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Protein

Phospholipid scramblase 4

Gene

PLSCR4

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

Functioni

May mediate accelerated ATP-independent bidirectional transbilayer migration of phospholipids upon binding calcium ions that results in a loss of phospholipid asymmetry in the plasma membrane. May play a central role in the initiation of fibrin clot formation, in the activation of mast cells and in the recognition of apoptotic and injured cells by the reticuloendothelial system.

Cofactori

Ca2+1 Publication, Mg2+1 Publication

GO - Molecular functioni

  • calcium ion binding Source: UniProtKB
  • CD4 receptor binding Source: UniProtKB
  • enzyme binding Source: UniProtKB
  • phospholipid scramblase activity Source: UniProtKB

GO - Biological processi

  • cellular response to lipopolysaccharide Source: Ensembl
  • phospholipid scrambling Source: UniProtKB
Complete GO annotation...

Keywords - Ligandi

Calcium

Enzyme and pathway databases

BRENDAi3.6.99.B1. 2681.

Names & Taxonomyi

Protein namesi
Recommended name:
Phospholipid scramblase 4
Short name:
PL scramblase 4
Alternative name(s):
Ca(2+)-dependent phospholipid scramblase 4
Cell growth-inhibiting gene 43 protein
TRA1
Gene namesi
Name:PLSCR4
ORF Names:GIG43
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 3

Organism-specific databases

HGNCiHGNC:16497. PLSCR4.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 303303CytoplasmicBy similarityAdd
BLAST
Transmembranei304 – 32017HelicalSequence AnalysisAdd
BLAST
Topological domaini321 – 3299ExtracellularBy similarity

GO - Cellular componenti

  • extracellular exosome Source: UniProtKB
  • integral component of membrane Source: UniProtKB-KW
  • plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi290 – 2901D → A: 50% decrease in scramblase activity in presence of Ca2+, and 40% decrease in scramblase activity in presence of Mg2+. 1 Publication

Organism-specific databases

PharmGKBiPA33422.

Polymorphism and mutation databases

BioMutaiPLSCR4.
DMDMi212276457.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 329329Phospholipid scramblase 4PRO_0000100792Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei83 – 831Phosphotyrosine; by ABLBy similarity
Modified residuei88 – 881Phosphotyrosine; by ABLBy similarity
Lipidationi250 – 2501S-palmitoyl cysteineCurated
Lipidationi255 – 2551S-palmitoyl cysteineCurated

Keywords - PTMi

Lipoprotein, Palmitate, Phosphoprotein

Proteomic databases

MaxQBiQ9NRQ2.
PaxDbiQ9NRQ2.
PRIDEiQ9NRQ2.

PTM databases

PhosphoSiteiQ9NRQ2.

Expressioni

Tissue specificityi

Expressed in heart, brain, placenta, lung, liver, kidney, pancreas, spleen, thymus, prostate, testis, uterus, small intestine and colon. Not detected in peripheral blood lymphocytes.

Gene expression databases

BgeeiQ9NRQ2.
CleanExiHS_PLSCR4.
ExpressionAtlasiQ9NRQ2. baseline and differential.
GenevisibleiQ9NRQ2. HS.

Organism-specific databases

HPAiHPA002276.

Interactioni

Subunit structurei

Interacts with PDCD6.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
Hoxa1P090224EBI-769257,EBI-3957603From a different organism.
MTUS2Q5JR594EBI-769257,EBI-742948
NOTCH2NLQ7Z3S93EBI-769257,EBI-945833

Protein-protein interaction databases

BioGridi121357. 13 interactions.
IntActiQ9NRQ2. 17 interactions.
MINTiMINT-1443866.
STRINGi9606.ENSP00000347038.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3Q5UX-ray2.50B271-283[»]
ProteinModelPortaliQ9NRQ2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 9898Proline-rich domain (PRD)By similarityAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi18 – 258SH3-binding 1Sequence Analysis
Motifi30 – 334WW-bindingSequence Analysis
Motifi41 – 499SH3-binding 2Sequence Analysis
Motifi98 – 1069SH3-binding 3Sequence Analysis

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi195 – 2028Cys-rich

Domaini

The N-terminal proline-rich domain (PRD) is required for phospholipid scramblase activity.By similarity

Sequence similaritiesi

Belongs to the phospholipid scramblase family.Curated

Keywords - Domaini

Repeat, SH3-binding, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG317744.
GeneTreeiENSGT00390000002884.
HOGENOMiHOG000237356.
HOVERGENiHBG019157.
InParanoidiQ9NRQ2.
OMAiNRYDIKN.
OrthoDBiEOG77T14X.
PhylomeDBiQ9NRQ2.
TreeFamiTF314939.

Family and domain databases

InterProiIPR005552. Scramblase.
[Graphical view]
PANTHERiPTHR23248. PTHR23248. 1 hit.
PfamiPF03803. Scramblase. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9NRQ2-1) [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
MSGVVPTAPE QPAGEMENQT KPPDPRPDAP PEYNSHFLPG PPGTAVPPPT
60 70 80 90 100
GYPGGLPMGY YSPQQPSTFP LYQPVGGIHP VRYQPGKYPM PNQSVPITWM
110 120 130 140 150
PGPTPMANCP PGLEYLVQLD NIHVLQHFEP LEMMTCFETN NRYDIKNNSD
160 170 180 190 200
QMVYIVTEDT DDFTRNAYRT LRPFVLRVTD CMGREIMTMQ RPFRCTCCCF
210 220 230 240 250
CCPSARQELE VQCPPGVTIG FVAEHWNLCR AVYSIQNEKK ENVMRVRGPC
260 270 280 290 300
STYGCGSDSV FEVKSLDGIS NIGSIIRKWN GLLSAMADAD HFDIHFPLDL
310 320
DVKMKAMIFG ACFLIDFMYF ERSPPQRSR
Length:329
Mass (Da):37,005
Last modified:November 4, 2008 - v2
Checksum:i12BE86728D54F794
GO
Isoform 2 (identifier: Q9NRQ2-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-15: Missing.
     119-208: Missing.

Note: No experimental confirmation available.
Show »
Length:224
Mass (Da):24,797
Checksum:i55E36F0305DAB876
GO

Sequence cautioni

The sequence AAP97186.1 differs from that shown. Reason: Frameshift at positions 152, 155, 163 and 325. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti56 – 572LP → FL in AAP97186 (Ref. 8) Curated
Sequence conflicti74 – 741P → S in AAT52217 (Ref. 2) Curated
Sequence conflicti149 – 1491S → L in AAP97186 (Ref. 8) Curated
Sequence conflicti163 – 1631F → V in AAP97186 (Ref. 8) Curated
Sequence conflicti175 – 1751V → G in AAP97186 (Ref. 8) Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti34 – 341N → S.2 Publications
Corresponds to variant rs3762685 [ dbSNP | Ensembl ].
VAR_011315
Natural varianti155 – 1551I → V.2 Publications
Corresponds to variant rs1061409 [ dbSNP | Ensembl ].
VAR_011316

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 1515Missing in isoform 2. 1 PublicationVSP_042931Add
BLAST
Alternative sequencei119 – 20890Missing in isoform 2. 1 PublicationVSP_042932Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF199023 mRNA. Translation: AAF89960.1.
AY550971 mRNA. Translation: AAT52217.1.
AK128442 mRNA. Translation: BAC87442.1.
AK290214 mRNA. Translation: BAF82903.1.
AL833760 mRNA. Translation: CAH56232.1.
AC092982 Genomic DNA. No translation available.
CH471052 Genomic DNA. Translation: EAW78935.1.
BC028354 mRNA. Translation: AAH28354.1.
AF087887 mRNA. Translation: AAP97186.1. Sequence problems.
CCDSiCCDS3133.1. [Q9NRQ2-1]
CCDS54651.1. [Q9NRQ2-2]
RefSeqiNP_001121776.1. NM_001128304.1. [Q9NRQ2-1]
NP_001121777.1. NM_001128305.1. [Q9NRQ2-1]
NP_001121778.1. NM_001128306.1.
NP_001170775.1. NM_001177304.1. [Q9NRQ2-2]
NP_065086.2. NM_020353.2. [Q9NRQ2-1]
XP_005247711.1. XM_005247654.1. [Q9NRQ2-1]
XP_005247712.1. XM_005247655.1. [Q9NRQ2-1]
UniGeneiHs.477869.

Genome annotation databases

EnsembliENST00000354952; ENSP00000347038; ENSG00000114698. [Q9NRQ2-1]
ENST00000433593; ENSP00000415605; ENSG00000114698. [Q9NRQ2-2]
ENST00000446574; ENSP00000399315; ENSG00000114698. [Q9NRQ2-1]
ENST00000493382; ENSP00000419040; ENSG00000114698. [Q9NRQ2-1]
GeneIDi57088.
KEGGihsa:57088.
UCSCiuc003evt.4. human. [Q9NRQ2-1]
uc003evu.4. human. [Q9NRQ2-2]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF199023 mRNA. Translation: AAF89960.1.
AY550971 mRNA. Translation: AAT52217.1.
AK128442 mRNA. Translation: BAC87442.1.
AK290214 mRNA. Translation: BAF82903.1.
AL833760 mRNA. Translation: CAH56232.1.
AC092982 Genomic DNA. No translation available.
CH471052 Genomic DNA. Translation: EAW78935.1.
BC028354 mRNA. Translation: AAH28354.1.
AF087887 mRNA. Translation: AAP97186.1. Sequence problems.
CCDSiCCDS3133.1. [Q9NRQ2-1]
CCDS54651.1. [Q9NRQ2-2]
RefSeqiNP_001121776.1. NM_001128304.1. [Q9NRQ2-1]
NP_001121777.1. NM_001128305.1. [Q9NRQ2-1]
NP_001121778.1. NM_001128306.1.
NP_001170775.1. NM_001177304.1. [Q9NRQ2-2]
NP_065086.2. NM_020353.2. [Q9NRQ2-1]
XP_005247711.1. XM_005247654.1. [Q9NRQ2-1]
XP_005247712.1. XM_005247655.1. [Q9NRQ2-1]
UniGeneiHs.477869.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3Q5UX-ray2.50B271-283[»]
ProteinModelPortaliQ9NRQ2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi121357. 13 interactions.
IntActiQ9NRQ2. 17 interactions.
MINTiMINT-1443866.
STRINGi9606.ENSP00000347038.

PTM databases

PhosphoSiteiQ9NRQ2.

Polymorphism and mutation databases

BioMutaiPLSCR4.
DMDMi212276457.

Proteomic databases

MaxQBiQ9NRQ2.
PaxDbiQ9NRQ2.
PRIDEiQ9NRQ2.

Protocols and materials databases

DNASUi57088.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000354952; ENSP00000347038; ENSG00000114698. [Q9NRQ2-1]
ENST00000433593; ENSP00000415605; ENSG00000114698. [Q9NRQ2-2]
ENST00000446574; ENSP00000399315; ENSG00000114698. [Q9NRQ2-1]
ENST00000493382; ENSP00000419040; ENSG00000114698. [Q9NRQ2-1]
GeneIDi57088.
KEGGihsa:57088.
UCSCiuc003evt.4. human. [Q9NRQ2-1]
uc003evu.4. human. [Q9NRQ2-2]

Organism-specific databases

CTDi57088.
GeneCardsiGC03M145910.
HGNCiHGNC:16497. PLSCR4.
HPAiHPA002276.
MIMi607612. gene.
neXtProtiNX_Q9NRQ2.
PharmGKBiPA33422.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG317744.
GeneTreeiENSGT00390000002884.
HOGENOMiHOG000237356.
HOVERGENiHBG019157.
InParanoidiQ9NRQ2.
OMAiNRYDIKN.
OrthoDBiEOG77T14X.
PhylomeDBiQ9NRQ2.
TreeFamiTF314939.

Enzyme and pathway databases

BRENDAi3.6.99.B1. 2681.

Miscellaneous databases

GeneWikiiPLSCR4.
GenomeRNAii57088.
NextBioi62887.
PROiQ9NRQ2.
SOURCEiSearch...

Gene expression databases

BgeeiQ9NRQ2.
CleanExiHS_PLSCR4.
ExpressionAtlasiQ9NRQ2. baseline and differential.
GenevisibleiQ9NRQ2. HS.

Family and domain databases

InterProiIPR005552. Scramblase.
[Graphical view]
PANTHERiPTHR23248. PTHR23248. 1 hit.
PfamiPF03803. Scramblase. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of three new members of the phospholipid scramblase gene family."
    Wiedmer T., Zhou Q., Kwoh D.Y., Sims P.J.
    Biochim. Biophys. Acta 1467:244-253(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS SER-34 AND VAL-155.
    Tissue: Pancreas.
  2. "Identification of a human cell growth inhibiting gene."
    Kim J.W.
    Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANTS SER-34 AND VAL-155.
  3. "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: Thalamus and Thymus.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Stomach.
  5. "The DNA sequence, annotation and analysis of human chromosome 3."
    Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
    , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
    Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. 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: Testis.
  8. "Cloning and characterization of a novel human cDNA homology to murine TRA1 mRNA."
    Cui W.C., Yu L., Gao J., Fan Y.X., Xu Y.F., Zhao S.Y.
    Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 46-329 (ISOFORM 1).
  9. "Identification of Alix-type and non-Alix-type ALG-2-binding sites in human phospholipid scramblase 3: differential binding to an alternatively spliced isoform and amino acid-substituted mutants."
    Shibata H., Suzuki H., Kakiuchi T., Inuzuka T., Yoshida H., Mizuno T., Maki M.
    J. Biol. Chem. 283:9623-9632(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PDCD6.
  10. "Biochemical and functional characterization of human phospholipid scramblase 4 (hPLSCR4)."
    Francis V.G., Gummadi S.N.
    Biol. Chem. 393:1173-1181(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: COFACTOR, MUTAGENESIS OF ASP-290.

Entry informationi

Entry nameiPLS4_HUMAN
AccessioniPrimary (citable) accession number: Q9NRQ2
Secondary accession number(s): A8K2E9
, Q2TTR3, Q658L3, Q6ZR73, Q7Z505
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 20, 2001
Last sequence update: November 4, 2008
Last modified: June 24, 2015
This is version 132 of the entry and version 2 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, Reference proteome

Documents

  1. Human chromosome 3
    Human chromosome 3: 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

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.