Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

DNA-binding protein RFX7

Gene

RFX7

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi11 – 8676RFX-type winged-helixPROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

DNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
DNA-binding protein RFX7
Alternative name(s):
Regulatory factor X 7
Regulatory factor X domain-containing protein 2
Gene namesi
Name:RFX7
Synonyms:RFXDC2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 15

Organism-specific databases

HGNCiHGNC:25777. RFX7.

Subcellular locationi

  • Nucleus PROSITE-ProRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA162401255.

Polymorphism and mutation databases

BioMutaiRFX7.
DMDMi121946796.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 13631363DNA-binding protein RFX7PRO_0000342186Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei282 – 2821PhosphoserineCombined sources
Modified residuei358 – 3581PhosphoserineCombined sources
Modified residuei607 – 6071N6-acetyllysineCombined sources
Modified residuei891 – 8911PhosphothreonineCombined sources
Modified residuei1081 – 10811PhosphoserineCombined sources
Modified residuei1232 – 12321PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ2KHR2.
MaxQBiQ2KHR2.
PaxDbiQ2KHR2.
PRIDEiQ2KHR2.

PTM databases

iPTMnetiQ2KHR2.
PhosphoSiteiQ2KHR2.

Expressioni

Gene expression databases

BgeeiQ2KHR2.
CleanExiHS_RFX7.
ExpressionAtlasiQ2KHR2. baseline and differential.
GenevisibleiQ2KHR2. HS.

Organism-specific databases

HPAiHPA035462.
HPA057957.

Interactioni

Protein-protein interaction databases

BioGridi122335. 3 interactions.
IntActiQ2KHR2. 3 interactions.
MINTiMINT-4720321.
STRINGi9606.ENSP00000397644.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4QQIX-ray2.03X85-101[»]
4QQMX-ray1.78B/D85-101[»]
ProteinModelPortaliQ2KHR2.
SMRiQ2KHR2. Positions 14-86.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi538 – 5414Poly-Ser

