241.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110224. 9 interactions.
IntActiP33241. 7 interactions.

PTM databases

PhosphoSiteiP33241.

Polymorphism and mutation databases

BioMutaiLSP1.
DMDMi462553.

2D gel databases

SWISS-2DPAGEP33241.

Proteomic databases

MaxQBiP33241.
PaxDbiP33241.
PeptideAtlasiP33241.
PRIDEiP33241.

Protocols and materials databases

DNASUi4046.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000311604; ENSP00000308383; ENSG00000130592. [P33241-1]
ENST00000381775; ENSP00000371194; ENSG00000130592. [P33241-3]
ENST00000405957; ENSP00000383932; ENSG00000130592. [P33241-2]
ENST00000406638; ENSP00000384022; ENSG00000130592. [P33241-2]
ENST00000612798; ENSP00000484140; ENSG00000130592. [P33241-2]
GeneIDi4046.
KEGGihsa:4046.
UCSCiuc001lui.3. human. [P33241-1]

Organism-specific databases

CTDi4046.
GeneCardsiGC11P001874.
HGNCiHGNC:6707. LSP1.
HPAiCAB017781.
HPA019693.
MIMi153432. gene.
neXtProtiNX_P33241.
PharmGKBiPA30472.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG302084.
GeneTreeiENSGT00730000111324.
HOGENOMiHOG000231050.
HOVERGENiHBG001610.
InParanoidiP33241.
KOiK14957.
OMAiRLTAQWS.
OrthoDBiEOG7FNC7W.
PhylomeDBiP33241.
TreeFamiTF336257.

Enzyme and pathway databases

SignaLinkiP33241.

Miscellaneous databases

ChiTaRSiLSP1. human.
EvolutionaryTraceiP33241.
GeneWikiiLSP1.
GenomeRNAii4046.
NextBioi15838.
PROiP33241.
SOURCEiSearch...

Gene expression databases

BgeeiP33241.
CleanExiHS_LSP1.
ExpressionAtlasiP33241. baseline and differential.
GenevisibleiP33241. HS.

Family and domain databases

InterProiIPR006018. Caldesmon_LSP.
IPR002211. Lymphspecific.
[Graphical view]
PANTHERiPTHR18949. PTHR18949. 1 hit.
PfamiPF02029. Caldesmon. 1 hit.
[Graphical view]
PRINTSiPR01083. LYMPHSPCIFIC.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Human and mouse LSP1 genes code for highly conserved phosphoproteins."
    Jongstra-Bilen J., Young A.J., Chong R., Jongstra J.
    J. Immunol. 144:1104-1110(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "Molecular cloning and characterization of WP34, a phosphorylated human lymphocyte differentiation and activation antigen."
    Kadiyala R.K., McIntyre B.W., Krensky A.M.
    Eur. J. Immunol. 20:2417-2423(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Lymphocyte.
  3. "The 47-kD protein increased in neutrophil actin dysfunction with 47- and 89-kD protein abnormalities is lymphocyte-specific protein."
    Howard T., Li Y., Torres M., Guerrero A., Coates T.
    Blood 83:231-241(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE.
  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] (ISOFORM 1).
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3), VARIANT THR-100.
    Tissue: Esophagus and Tongue.
  6. 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), VARIANT THR-100.
    Tissue: Dermoid cancer.
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "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), VARIANT THR-100.
    Tissue: Lymph.
  9. "MAPKAPK2-mediated LSP1 phosphorylation and FMLP-induced neutrophil polarization."
    Wu Y., Zhan L., Ai Y., Hannigan M., Gaestel M., Huang C.-K., Madri J.A.
    Biochem. Biophys. Res. Commun. 358:170-175(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-252 BY MAPKAPK2.
  10. "Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment."
    Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.
    J. Proteome Res. 7:5167-5176(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-252, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: T-cell.
  11. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-189, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  12. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-327, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24; SER-111; SER-188; SER-189; SER-193 AND SER-252, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiLSP1_HUMAN
AccessioniPrimary (citable) accession number: P33241
Secondary accession number(s): B3KPP1
, B3KRR6, E9PBV6, E9PFP3, Q16096, Q53H48, Q6FHM3, Q9BUY8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: June 24, 2015
This is version 141 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 11
    Human chromosome 11: 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

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.