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Protein

Corepressor interacting with RBPJ 1

Gene

CIR1

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

Functioni

May modulate splice site selection during alternative splicing of pre-mRNAs (By similarity). Regulates transcription and acts as corepressor for RBPJ. Recruits RBPJ to the Sin3-histone deacetylase complex (HDAC). Required for RBPJ-mediated repression of transcription.By similarity2 Publications

GO - Molecular functioni

  • transcription corepressor activity Source: ProtInc
  • transcription factor activity, RNA polymerase II distal enhancer sequence-specific binding Source: BHF-UCL
  • transcription factor activity, sequence-specific DNA binding Source: ProtInc

GO - Biological processi

  • mRNA processing Source: UniProtKB-KW
  • negative regulation of transcription, DNA-templated Source: UniProtKB
  • regulation of transcription from RNA polymerase II promoter Source: GOC
  • RNA splicing Source: UniProtKB-KW
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Repressor

Keywords - Biological processi

mRNA processing, mRNA splicing, Transcription, Transcription regulation

Enzyme and pathway databases

SignaLinkiQ86X95.

Names & Taxonomyi

Protein namesi
Recommended name:
Corepressor interacting with RBPJ 1
Alternative name(s):
CBF1-interacting corepressor
Recepin
Gene namesi
Name:CIR1
Synonyms:CIR
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:24217. CIR1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB-KW
  • microtubule organizing center Source: UniProtKB-SubCell
  • nuclear speck Source: UniProtKB-SubCell
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA165696415.

Polymorphism and mutation databases

BioMutaiCIR1.
DMDMi74727790.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 450450Corepressor interacting with RBPJ 1PRO_0000247984Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei202 – 2021PhosphoserineCombined sources

Post-translational modificationi

Phosphorylated by NEK6.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ86X95.
MaxQBiQ86X95.
PaxDbiQ86X95.
PRIDEiQ86X95.

PTM databases

iPTMnetiQ86X95.
PhosphoSiteiQ86X95.

Expressioni

Tissue specificityi

Highly expressed in heart, brain, placenta, liver, skeletal muscle and pancreas.1 Publication

Gene expression databases

BgeeiQ86X95.
ExpressionAtlasiQ86X95. baseline and differential.
GenevisibleiQ86X95. HS.

Organism-specific databases

HPAiHPA015784.

Interactioni

Subunit structurei

Interacts with RP9, SNW1, SFRS1, SFRS2,U2AF1, RBPJ, SAP30, HDAC2 NKAP and NEK6. Interacts with Epstein-Barr virus RPMS1. Component of the histone deacetylase complex. Component of the Notch corepressor complex.5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CEP76Q8TAP63EBI-627102,EBI-742887
SRSF1Q079553EBI-627102,EBI-398920
SRSF2Q011304EBI-627102,EBI-627047
U2AF1Q010814EBI-627102,EBI-632461

Protein-protein interaction databases

BioGridi114916. 22 interactions.
IntActiQ86X95. 13 interactions.
MINTiMINT-207899.
STRINGi9606.ENSP00000339723.

Structurei

3D structure databases

ProteinModelPortaliQ86X95.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 121121Interaction with RBPJAdd
BLAST
Regioni204 – 23229Interaction with RP9By similarityAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi235 – 24511Nuclear localization signalSequence analysisAdd
BLAST
Motifi291 – 2988Nuclear localization signalSequence analysis

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi214 – 368155Lys/Ser-richAdd
BLAST
Compositional biasi369 – 45082Arg/Ser-rich (RS domain)Add
BLAST

Phylogenomic databases

eggNOGiKOG3794. Eukaryota.
ENOG410ZVMR. LUCA.
GeneTreeiENSGT00730000111135.
InParanoidiQ86X95.
KOiK06066.
OMAiPRFLKHE.
OrthoDBiEOG7GBFXV.
PhylomeDBiQ86X95.
TreeFamiTF317567.

Family and domain databases

InterProiIPR019339. CIR_N_dom.
[Graphical view]
PfamiPF10197. Cir_N. 1 hit.
[Graphical view]
SMARTiSM01083. Cir_N. 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: Q86X95-1) [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
MGKSFANFMC KKDFHPASKS NIKKVWMAEQ KISYDKKKQE ELMQQYLKEQ
60 70 80 90 100
ESYDNRLLMG DERVKNGLNF MYEAPPGAKK ENKEKEETEG ETEYKFEWQK
110 120 130 140 150
GAPREKYAKD DMNIRDQPFG IQVRNVRCIK CHKWGHVNTD RECPLFGLSG
160 170 180 190 200
INASSVPTDG SGPSMHPSEL IAEMRNSGFA LKRNVLGRNL TANDPSQEYV
210 220 230 240 250
ASEGEEDPEV EFLKSLTTKQ KQKLLRKLDR LEKKKKKKDR KKKKFQKSRS
260 270 280 290 300
KHKKHKSSSS SSSSSSSSSS TETSESSSES ESNNKEKKIQ RKKRKKNKCS
310 320 330 340 350
GHNNSDSEEK DKSKKRKLHE ELSSSHHNRE KAKEKPRFLK HESSREDSKW
360 370 380 390 400
SHSDSDKKSR THKHSPEKRG SERKEGSSRS HGREERSRRS RSRSPGSYKQ
410 420 430 440 450
RETRKRAQRN PGEEQSRRND SRSHGTDLYR GEKMYREHPG GTHTKVTQRE
Length:450
Mass (Da):52,313
Last modified:June 1, 2003 - v1
Checksum:i5D0C1CBD9C87569D
GO
Isoform 2 (identifier: Q86X95-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     162-202: GPSMHPSELI...NDPSQEYVAS → DAVLQIEGFW...KCTGEKLDRK
     203-450: Missing.

Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.
Show »
Length:202
Mass (Da):23,274
Checksum:i6C16582B3E91B8DE
GO

Sequence cautioni

The sequence AAA17853.1 differs from that shown. Reason: Frameshift at positions 135, 151, 177, 203, 261, 299, 391 and 410. Curated
The sequence AAH21175.1 differs from that shown.Contaminating sequence. Potential poly-A sequence.Curated
The sequence AAH38987.1 differs from that shown.Contaminating sequence. Potential poly-A sequence.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti48 – 481K → R in AAD05243 (PubMed:9874765).Curated
Sequence conflicti113 – 1131N → S in AAD05243 (PubMed:9874765).Curated
Sequence conflicti172 – 1721A → G in AAA17853 (Ref. 2) Curated
Sequence conflicti325 – 3251S → T in AAD05243 (PubMed:9874765).Curated
Sequence conflicti325 – 3251S → T in AAA17853 (Ref. 2) Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei162 – 20241GPSMH…EYVAS → DAVLQIEGFWAIDAPLGANS GDEKQWVCTETKCTGEKLDR K in isoform 2. 1 PublicationVSP_020091Add
BLAST
Alternative sequencei203 – 450248Missing in isoform 2. 1 PublicationVSP_020092Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF098297 mRNA. Translation: AAD05243.1.
U03644 mRNA. Translation: AAA17853.1. Frameshift.
AK292389 mRNA. Translation: BAF85078.1.
AC018470 Genomic DNA. Translation: AAY24216.1.
BC015040 mRNA. No translation available.
BC021175 mRNA. Translation: AAH21175.1. Sequence problems.
BC038987 mRNA. Translation: AAH38987.1. Sequence problems.
BC046098 mRNA. Translation: AAH46098.1.
CCDSiCCDS2256.1. [Q86X95-1]
PIRiG01227.
RefSeqiNP_004873.3. NM_004882.3. [Q86X95-1]
UniGeneiHs.632531.

Genome annotation databases

EnsembliENST00000342016; ENSP00000339723; ENSG00000138433. [Q86X95-1]
GeneIDi9541.
KEGGihsa:9541.
UCSCiuc002uim.4. human. [Q86X95-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF098297 mRNA. Translation: AAD05243.1.
U03644 mRNA. Translation: AAA17853.1. Frameshift.
AK292389 mRNA. Translation: BAF85078.1.
AC018470 Genomic DNA. Translation: AAY24216.1.
BC015040 mRNA. No translation available.
BC021175 mRNA. Translation: AAH21175.1. Sequence problems.
BC038987 mRNA. Translation: AAH38987.1. Sequence problems.
BC046098 mRNA. Translation: AAH46098.1.
CCDSiCCDS2256.1. [Q86X95-1]
PIRiG01227.
RefSeqiNP_004873.3. NM_004882.3. [Q86X95-1]
UniGeneiHs.632531.