Sequence similaritiesi

Belongs to the RFX family.PROSITE-ProRule annotation
Contains 1 RFX-type winged-helix DNA-binding domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG410IT80. Eukaryota.
ENOG410XSVI. LUCA.
GeneTreeiENSGT00550000074532.
HOGENOMiHOG000168347.
HOVERGENiHBG098639.
InParanoidiQ2KHR2.
OMAiGDNQAQS.
PhylomeDBiQ2KHR2.
TreeFamiTF321340.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
InterProiIPR003150. DNA-bd_RFX.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF02257. RFX_DNA_binding. 1 hit.
[Graphical view]
SUPFAMiSSF46785. SSF46785. 1 hit.
PROSITEiPS51526. RFX_DBD. 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: Q2KHR2-1) [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
MSSSRAQQMH AFSWIRNTLE EHPETSLPKQ EVYDEYKSYC DNLGYHPLSA
60 70 80 90 100
ADFGKIMKNV FPNMKARRLG TRGKSKYCYS GLRKKAFVHM PTLPNLDFHK
110 120 130 140 150
TGDGLEGAEP SGQLQNIDEE VISSACRLVC EWAQKVLSQP FDTVLELARF
160 170 180 190 200
LVKSHYIGTK SMAALTVMAA APAGMKGITQ PSAFIPTAES NSFQPQVKTL
210 220 230 240 250
PSPIDAKQQL QRKIQKKQQE QKLQSPLPGE SAAKKSESAT SNGVTNLPNG
260 270 280 290 300
NPSILSPQPI GIVVAAVPSP IPVQRTRQLV TSPSPMSSSD GKVLPLNVQV
310 320 330 340 350
VTQHMQSVKQ APKTPQNVPA SPGGDRSARH RYPQILPKPA NTSALTIRSP
360 370 380 390 400
TTVLFTSSPI KTAVVPASHM SSLNVVKMTT ISLTPSNSNT PLKHSASVSS
410 420 430 440 450
ATGTTEESRS VPQIKNGSVV SLQSPGSRSS SAGGTSAVEV KVEPETSSDE
460 470 480 490 500
HPVQCQENSD EAKAPQTPSA LLGQKSNTDG ALQKPSNEGV IEIKATKVCD
510 520 530 540 550
QRTKCKSRCN EMLPGTSTGN NQSTITLSVA SQNLTFTSSS SPPNGDSINK
560 570 580 590 600
DPKLCTKSPR KRLSSTLQET QVPPVKKPIV EQLSAATIEG QKQGSVKKDQ
610 620 630 640 650
KVPHSGKTEG STAGAQIPSK VSVNVSSHIG ANQPLNSSAL VISDSALEQQ
660 670 680 690 700
TTPSSSPDIK VKLEGSVFLL DSDSKSVGSF NPNGWQQITK DSEFISASCE
710 720 730 740 750
QQQDISVMTI PEHSDINDLE KSVWELEGMP QDTYSQQLHS QIQESSLNQI
760 770 780 790 800
QAHSSDQLPL QSELKEFEPS VSQTNESYFP FDDELTQDSI VEELVLMEQQ
810 820 830 840 850
MSMNNSHSYG NCLGMTLQSQ SVTPGAPMSS HTSSTHFYHP IHSNGTPIHT
860 870 880 890 900
PTPTPTPTPT PTPTPTPTSE MIAGSQSLSR ESPCSRLAQT TPVDSALGSS
910 920 930 940 950
RHTPIGTPHS NCSSSVPPSP VECRNPFAFT PISSSMAYHD ASIVSSSPVK
960 970 980 990 1000
PMQRPMATHP DKTKLEWMNN GYSGVGNSSV SGHGILPSYQ ELVEDRFRKP
1010 1020 1030 1040 1050
HAFAVPGQSY QSQSRHHDTH FGRLTPVSPV QHQGATVNNT NKQEGFAVPA
1060 1070 1080 1090 1100
PLDNKGTNSS ASSNFRCRSV SPAVHRQRNL SGSTLYPVSN IPRSNVTPFG
1110 1120 1130 1140 1150
SPVTPEVHVF TNVHTDACAN NIAQRSQSVP LTVMMQTAFP NALQKQANSK
1160 1170 1180 1190 1200
KITNVLLSKL DSDNDDAVRG LGMNNLPSNY TARMNLTQIL EPSTVFPSAN
1210 1220 1230 1240 1250
PQNMIDSSTS VYEFQTPSYL TKSNSTGQIN FSPGDNQAQS EIGEQQLDFN
1260 1270 1280 1290 1300
STVKDLLSGD SLQTNQQLVG QGASDLTNTA SDFSSDIRLS SELSGSINDL
1310 1320 1330 1340 1350
NTLDPNLLFD PGRQQGQDDE ATLEELKNDP LFQQICSESM NSMTSSGFEW
1360
IESKDHPTVE MLG
Length:1,363
Mass (Da):146,896
Last modified:March 7, 2006 - v1
Checksum:i6037DB7455278EAE
GO
Isoform 2 (identifier: Q2KHR2-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1269-1363: VGQGASDLTN...KDHPTVEMLG → CSCPSSLLAGMQM

Show »
Length:1,281
Mass (Da):137,868
Checksum:iD1782B97E3342650
GO

Sequence cautioni

The sequence BAB14381.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAB14988.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAC86441.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti511 – 5111E → K in BAC86441 (PubMed:14702039).Curated
Sequence conflicti739 – 7391H → R in BAC87248 (PubMed:14702039).Curated
Sequence conflicti1093 – 10931R → Q in BAC87248 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti434 – 4341G → V.
Corresponds to variant rs16976751 [ dbSNP | Ensembl ].
VAR_044135
Natural varianti677 – 6771V → L.
Corresponds to variant rs3803460 [ dbSNP | Ensembl ].
VAR_044136
Natural varianti1256 – 12561L → P.
Corresponds to variant rs33984059 [ dbSNP | Ensembl ].
VAR_044137

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1269 – 136395VGQGA…VEMLG → CSCPSSLLAGMQM in isoform 2. 1 PublicationVSP_034394Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK023056 mRNA. Translation: BAB14381.1. Different initiation.
AK024757 mRNA. Translation: BAB14988.1. Different initiation.
AK126103 mRNA. Translation: BAC86441.1. Different initiation.
AK128045 mRNA. Translation: BAC87248.1.
AL834302 mRNA. Translation: CAD38972.1.
BC112936 mRNA. Translation: AAI12937.1.
RefSeqiNP_073752.5. NM_022841.5.
XP_011520227.1. XM_011521925.1. [Q2KHR2-1]
XP_011520228.1. XM_011521926.1. [Q2KHR2-1]
UniGeneiHs.745089.

Genome annotation databases

EnsembliENST00000559447; ENSP00000453281; ENSG00000181827. [Q2KHR2-1]
GeneIDi64864.
KEGGihsa:64864.
UCSCiuc059jng.1. human. [Q2KHR2-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK023056 mRNA. