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Protein

Cell differentiation protein RCD1 homolog

Gene

RQCD1

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

Functioni

Component of the CCR4-NOT complex which is one of the major cellular mRNA deadenylases and is linked to various cellular processes including bulk mRNA degradation, miRNA-mediated repression, translational repression during translational initiation and general transcription regulation. Additional complex functions may be a consequence of its influence on mRNA expression. Involved in down-regulation of MYB- and JUN-dependent transcription. May play a role in cell differentiation (By similarity). Can bind oligonucleotides, such as poly-G, poly-C or poly-T (in vitro), but the physiological relevance of this is not certain. Does not bind poly-A. Enhances ligand-dependent transcriptional activity of nuclear hormone receptors, including RARA, expect ESR1-mediated transcription that is not only slightly increased, if at all.By similarity2 Publications

GO - Molecular functioni

  • protein domain specific binding Source: BHF-UCL
  • protein homodimerization activity Source: BHF-UCL

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Activator, Repressor

Keywords - Biological processi

RNA-mediated gene silencing, Transcription, Transcription regulation, Translation regulation

Enzyme and pathway databases

ReactomeiREACT_20514. Deadenylation of mRNA.

Names & Taxonomyi

Protein namesi
Recommended name:
Cell differentiation protein RCD1 homolog
Short name:
Rcd-1
Alternative name(s):
CCR4-NOT transcription complex subunit 9
Gene namesi
Name:RQCD1
Synonyms:CNOT9, RCD1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:10445. RQCD1.

Subcellular locationi

  • Nucleus By similarity
  • CytoplasmP-body By similarity

  • Note: NANOS2 promotes its localization to P-body.By similarity

GO - Cellular componenti

  • CCR4-NOT complex Source: UniProtKB
  • cytoplasmic mRNA processing body Source: UniProtKB
  • cytosol Source: Reactome
  • membrane Source: UniProtKB
  • nucleus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi227 – 2271R → E: Loss of DNA binding. 1 Publication

Organism-specific databases

PharmGKBiPA34859.

Polymorphism and mutation databases

DMDMi74716599.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 299299Cell differentiation protein RCD1 homologPRO_0000327224Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine2 Publications

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ92600.
PaxDbiQ92600.
PRIDEiQ92600.

PTM databases

PhosphoSiteiQ92600.

Expressioni

Tissue specificityi

Detected in spleen, thymus, prostate, testis, ovary and intestine.1 Publication

Gene expression databases

BgeeiQ92600.
CleanExiHS_RQCD1.
ExpressionAtlasiQ92600. baseline and differential.
GenevisibleiQ92600. HS.

Organism-specific databases

HPAiHPA046622.

Interactioni

Subunit structurei

Homodimer. Component of the CCR4-NOT complex; distinct complexes seem to exist that differ in the participation of probably mutually exclusive catalytic subunits. Interacts with MYB, ATF2, RARA, RARB, RARG, RXRA, RXRB and RXRG. Identified in a complex with ATF2 bound to target DNA (By similarity). Interacts with NANOS2 (By similarity). Directly interacts with ZNF335.By similarity3 Publications

Protein-protein interaction databases

BioGridi114573. 28 interactions.
DIPiDIP-46840N.
IntActiQ92600. 7 interactions.
MINTiMINT-1162783.
STRINGi9606.ENSP00000273064.

Structurei

Secondary structure

1
299
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi19 – 279Combined sources
Beta strandi29 – 313Combined sources
Helixi32 – 4312Combined sources
Turni44 – 485Combined sources
Helixi52 – 587Combined sources
Beta strandi59 – 613Combined sources
Helixi62 – 7110Combined sources
Helixi72 – 765Combined sources
Turni77 – 804Combined sources
Helixi84 – 10219Combined sources
Turni104 – 1063Combined sources
Helixi107 – 1126Combined sources
Helixi115 – 1184Combined sources
Helixi120 – 1234Combined sources
Helixi130 – 14718Combined sources
Helixi152 – 1609Combined sources
Helixi164 – 17310Combined sources
Helixi176 – 19116Combined sources
Helixi193 – 1997Combined sources
Helixi203 – 22220Combined sources
Helixi226 – 23914Combined sources
Helixi243 – 25210Combined sources
Helixi255 – 2573Combined sources
Turni261 – 2688Combined sources
Helixi270 – 28415Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2FV2X-ray2.20A/B/C/D18-285[»]
4CRUX-ray1.65B19-285[»]
4CRVX-ray2.05B19-285[»]
4CT6X-ray2.10B18-285[»]
4CT7X-ray1.90B16-285[»]
ProteinModelPortaliQ92600.
SMRiQ92600. Positions 16-284.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ92600.

Family & Domainsi

Sequence similaritiesi

Belongs to the RCD1 family.Curated

Phylogenomic databases

eggNOGiCOG5209.
GeneTreeiENSGT00390000001225.
HOGENOMiHOG000192069.
HOVERGENiHBG056785.
InParanoidiQ92600.
KOiK12606.
OMAiCVASHND.
OrthoDBiEOG7M98GN.
PhylomeDBiQ92600.
TreeFamiTF105734.

Family and domain databases

Gene3Di1.25.10.10. 1 hit.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR007216. Rcd1.
[Graphical view]
PANTHERiPTHR12262. PTHR12262. 1 hit.
PfamiPF04078. Rcd1. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 1 hit.

Sequences (3)i

Sequence statusi: Complete.

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

Isoform 1 (identifier: Q92600-1) [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
MHSLATAAPV PTTLAQVDRE KIYQWINELS SPETRENALL ELSKKRESVP
60 70 80 90 100
DLAPMLWHSF GTIAALLQEI VNIYPSINPP TLTAHQSNRV CNALALLQCV
110 120 130 140 150
ASHPETRSAF LAAHIPLFLY PFLHTVSKTR PFEYLRLTSL GVIGALVKTD
160 170 180 190 200
EQEVINFLLT TEIIPLCLRI MESGSELSKT VATFILQKIL LDDTGLAYIC
210 220 230 240 250
QTYERFSHVA MILGKMVLQL SKEPSARLLK HVVRCYLRLS DNPRAREALR
260 270 280 290
QCLPDQLKDT TFAQVLKDDT TTKRWLAQLV KNLQEGQVTD PRGIPLPPQ
Length:299
Mass (Da):33,631
Last modified:February 1, 1997 - v1
Checksum:iCFA0E108F5E9D8F2
GO
Isoform 2 (identifier: Q92600-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     143-143: I → IVETGFHHVGQADLELPTSSDLPASASQSAGIT

Note: No experimental confirmation available.
Show »
Length:331
Mass (Da):36,837
Checksum:iAD81339464CE9A5C
GO
Isoform 3 (identifier: Q92600-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     245-258: AREALRQCLPDQLK → FSDLTFCWSSFQRK
     259-299: Missing.

Show »
Length:258
Mass (Da):29,140
Checksum:iAA7F7A655A9AFD3E
GO

Sequence cautioni

The sequence AAH07102.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti143 – 1431I → T.1 Publication
Corresponds to variant rs17856204 [ dbSNP | Ensembl ].
VAR_042429

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei143 – 1431I → IVETGFHHVGQADLELPTSS DLPASASQSAGIT in isoform 2. 1 PublicationVSP_054371
Alternative sequencei245 – 25814AREAL…PDQLK → FSDLTFCWSSFQRK in isoform 3. 1 PublicationVSP_055744Add
BLAST
Alternative sequencei259 – 29941Missing in isoform 3. 1 PublicationVSP_055745Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D87957 Genomic DNA. Translation: BAA13508.1.
AK293281 mRNA. Translation: BAH11481.1.
AC012510 Genomic DNA. No translation available.
CH471063 Genomic DNA. Translation: EAW70625.1.
CH471063 Genomic DNA. Translation: EAW70624.1.
BC007102 mRNA. Translation: AAH07102.2. Different initiation.
BC137455 mRNA. Translation: AAI37456.1.
BC137456 mRNA. Translation: AAI37457.1.
CCDSiCCDS33379.1. [Q92600-1]
CCDS63123.1. [Q92600-3]
RefSeqiNP_001258563.1. NM_001271634.1. [Q92600-2]
NP_001258564.1. NM_001271635.1. [Q92600-3]
NP_005435.1. NM_005444.2. [Q92600-1]
UniGeneiHs.148767.

Genome annotation databases

EnsembliENST00000273064; ENSP00000273064; ENSG00000144580. [Q92600-1]
ENST00000295701; ENSP00000295701; ENSG00000144580. [Q92600-3]
ENST00000542068; ENSP00000443687; ENSG00000144580. [Q92600-1]
ENST00000627282; ENSP00000486540; ENSG00000144580. [Q92600-2]
GeneIDi9125.
KEGGihsa:9125.
UCSCiuc002vih.2. human.
uc010zkh.3. human. [Q92600-1]
uc010zki.3. human.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D87957 Genomic DNA. Translation: BAA13508.1.
AK293281 mRNA. Translation: BAH11481.1.
AC012510 Genomic DNA. No translation available.
CH471063 Genomic DNA. Translation: EAW70625.1.
CH471063 Genomic DNA. Translation: EAW70624.1.
BC007102 mRNA. Translation: AAH07102.2. Different initiation.
BC137455 mRNA. Translation: AAI37456.1.
BC137456 mRNA. Translation: AAI37457.1.
CCDSiCCDS33379.1. [Q92600-1]
CCDS63123.1. [Q92600-3]
RefSeqiNP_001258563.1. NM_001271634.1. [Q92600-2]
NP_001258564.1. NM_001271635.1. [Q92600-3]
NP_005435.1. NM_005444.2. [Q92600-1]
UniGeneiHs.148767.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2FV2X-ray2.20A/B/C/D18-285[»]
4CRUX-ray1.65B19-285[»]
4CRVX-ray2.05B19-285[»]
4CT6X-ray2.10B18-285[»]
4CT7X-ray1.90B16-285[»]
ProteinModelPortaliQ92600.
SMRiQ92600. Positions 16-284.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114573. 28 interactions.
DIPiDIP-46840N.
IntActiQ92600. 7 interactions.
MINTiMINT-1162783.
STRINGi9606.ENSP00000273064.

PTM databases

PhosphoSiteiQ92600.

Polymorphism and mutation databases

DMDMi74716599.

Proteomic databases

MaxQBiQ92600.
PaxDbiQ92600.
PRIDEiQ92600.

Protocols and materials databases

DNASUi9125.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000273064; ENSP00000273064; ENSG00000144580. [Q92600-1]
ENST00000295701; ENSP00000295701; ENSG00000144580. [Q92600-3]
ENST00000542068; ENSP00000443687; ENSG00000144580. [Q92600-1]
ENST00000627282; ENSP00000486540; ENSG00000144580. [Q92600-2]
GeneIDi9125.
KEGGihsa:9125.
UCSCiuc002vih.2. human.
uc010zkh.3. human. [Q92600-1]
uc010zki.3. human.

Organism-specific databases

CTDi9125.
GeneCardsiGC02P219433.
HGNCiHGNC:10445. RQCD1.
HPAiHPA046622.
MIMi612054. gene.
neXtProtiNX_Q92600.
PharmGKBiPA34859.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5209.
GeneTreeiENSGT00390000001225.
HOGENOMiHOG000192069.
HOVERGENiHBG056785.
InParanoidiQ92600.
KOiK12606.
OMAiCVASHND.
OrthoDBiEOG7M98GN.
PhylomeDBiQ92600.
TreeFamiTF105734.

Enzyme and pathway databases

ReactomeiREACT_20514. Deadenylation of mRNA.

Miscellaneous databases

ChiTaRSiRQCD1. human.
EvolutionaryTraceiQ92600.
GenomeRNAii9125.
NextBioi34205.
PROiQ92600.
SOURCEiSearch...

Gene expression databases

BgeeiQ92600.
CleanExiHS_RQCD1.
ExpressionAtlasiQ92600. baseline and differential.
GenevisibleiQ92600. HS.

Family and domain databases

Gene3Di1.25.10.10. 1 hit.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR007216. Rcd1.
[Graphical view]
PANTHERiPTHR12262. PTHR12262. 1 hit.
PfamiPF04078. Rcd1. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Novel factor highly conserved among eukaryotes controls sexual development in fission yeast."
    Okazaki N., Okazaki K., Watanabe Y., Kato-Hayashi M., Yamamoto M., Okayama H.
    Mol. Cell. Biol. 18:887-895(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY.
    Tissue: Foreskin.
  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] (ISOFORM 2).
  3. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [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 1 AND 3), VARIANT THR-143.
    Tissue: Brain.
  6. Bienvenut W.V., Lempens A., Norman J.C.
    Submitted (OCT-2009) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 1-21; 36-44; 180-188 AND 275-292, ACETYLATION AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Ovarian carcinoma.
  7. "Components of the CCR4-NOT complex function as nuclear hormone receptor coactivators via association with the NRC-interacting Factor NIF-1."
    Garapaty S., Mahajan M.A., Samuels H.H.
    J. Biol. Chem. 283:6806-6816(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH ZNF335.
  8. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "C2ORF29/CNOT11 and CNOT10 form a new module of the CCR4-NOT complex."
    Mauxion F., Preve B., Seraphin B.
    RNA Biol. 10:267-276(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE CCR4-NOT COMPLEX.
  11. "Atomic model of human Rcd-1 reveals an armadillo-like-repeat protein with in vitro nucleic acid binding properties."
    Garces R.G., Gillon W., Pai E.F.
    Protein Sci. 16:176-188(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 18-285, DOMAIN, SUBUNIT, FUNCTION, MUTAGENESIS OF ARG-227.

Entry informationi

Entry nameiRCD1_HUMAN
AccessioniPrimary (citable) accession number: Q92600
Secondary accession number(s): B2RPI0
, B5MDQ4, B7Z1E5, Q96IX4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 8, 2008
Last sequence update: February 1, 1997
Last modified: June 24, 2015
This is version 126 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 2
    Human chromosome 2: 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.