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Protein

NFATC2-interacting protein

Gene

NFATC2IP

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

In T-helper 2 (Th2) cells, regulates the magnitude of NFAT-driven transcription of a specific subset of cytokine genes, including IL3, IL4, IL5 and IL13, but not IL2. Recruits PRMT1 to the IL4 promoter; this leads to enhancement of histone H4 'Arg-3'-methylation and facilitates subsequent histone acetylation at the IL4 locus, thus promotes robust cytokine expression (By similarity). Down-regulates formation of poly-SUMO chains by UBE2I/UBC9 (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
NFATC2-interacting protein
Alternative name(s):
45 kDa NF-AT-interacting protein
Short name:
45 kDa NFAT-interacting protein
Nuclear factor of activated T-cells, cytoplasmic 2-interacting protein
Gene namesi
Name:NFATC2IP
Synonyms:NIP45
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 16

Organism-specific databases

HGNCiHGNC:25906. NFATC2IP.

Subcellular locationi

  • Nucleus By similarity
  • Cytoplasm By similarity

  • Note: TRAF1 is associated with a fraction of NFATC2IP in the cytoplasm and prevents its translocation to the nucleus.By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134887712.

Polymorphism and mutation databases

BioMutaiNFATC2IP.
DMDMi74751188.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 419419NFATC2-interacting proteinPRO_0000281008Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei54 – 541PhosphoserineBy similarity
Modified residuei84 – 841PhosphoserineCombined sources
Modified residuei88 – 881PhosphoserineBy similarity
Modified residuei90 – 901PhosphoserineBy similarity
Modified residuei92 – 921PhosphoserineBy similarity
Modified residuei127 – 1271PhosphoserineCombined sources
Modified residuei198 – 1981PhosphoserineCombined sources
Modified residuei201 – 2011PhosphoserineCombined sources
Modified residuei204 – 2041PhosphoserineCombined sources
Modified residuei220 – 2201PhosphoserineCombined sources
Modified residuei314 – 3141PhosphoserineCombined sources
Modified residuei316 – 3161PhosphothreonineCombined sources
Modified residuei318 – 3181PhosphothreonineCombined sources
Modified residuei369 – 3691PhosphoserineCombined sources
Modified residuei390 – 3901PhosphoserineCombined sources

Post-translational modificationi

Methylation at the N-terminus by PRMT1 modulates interaction with the NFAT complex and results in augmented cytokine production.By similarity

Keywords - PTMi

Methylation, Phosphoprotein

Proteomic databases

EPDiQ8NCF5.
MaxQBiQ8NCF5.
PaxDbiQ8NCF5.
PeptideAtlasiQ8NCF5.
PRIDEiQ8NCF5.
TopDownProteomicsiQ8NCF5-2. [Q8NCF5-2]

PTM databases

iPTMnetiQ8NCF5.
PhosphoSiteiQ8NCF5.

Expressioni

Gene expression databases

BgeeiQ8NCF5.
CleanExiHS_NFATC2IP.
ExpressionAtlasiQ8NCF5. baseline and differential.
GenevisibleiQ8NCF5. HS.

Interactioni

Subunit structurei

Interacts with NFATC2, TRAF1, TRAF2 and PRMT1. Interacts with UBE2I/UBC9 (By similarity).By similarity

Protein-protein interaction databases

BioGridi124341. 32 interactions.
IntActiQ8NCF5. 3 interactions.
MINTiMINT-6169168.
STRINGi9606.ENSP00000324792.

Structurei

Secondary structure

1
419
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi252 – 2543Combined sources
Beta strandi265 – 2706Combined sources
Beta strandi272 – 2809Combined sources
Beta strandi282 – 2843Combined sources
Helixi287 – 29711Combined sources
Helixi301 – 3033Combined sources
Beta strandi304 – 3085Combined sources
Helixi319 – 3224Combined sources
Beta strandi329 – 3346Combined sources
Beta strandi347 – 3537Combined sources
Beta strandi359 – 3668Combined sources
Helixi371 – 38212Combined sources
Beta strandi385 – 3873Combined sources
Beta strandi390 – 3934Combined sources
Helixi404 – 4074Combined sources
Beta strandi414 – 4185Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2JXXNMR-A342-419[»]
2L76NMR-A244-338[»]
3RD2X-ray1.60A345-419[»]
ProteinModelPortaliQ8NCF5.
SMRiQ8NCF5. Positions 244-338, 345-419.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8NCF5.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini348 – 41972Ubiquitin-likePROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili209 – 23123Sequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi108 – 1125Poly-Arg

Sequence similaritiesi

Contains 1 ubiquitin-like domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG1769. Eukaryota.
COG5227. LUCA.
GeneTreeiENSGT00390000007119.
HOGENOMiHOG000285948.
HOVERGENiHBG082020.
InParanoidiQ8NCF5.
OMAiSHYEEAM.
OrthoDBiEOG73806D.
PhylomeDBiQ8NCF5.
TreeFamiTF328600.

Family and domain databases

InterProiIPR022617. Rad60/SUMO-like_dom.
IPR029071. Ubiquitin-rel_dom.
IPR000626. Ubiquitin_dom.
[Graphical view]
PfamiPF11976. Rad60-SLD. 1 hit.
[Graphical view]
SMARTiSM00213. UBQ. 2 hits.
[Graphical view]
SUPFAMiSSF54236. SSF54236. 2 hits.
PROSITEiPS50053. UBIQUITIN_2. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

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

Isoform 1 (identifier: Q8NCF5-1) [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
MAEPVGKRGR WSGGSGAGRG GRGGWGGRGR RPRAQRSPSR GTLDVVSVDL
60 70 80 90 100
VTDSDEEILE VATARGAADE VEVEPPEPPG PVASRDNSNS DSEGEDRRPA
110 120 130 140 150
GPPREPVRRR RRLVLDPGEA PLVPVYSGKV KSSLRLIPDD LSLLKLYPPG
160 170 180 190 200
DEEEAELADS SGLYHEGSPS PGSPWKTKLR TKDKEEKKKT EFLDLDNSPL
210 220 230 240 250
SPPSPRTKSR THTRALKKLS EVNKRLQDLR SCLSPKPPQG QEQQGQEDEV
260 270 280 290 300
VLVEGPTLPE TPRLFPLKIR CRADLVRLPL RMSEPLQSVV DHMATHLGVS
310 320 330 340 350
PSRILLLFGE TELSPTATPR TLKLGVADII DCVVLTSSPE ATETSQQLQL
360 370 380 390 400
RVQGKEKHQT LEVSLSRDSP LKTLMSHYEE AMGLSGRKLS FFFDGTKLSG
410
RELPADLGME SGDLIEVWG
Length:419
Mass (Da):45,817
Last modified:October 1, 2002 - v1
Checksum:iCA04220B4BF0B245
GO
Isoform 2 (identifier: Q8NCF5-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-281: Missing.

Note: No experimental confirmation available.
Show »
Length:138
Mass (Da):15,054
Checksum:i88093D025BC0865D
GO
Isoform 3 (identifier: Q8NCF5-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-292: Missing.

Show »
Length:127
Mass (Da):13,831
Checksum:iBE391D16B4ED93BF
GO

Sequence cautioni

The sequence AAM49721.1 differs from that shown. Reason: Frameshift at positions 107 and 114. Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti33 – 331R → W.
Corresponds to variant rs7201257 [ dbSNP | Ensembl ].
VAR_031208

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 292292Missing in isoform 3. 2 PublicationsVSP_023931Add
BLAST
Alternative sequencei1 – 281281Missing in isoform 2. 1 PublicationVSP_023932Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK027545 mRNA. Translation: BAB55189.1.
AK074761 mRNA. Translation: BAC11189.1.
AK297333 mRNA. Translation: BAH12551.1.
AK316535 mRNA. Translation: BAH14906.1.
AF458593 mRNA. Translation: AAM49721.1. Frameshift.
BC018311 mRNA. Translation: AAH18311.2.
BC021551 mRNA. Translation: AAH21551.2.
BC068007 mRNA. Translation: AAH68007.1.
BC080628 mRNA. Translation: AAH80628.1.
BC101741 mRNA. Translation: AAI01742.1.
BC112182 mRNA. Translation: AAI12183.1.
CCDSiCCDS10645.1. [Q8NCF5-1]
RefSeqiNP_116204.3. NM_032815.3. [Q8NCF5-1]
UniGeneiHs.513470.

Genome annotation databases

EnsembliENST00000320805; ENSP00000324792; ENSG00000176953. [Q8NCF5-1]
ENST00000568148; ENSP00000454958; ENSG00000176953. [Q8NCF5-3]
GeneIDi84901.
KEGGihsa:84901.
UCSCiuc002dru.4. human. [Q8NCF5-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK027545 mRNA. Translation: BAB55189.1.
AK074761 mRNA. Translation: BAC11189.1.
AK297333 mRNA. Translation: BAH12551.1.
AK316535 mRNA. Translation: BAH14906.1.
AF458593 mRNA. Translation: AAM49721.1. Frameshift.
BC018311 mRNA. Translation: AAH18311.2.
BC021551 mRNA. Translation: AAH21551.2.
BC068007 mRNA. Translation: AAH68007.1.
BC080628 mRNA. Translation: AAH80628.1.
BC101741 mRNA. Translation: AAI01742.1.
BC112182 mRNA. Translation: AAI12183.1.
CCDSiCCDS10645.1. [Q8NCF5-1]
RefSeqiNP_116204.3. NM_032815.3. [Q8NCF5-1]
UniGeneiHs.513470.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2JXXNMR-A342-419[»]
2L76NMR-A244-338[»]
3RD2X-ray1.60A345-419[»]
ProteinModelPortaliQ8NCF5.
SMRiQ8NCF5. Positions 244-338, 345-419.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi124341. 32 interactions.
IntActiQ8NCF5. 3 interactions.
MINTiMINT-6169168.
STRINGi9606.ENSP00000324792.

PTM databases

iPTMnetiQ8NCF5.
PhosphoSiteiQ8NCF5.

Polymorphism and mutation databases

BioMutaiNFATC2IP.
DMDMi74751188.

Proteomic databases

EPDiQ8NCF5.
MaxQBiQ8NCF5.
PaxDbiQ8NCF5.
PeptideAtlasiQ8NCF5.
PRIDEiQ8NCF5.
TopDownProteomicsiQ8NCF5-2. [Q8NCF5-2]

Protocols and materials databases

DNASUi84901.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000320805; ENSP00000324792; ENSG00000176953. [Q8NCF5-1]
ENST00000568148; ENSP00000454958; ENSG00000176953. [Q8NCF5-3]
GeneIDi84901.
KEGGihsa:84901.
UCSCiuc002dru.4. human. [Q8NCF5-1]

Organism-specific databases

CTDi84901.
GeneCardsiNFATC2IP.
H-InvDBHIX0018982.
HGNCiHGNC:25906. NFATC2IP.
MIMi614525. gene.
neXtProtiNX_Q8NCF5.
PharmGKBiPA134887712.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1769. Eukaryota.
COG5227. LUCA.
GeneTreeiENSGT00390000007119.
HOGENOMiHOG000285948.
HOVERGENiHBG082020.
InParanoidiQ8NCF5.
OMAiSHYEEAM.
OrthoDBiEOG73806D.
PhylomeDBiQ8NCF5.
TreeFamiTF328600.

Miscellaneous databases

EvolutionaryTraceiQ8NCF5.
GenomeRNAii84901.
PROiQ8NCF5.
SOURCEiSearch...

Gene expression databases

BgeeiQ8NCF5.
CleanExiHS_NFATC2IP.
ExpressionAtlasiQ8NCF5. baseline and differential.
GenevisibleiQ8NCF5. HS.

Family and domain databases

InterProiIPR022617. Rad60/SUMO-like_dom.
IPR029071. Ubiquitin-rel_dom.
IPR000626. Ubiquitin_dom.
[Graphical view]
PfamiPF11976. Rad60-SLD. 1 hit.
[Graphical view]
SMARTiSM00213. UBQ. 2 hits.
[Graphical view]
SUPFAMiSSF54236. SSF54236. 2 hits.
PROSITEiPS50053. UBIQUITIN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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; 2 AND 3).
    Tissue: Brain and Uterus.
  2. Guo J.H., Zan Q., Yu L.
    Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Brain.
  3. "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 1 AND 3).
    Tissue: Brain, Eye and Liver.
  4. "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-204, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  5. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
    Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
    Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-316, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-127; SER-198; SER-201; SER-204 AND SER-390, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. "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-204, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  8. "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-204; SER-220; SER-314; THR-318 AND SER-369, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "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-204 AND SER-369, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "Toward a comprehensive characterization of a human cancer cell phosphoproteome."
    Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S.
    J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-84; SER-201; SER-204; SER-314; SER-369 AND SER-390, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma and Erythroleukemia.
  11. "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-204, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  12. "Human NFATC2IP ubiquitin-like domains."
    Northeast structural genomics consortium (NESG)
    Submitted (DEC-2010) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 244-419.

Entry informationi

Entry nameiNF2IP_HUMAN
AccessioniPrimary (citable) accession number: Q8NCF5
Secondary accession number(s): B7Z4G5
, Q66K34, Q6NVK1, Q8NFR2, Q96ST9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 20, 2007
Last sequence update: October 1, 2002
Last modified: July 6, 2016
This is version 113 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

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 one 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.