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Protein

CD2 antigen cytoplasmic tail-binding protein 2

Gene

CD2BP2

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

Functioni

Involved in pre-mRNA splicing as component of the U5 snRNP complex that is involved in spliceosome assembly.1 Publication

GO - Molecular functioni

  • ribonucleoprotein complex binding Source: BHF-UCL

GO - Biological processi

  • gene expression Source: Reactome
  • mRNA splicing, via spliceosome Source: Reactome
  • negative regulation of phosphatase activity Source: UniProtKB
  • RNA splicing Source: Reactome
  • spliceosomal tri-snRNP complex assembly Source: BHF-UCL
Complete GO annotation...

Keywords - Biological processi

mRNA processing, mRNA splicing

Enzyme and pathway databases

ReactomeiREACT_467. mRNA Splicing - Major Pathway.

Names & Taxonomyi

Protein namesi
Recommended name:
CD2 antigen cytoplasmic tail-binding protein 2
Short name:
CD2 cytoplasmic domain-binding protein 2
Short name:
CD2 tail-binding protein 2
Alternative name(s):
U5 snRNP 52K protein
Short name:
U5-52K
Gene namesi
Name:CD2BP2
Synonyms:KIAA1178
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 16

Organism-specific databases

HGNCiHGNC:1656. CD2BP2.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: HPA
  • nucleoplasm Source: BHF-UCL
  • nucleus Source: BHF-UCL
  • U5 snRNP Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA26209.

Polymorphism and mutation databases

BioMutaiCD2BP2.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 341341CD2 antigen cytoplasmic tail-binding protein 2PRO_0000089437Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei44 – 441N6-acetyllysineBy similarity
Modified residuei46 – 461Phosphoserine1 Publication
Modified residuei49 – 491Phosphoserine7 Publications
Modified residuei118 – 1181Phosphoserine1 Publication
Modified residuei194 – 1941Phosphoserine1 Publication
Modified residuei195 – 1951Phosphoserine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiO95400.
PaxDbiO95400.
PRIDEiO95400.

PTM databases

PhosphoSiteiO95400.

Expressioni

Gene expression databases

BgeeiO95400.
CleanExiHS_CD2BP2.
ExpressionAtlasiO95400. baseline and differential.
GenevestigatoriO95400.

Organism-specific databases

HPAiHPA041508.

Interactioni

Subunit structurei

Component of the U5 snRNP complex composed of the U5 snRNA and at least PRPF6, PRPF8, SNRNP200, EFTUD2, SNRNP40, DDX23, TXNL4A and CD2BP2. Interacts directly with TXNL4A and PRPF6. Interacts (via GYF domain) with CD2 (via Pro-rich sequence in the cytoplasmic domain). Interacts with PQBP1.6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CD2P067293EBI-768015,EBI-3912464
PPP1CAP621362EBI-768015,EBI-357253
PPP1CCP368733EBI-768015,EBI-356283
PRPF6O949064EBI-768015,EBI-536755
SNRPBP14678-23EBI-768015,EBI-372475
TXNL4AP838762EBI-768015,EBI-746539

Protein-protein interaction databases

BioGridi115690. 57 interactions.
IntActiO95400. 14 interactions.
MINTiMINT-99472.
STRINGi9606.ENSP00000304903.

Structurei

Secondary structure

1
341
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi282 – 29312Combined sources
Beta strandi296 – 3005Combined sources
Helixi301 – 3099Combined sources
Beta strandi318 – 3247Combined sources
Helixi332 – 3343Combined sources
Helixi337 – 3404Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1GYFNMR-A280-341[»]
1L2ZNMR-A280-341[»]
1SYXX-ray2.34B/D/F262-341[»]
4BWSX-ray2.50C/F280-341[»]
ProteinModelPortaliO95400.
SMRiO95400. Positions 280-341.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO95400.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini280 – 33859GYFPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 GYF domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG301637.
GeneTreeiENSGT00390000012483.
HOGENOMiHOG000007061.
HOVERGENiHBG056920.
InParanoidiO95400.
KOiK13099.
OMAiQMQTWVN.
OrthoDBiEOG7VMP6C.
PhylomeDBiO95400.
TreeFamiTF313042.