3D structure databases

ProteinModelPortaliQ86X95.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114916. 22 interactions.
IntActiQ86X95. 13 interactions.
MINTiMINT-207899.
STRINGi9606.ENSP00000339723.

PTM databases

iPTMnetiQ86X95.
PhosphoSiteiQ86X95.

Polymorphism and mutation databases

BioMutaiCIR1.
DMDMi74727790.

Proteomic databases

EPDiQ86X95.
MaxQBiQ86X95.
PaxDbiQ86X95.
PRIDEiQ86X95.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000342016; ENSP00000339723; ENSG00000138433. [Q86X95-1]
GeneIDi9541.
KEGGihsa:9541.
UCSCiuc002uim.4. human. [Q86X95-1]

Organism-specific databases

CTDi9541.
GeneCardsiCIR1.
H-InvDBHIX0023923.
HGNCiHGNC:24217. CIR1.
HPAiHPA015784.
MIMi605228. gene.
neXtProtiNX_Q86X95.
PharmGKBiPA165696415.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3794. Eukaryota.
ENOG410ZVMR. LUCA.
GeneTreeiENSGT00730000111135.
InParanoidiQ86X95.
KOiK06066.
OMAiPRFLKHE.
OrthoDBiEOG7GBFXV.
PhylomeDBiQ86X95.
TreeFamiTF317567.

Enzyme and pathway databases

SignaLinkiQ86X95.

Miscellaneous databases

ChiTaRSiCIR1. human.
GeneWikiiCIR_(gene).
GenomeRNAii9541.
NextBioi35776.
PROiQ86X95.
SOURCEiSearch...

Gene expression databases

BgeeiQ86X95.
ExpressionAtlasiQ86X95. baseline and differential.
GenevisibleiQ86X95. HS.

Family and domain databases

InterProiIPR019339. CIR_N_dom.
[Graphical view]
PfamiPF10197. Cir_N. 1 hit.
[Graphical view]
SMARTiSM01083. Cir_N. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "CIR, a corepressor linking the DNA binding factor CBF1 to the histone deacetylase complex."
    Hsieh J.J.-D., Zhou S., Chen L., Young D.B., Hayward S.D.
    Proc. Natl. Acad. Sci. U.S.A. 96:23-28(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH RBPJ; SAP30 AND HDAC2, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  2. Chai K.X., Li L., Chao J., Chao L.
    Submitted (NOV-1993) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Liver.
  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] (ISOFORM 1).
    Tissue: Testis.
  4. "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].
  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 2).
    Tissue: Eye, Lymph, Testis and Uterus.
  6. "A role for SKIP in EBNA2 activation of CBF1-repressed promoters."
    Zhou S., Fujimuro M., Hsieh J.J., Chen L., Hayward S.D.
    J. Virol. 74:1939-1947(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SNW1.
  7. "Epstein-Barr virus BamHi-a rightward transcript-encoded RPMS protein interacts with the CBF1-associated corepressor CIR to negatively regulate the activity of EBNA2 and NotchIC."
    Zhang J., Chen H., Weinmaster G., Hayward S.D.
    J. Virol. 75:2946-2956(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH EPSTEIN-BARR VIRUS RPMS1, SUBCELLULAR LOCATION.
  8. "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-202, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-202, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "NKAP is a transcriptional repressor of notch signaling and is required for T cell development."
    Pajerowski A.G., Nguyen C., Aghajanian H., Shapiro M.J., Shapiro V.S.
    Immunity 30:696-707(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH NKAP.
  11. "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-202, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  12. "Characterization of hNek6 interactome reveals an important role for its short N-terminal domain and colocalization with proteins at the centrosome."
    Vaz Meirelles G., Ferreira Lanza D.C., da Silva J.C., Santana Bernachi J., Paes Leme A.F., Kobarg J.
    J. Proteome Res. 9:6298-6316(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INTERACTION WITH NEK6, PHOSPHORYLATION.
  13. "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-202, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiCIR1_HUMAN
AccessioniPrimary (citable) accession number: Q86X95
Secondary accession number(s): A6NFI6
, A8K8M4, O95367, Q12804, Q4G1B9, Q6PJI4, Q8IWI2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 5, 2006
Last sequence update: June 1, 2003
Last modified: April 13, 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

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.