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Protein

Polyadenylate-binding protein 4

Gene

PABPC4

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

Functioni

Binds the poly(A) tail of mRNA. May be involved in cytoplasmic regulatory processes of mRNA metabolism. Can probably bind to cytoplasmic RNA sequences other than poly(A) in vivo (By similarity).By similarity

GO - Molecular functioni

  • nucleotide binding Source: InterPro
  • poly(A) binding Source: MGI
  • poly(A) RNA binding Source: UniProtKB
  • poly(U) RNA binding Source: MGI

GO - Biological processi

  • blood coagulation Source: ProtInc
  • RNA catabolic process Source: ProtInc
  • RNA processing Source: ProtInc
  • translation Source: ProtInc
Complete GO annotation...

Keywords - Ligandi

RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Polyadenylate-binding protein 4
Short name:
PABP-4
Short name:
Poly(A)-binding protein 4
Alternative name(s):
Activated-platelet protein 1
Short name:
APP-1
Inducible poly(A)-binding protein
Short name:
iPABP
Gene namesi
Name:PABPC4
Synonyms:APP1, PABP4
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:8557. PABPC4.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: HPA
  • cytoplasmic stress granule Source: MGI
  • nucleus Source: MGI
  • ribonucleoprotein complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA32883.

Polymorphism and mutation databases

BioMutaiPABPC4.
DMDMi12229875.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 644644Polyadenylate-binding protein 4PRO_0000081703Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei140 – 1401Phosphotyrosine1 Publication
Modified residuei299 – 2991N6-methyllysineBy similarity
Modified residuei315 – 3151Phosphoserine1 Publication
Modified residuei361 – 3611N6,N6-dimethyllysine1 Publication
Modified residuei509 – 5091Dimethylated arginine; alternateBy similarity
Modified residuei509 – 5091Omega-N-methylarginine; alternateBy similarity
Modified residuei518 – 5181Dimethylated arginine1 Publication
Modified residuei524 – 5241N6-acetyllysineBy similarity
Modified residuei531 – 5311Phosphoserine1 Publication

Post-translational modificationi

Arg-518 is dimethylated, probably to asymmetric dimethylarginine.

Keywords - PTMi

Acetylation, Methylation, Phosphoprotein

Proteomic databases

MaxQBiQ13310.
PaxDbiQ13310.
PRIDEiQ13310.

PTM databases

PhosphoSiteiQ13310.

Expressioni

Tissue specificityi

Expressed at low levels in resting normal T cells; following T-cell activation, however, mRNA levels are rapidly up-regulated.

Gene expression databases

BgeeiQ13310.
CleanExiHS_PABPC4.
ExpressionAtlasiQ13310. baseline.
GenevisibleiQ13310. HS.

Organism-specific databases

HPAiHPA027301.
HPA056496.

Interactioni

Subunit structurei

Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs. Interacts with NFX1.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
PHLDA1Q8WV242EBI-372844,EBI-738731

Protein-protein interaction databases

BioGridi114296. 66 interactions.
IntActiQ13310. 33 interactions.
MINTiMINT-1189867.
STRINGi9606.ENSP00000361949.

Structurei

3D structure databases

ProteinModelPortaliQ13310.
SMRiQ13310. Positions 10-376, 510-643.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini11 – 8979RRM 1PROSITE-ProRule annotationAdd
BLAST
Domaini99 – 17577RRM 2PROSITE-ProRule annotationAdd
BLAST
Domaini191 – 26878RRM 3PROSITE-ProRule annotationAdd
BLAST
Domaini294 – 37077RRM 4PROSITE-ProRule annotationAdd
BLAST
Domaini551 – 62878PABCPROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi510 – 5167Poly-Ala

Sequence similaritiesi

Contains 1 PABC domain.PROSITE-ProRule annotation
Contains 4 RRM (RNA recognition motif) domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG0724.
GeneTreeiENSGT00760000118913.
HOGENOMiHOG000217922.
HOVERGENiHBG002295.
InParanoidiQ13310.
KOiK13126.
OMAiTDSCKSG.
PhylomeDBiQ13310.
TreeFamiTF300458.

Family and domain databases

Gene3Di1.10.1900.10. 1 hit.
3.30.70.330. 4 hits.
InterProiIPR012677. Nucleotide-bd_a/b_plait.
IPR006515. PABP_1234.
IPR002004. PABP_HYD.
IPR000504. RRM_dom.
[Graphical view]
PfamiPF00658. PABP. 1 hit.
PF00076. RRM_1. 4 hits.
[Graphical view]
SMARTiSM00517. PolyA. 1 hit.
SM00360. RRM. 4 hits.
[Graphical view]
SUPFAMiSSF63570. SSF63570. 1 hit.
TIGRFAMsiTIGR01628. PABP-1234. 1 hit.
PROSITEiPS51309. PABC. 1 hit.
PS50102. RRM. 4 hits.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

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

Isoform 1 (identifier: Q13310-1) [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
MNAAASSYPM ASLYVGDLHS DVTEAMLYEK FSPAGPVLSI RVCRDMITRR
60 70 80 90 100
SLGYAYVNFQ QPADAERALD TMNFDVIKGK PIRIMWSQRD PSLRKSGVGN
110 120 130 140 150
VFIKNLDKSI DNKALYDTFS AFGNILSCKV VCDENGSKGY AFVHFETQEA
160 170 180 190 200
ADKAIEKMNG MLLNDRKVFV GRFKSRKERE AELGAKAKEF TNVYIKNFGE
210 220 230 240 250
EVDDESLKEL FSQFGKTLSV KVMRDPNGKS KGFGFVSYEK HEDANKAVEE
260 270 280 290 300
MNGKEISGKI IFVGRAQKKV ERQAELKRKF EQLKQERISR YQGVNLYIKN
310 320 330 340 350
LDDTIDDEKL RKEFSPFGSI TSAKVMLEDG RSKGFGFVCF SSPEEATKAV
360 370 380 390 400
TEMNGRIVGS KPLYVALAQR KEERKAHLTN QYMQRVAGMR ALPANAILNQ
410 420 430 440 450
FQPAAGGYFV PAVPQAQGRP PYYTPNQLAQ MRPNPRWQQG GRPQGFQGMP
460 470 480 490 500
SAIRQSGPRP TLRHLAPTGS ECPDRLAMDF GGAGAAQQGL TDSCQSGGVP
510 520 530 540 550
TAVQNLAPRA AVAAAAPRAV APYKYASSVR SPHPAIQPLQ APQPAVHVQG
560 570 580 590 600
QEPLTASMLA AAPPQEQKQM LGERLFPLIQ TMHSNLAGKI TGMLLEIDNS
610 620 630 640
ELLHMLESPE SLRSKVDEAV AVLQAHHAKK EAAQKVGAVA AATS
Length:644
Mass (Da):70,783
Last modified:November 1, 1996 - v1
Checksum:iA761488F0B10DF5A
GO
Isoform 2 (identifier: Q13310-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     470-497: SECPDRLAMDFGGAGAAQQGLTDSCQSG → NAPASRGLPTTTQRV

Note: No experimental confirmation available.
Show »
Length:631
Mass (Da):69,579
Checksum:i1891E205916695F6
GO
Isoform 3 (identifier: Q13310-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     468-468: T → TGNAPASRGLPTTTQRV

Note: No experimental confirmation available.
Show »
Length:660
Mass (Da):72,391
Checksum:iBC4FB29689689633
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti114 – 1141A → V in AAH65540 (PubMed:15489334).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti382 – 3821Y → F.
Corresponds to variant rs9820 [ dbSNP | Ensembl ].
VAR_054048

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei468 – 4681T → TGNAPASRGLPTTTQRV in isoform 3. 1 PublicationVSP_043357
Alternative sequencei470 – 49728SECPD…SCQSG → NAPASRGLPTTTQRV in isoform 2. 1 PublicationVSP_013335Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U33818 mRNA. Translation: AAC50350.1.
U75686 mRNA. Translation: AAB97309.1.
AL365277, AL845289 Genomic DNA. Translation: CAI16412.1.
AL365277, AL845289 Genomic DNA. Translation: CAI16414.1.
AL845289, AL365277 Genomic DNA. Translation: CAI12298.1.
AL845289, AL365277 Genomic DNA. Translation: CAI12300.1.
CH471059 Genomic DNA. Translation: EAX07263.1.
CH471059 Genomic DNA. Translation: EAX07264.1.
BC065540 mRNA. Translation: AAH65540.1.
BC094755 mRNA. Translation: AAH94755.1.
CCDSiCCDS438.1. [Q13310-1]
CCDS44114.1. [Q13310-2]
CCDS44115.1. [Q13310-3]
RefSeqiNP_001129125.1. NM_001135653.1. [Q13310-3]
NP_001129126.1. NM_001135654.1. [Q13310-2]
NP_003810.1. NM_003819.3. [Q13310-1]
UniGeneiHs.169900.

Genome annotation databases

EnsembliENST00000372856; ENSP00000361947; ENSG00000090621. [Q13310-2]
ENST00000372857; ENSP00000361948; ENSG00000090621.
ENST00000372858; ENSP00000361949; ENSG00000090621. [Q13310-3]
GeneIDi8761.
KEGGihsa:8761.
UCSCiuc001cdl.2. human. [Q13310-3]
uc001cdm.2. human. [Q13310-2]
uc010oiv.1. human. [Q13310-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U33818 mRNA. Translation: AAC50350.1.
U75686 mRNA. Translation: AAB97309.1.
AL365277, AL845289 Genomic DNA. Translation: CAI16412.1.
AL365277, AL845289 Genomic DNA. Translation: CAI16414.1.
AL845289, AL365277 Genomic DNA. Translation: CAI12298.1.
AL845289, AL365277 Genomic DNA. Translation: CAI12300.1.
CH471059 Genomic DNA. Translation: EAX07263.1.
CH471059 Genomic DNA. Translation: EAX07264.1.
BC065540 mRNA. Translation: AAH65540.1.
BC094755 mRNA. Translation: AAH94755.1.
CCDSiCCDS438.1. [Q13310-1]
CCDS44114.1. [Q13310-2]
CCDS44115.1. [Q13310-3]
RefSeqiNP_001129125.1. NM_001135653.1. [Q13310-3]
NP_001129126.1. NM_001135654.1. [Q13310-2]
NP_003810.1. NM_003819.3. [Q13310-1]
UniGeneiHs.169900.