Family and domain databases

Gene3Di3.30.1490.40. 1 hit.
InterProiIPR003169. GYF.
[Graphical view]
PfamiPF02213. GYF. 1 hit.
[Graphical view]
SMARTiSM00444. GYF. 1 hit.
[Graphical view]
SUPFAMiSSF55277. SSF55277. 1 hit.
PROSITEiPS50829. GYF. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O95400-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPKRKVTFQG VGDEEDEDEI IVPKKKLVDP VAGSGGPGSR FKGKHSLDSD
60 70 80 90 100
EEEDDDDGGS SKYDILASED VEGQEAATLP SEGGVRITPF NLQEEMEEGH
110 120 130 140 150
FDADGNYFLN RDAQIRDSWL DNIDWVKIRE RPPGQRQASD SEEEDSLGQT
160 170 180 190 200
SMSAQALLEG LLELLLPRET VAGALRRLGA RGGGKGRKGP GQPSSPQRLD
210 220 230 240 250
RLSGLADQMV ARGNLGVYQE TRERLAMRLK GLGCQTLGPH NPTPPPSLDM
260 270 280 290 300
FAEELAEEEL ETPTPTQRGE AESRGDGLVD VMWEYKWENT GDAELYGPFT
310 320 330 340
SAQMQTWVSE GYFPDGVYCR KLDPPGGQFY NSKRIDFDLY T
Length:341
Mass (Da):37,646
Last modified:May 1, 1999 - v1
Checksum:i8E9A7EE0C40474D5
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti231 – 2311G → D.
Corresponds to variant rs13330462 [ dbSNP | Ensembl ].
VAR_050772
Natural varianti262 – 2621T → I.
Corresponds to variant rs34391305 [ dbSNP | Ensembl ].
VAR_050773

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF104222 mRNA. Translation: AAC84141.1.
AK315708 mRNA. Translation: BAG38069.1.
CH471192 Genomic DNA. Translation: EAW52260.1.
BC000495 mRNA. Translation: AAH00495.1.
BC001947 mRNA. Translation: AAH01947.1.
AB033004 mRNA. Translation: BAA86492.1.
CCDSiCCDS10675.1.
RefSeqiNP_001230575.1. NM_001243646.1.
NP_006101.1. NM_006110.2.
UniGeneiHs.202677.

Genome annotation databases

EnsembliENST00000305596; ENSP00000304903; ENSG00000169217.
ENST00000569466; ENSP00000456935; ENSG00000169217.
GeneIDi10421.
KEGGihsa:10421.
UCSCiuc002dxr.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF104222 mRNA. Translation: AAC84141.1.
AK315708 mRNA. Translation: BAG38069.1.
CH471192 Genomic DNA. Translation: EAW52260.1.
BC000495 mRNA. Translation: AAH00495.1.
BC001947 mRNA. Translation: AAH01947.1.
AB033004 mRNA. Translation: BAA86492.1.
CCDSiCCDS10675.1.
RefSeqiNP_001230575.1. NM_001243646.1.
NP_006101.1. NM_006110.2.
UniGeneiHs.202677.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1GYFNMR-A280-341[»]
1L2ZNMR-A280-341[»]
1SYXX-ray2.34B/D/F262-341[»]
4BWSX-ray2.50C/F280-341[»]
ProteinModelPortaliO95400.
SMRiO95400. Positions 280-341.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115690. 57 interactions.
IntActiO95400. 14 interactions.
MINTiMINT-99472.
STRINGi9606.ENSP00000304903.

PTM databases

PhosphoSiteiO95400.

Polymorphism and mutation databases

BioMutaiCD2BP2.

Proteomic databases

MaxQBiO95400.
PaxDbiO95400.
PRIDEiO95400.

Protocols and materials databases

DNASUi10421.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000305596; ENSP00000304903; ENSG00000169217.
ENST00000569466; ENSP00000456935; ENSG00000169217.
GeneIDi10421.
KEGGihsa:10421.
UCSCiuc002dxr.3. human.

Organism-specific databases

CTDi10421.
GeneCardsiGC16M030363.
HGNCiHGNC:1656. CD2BP2.
HPAiHPA041508.
MIMi604470. gene.
neXtProtiNX_O95400.
PharmGKBiPA26209.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG301637.
GeneTreeiENSGT00390000012483.
HOGENOMiHOG000007061.
HOVERGENiHBG056920.
InParanoidiO95400.
KOiK13099.
OMAiQMQTWVN.
OrthoDBiEOG7VMP6C.
PhylomeDBiO95400.
TreeFamiTF313042.

Enzyme and pathway databases

ReactomeiREACT_467. mRNA Splicing - Major Pathway.

Miscellaneous databases

ChiTaRSiCD2BP2. human.
EvolutionaryTraceiO95400.
GeneWikiiCD2BP2.
GenomeRNAii10421.
NextBioi39496.
PROiO95400.
SOURCEiSearch...

Gene expression databases

BgeeiO95400.
CleanExiHS_CD2BP2.
ExpressionAtlasiO95400. baseline and differential.
GenevestigatoriO95400.

Family and domain databases

Gene3Di3.30.1490.40. 1 hit.
InterProiIPR003169. GYF.
[Graphical view]
PfamiPF02213. GYF. 1 hit.
[Graphical view]
SMARTiSM00444. GYF. 1 hit.
[Graphical view]
SUPFAMiSSF55277. SSF55277. 1 hit.
PROSITEiPS50829. GYF. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of a proline-binding motif regulating CD2-triggered T lymphocyte activation."
    Nishizawa K., Freund C., Li J., Wagner G., Reinherz E.L.
    Proc. Natl. Acad. Sci. U.S.A. 95:14897-14902(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH CD2.
  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].
    Tissue: Testis.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  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].
    Tissue: Lung.
  5. "Characterization of cDNA clones selected by the GeneMark analysis from size-fractionated cDNA libraries from human brain."
    Hirosawa M., Nagase T., Ishikawa K., Kikuno R., Nomura N., Ohara O.
    DNA Res. 6:329-336(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 218-341.
    Tissue: Brain.
  6. "The human U5 snRNP 52K protein (CD2BP2) interacts with U5-102K (hPrp6), a U4/U6.U5 tri-snRNP bridging protein, but dissociates upon tri-snRNP formation."
    Laggerbauer B., Liu S., Makarov E., Vornlocher H.P., Makarova O., Ingelfinger D., Achsel T., Luhrmann R.
    RNA 11:598-608(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT, INTERACTION WITH PRPF6 AND TXNL4A, SUBCELLULAR LOCATION.
  7. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. "The network of protein-protein interactions within the human U4/U6.U5 tri-snRNP."
    Liu S., Rauhut R., Vornlocher H.-P., Luehrmann R.
    RNA 12:1418-1430(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT.
  9. "Investigating the functional role of CD2BP2 in T cells."
    Heinze M., Kofler M., Freund C.
    Int. Immunol. 19:1313-1318(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  10. "Quantitative phosphoproteome profiling of Wnt3a-mediated signaling network: indicating the involvement of ribonucleoside-diphosphate reductase M2 subunit phosphorylation at residue serine 20 in canonical Wnt signal transduction."
    Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S., Li S.-J., Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R.
    Mol. Cell. Proteomics 6:1952-1967(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  11. "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-49, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: T-cell.
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. "Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography."
    Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.
    Proteomics 8:1346-1361(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  14. "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-49; SER-118; SER-194 AND SER-195, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "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-46 AND SER-49, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  18. "The GYF domain is a novel structural fold that is involved in lymphoid signaling through proline-rich sequences."
    Freund C., Dotsch V., Nishizawa K., Reinherz E.L., Wagner G.
    Nat. Struct. Biol. 6:656-660(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 280-341.
  19. "Dynamic interaction of CD2 with the GYF and the SH3 domain of compartmentalized effector molecules."
    Freund C., Kuhne R., Yang H., Park S., Reinherz E.L., Wagner G.
    EMBO J. 21:5985-5995(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 280-341, INTERACTION WITH CD2 PEPTIDE, SUBCELLULAR LOCATION.
  20. "Structural basis for the bifunctionality of the U5 snRNP 52K protein (CD2BP2)."
    Nielsen T.K., Liu S., Luhrmann R., Ficner R.
    J. Mol. Biol. 369:902-908(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 256-341 IN COMPLEX WITH TXNL4A, INTERACTION WITH TXNL4A.
  21. "Mutations in the PQBP1 gene prevent its interaction with the spliceosomal protein U5-15 kD."
    Mizuguchi M., Obita T., Serita T., Kojima R., Nabeshima Y., Okazawa H.
    Nat. Commun. 5:3822-3822(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 280-341 IN COMPLEX WITH PQBP1 AND TXNL4A, SUBUNIT.

Entry informationi

Entry nameiCD2B2_HUMAN
AccessioniPrimary (citable) accession number: O95400
Secondary accession number(s): B2RDX2, Q9ULP2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2003
Last sequence update: May 1, 1999
Last modified: April 29, 2015
This is version 130 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, Reference proteome

Documents

  1. Human chromosome 16
    Human chromosome 16: 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.