3D structure databases

ProteinModelPortaliQ13310.
SMRiQ13310. Positions 10-376, 510-643.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114296. 66 interactions.
IntActiQ13310. 33 interactions.
MINTiMINT-1189867.
STRINGi9606.ENSP00000361949.

Chemistry

ChEMBLiCHEMBL5333.

PTM databases

PhosphoSiteiQ13310.

Polymorphism and mutation databases

BioMutaiPABPC4.
DMDMi12229875.

Proteomic databases

MaxQBiQ13310.
PaxDbiQ13310.
PRIDEiQ13310.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000372856; ENSP00000361947; ENSG00000090621. [Q13310-2]
ENST00000372857; ENSP00000361948; ENSG00000090621.
ENST00000372858; ENSP00000361949; ENSG00000090621. [Q13310-3]
GeneIDi8761.
KEGGihsa:8761.
UCSCiuc001cdl.2. human. [Q13310-3]
uc001cdm.2. human. [Q13310-2]
uc010oiv.1. human. [Q13310-1]

Organism-specific databases

CTDi8761.
GeneCardsiGC01M040026.
HGNCiHGNC:8557. PABPC4.
HPAiHPA027301.
HPA056496.
MIMi603407. gene.
neXtProtiNX_Q13310.
PharmGKBiPA32883.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0724.
GeneTreeiENSGT00760000118913.
HOGENOMiHOG000217922.
HOVERGENiHBG002295.
InParanoidiQ13310.
KOiK13126.
OMAiTDSCKSG.
PhylomeDBiQ13310.
TreeFamiTF300458.

Miscellaneous databases

ChiTaRSiPABPC4. human.
GeneWikiiPABPC4.
GenomeRNAii8761.
NextBioi32864.
PROiQ13310.
SOURCEiSearch...

Gene expression databases

BgeeiQ13310.
CleanExiHS_PABPC4.
ExpressionAtlasiQ13310. baseline.
GenevisibleiQ13310. HS.

Family and domain databases

Gene3Di1.10.1900.10. 1 hit.
3.30.70.330. 4 hits.
InterProiIPR012677. Nucleotide-bd_a/b_plait.
IPR006515. PABP_1234.
IPR002004. PABP_HYD.
IPR000504. RRM_dom.
[Graphical view]
PfamiPF00658. PABP. 1 hit.
PF00076. RRM_1. 4 hits.
[Graphical view]
SMARTiSM00517. PolyA. 1 hit.
SM00360. RRM. 4 hits.
[Graphical view]
SUPFAMiSSF63570. SSF63570. 1 hit.
TIGRFAMsiTIGR01628. PABP-1234. 1 hit.
PROSITEiPS51309. PABC. 1 hit.
PS50102. RRM. 4 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "iPABP, an inducible poly(A)-binding protein detected in activated human T cells."
    Yang H., Duckett C.S., Lindsten T.
    Mol. Cell. Biol. 15:6770-6776(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "Identification and structure of activated-platelet protein-1, a protein with RNA-binding domain motifs that is expressed by activated platelets."
    Houng A.K., Maggini L., Clement C.Y., Reed G.L.
    Eur. J. Biochem. 243:209-218(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  3. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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 2 AND 3).
    Tissue: Placenta and Skin.
  6. Bienvenut W.V., Waridel P., Quadroni M.
    Submitted (MAR-2009) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 31-41; 51-78; 84-89; 96-104; 114-129; 139-153; 158-166; 187-216; 232-240; 291-311; 313-324; 334-348; 357-370; 376-385; 510-524 AND 575-629, METHYLATION AT LYS-361 AND ARG-518, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Cervix carcinoma.
  7. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-140, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "NFX1-123 and poly(A) binding proteins synergistically augment activation of telomerase in human papillomavirus type 16 E6-expressing cells."
    Katzenellenbogen R.A., Egelkrout E.M., Vliet-Gregg P., Gewin L.C., Gafken P.R., Galloway D.A.
    J. Virol. 81:3786-3796(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NFX1.
  9. Cited for: IDENTIFICATION IN A MRNP GRANULE COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION.
  10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-531, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-315, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiPABP4_HUMAN
AccessioniPrimary (citable) accession number: Q13310
Secondary accession number(s): B1ANQ8, Q4VC03, Q6P0N3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: November 1, 1996
Last modified: July 22, 2015
This is version 158 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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: 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. 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.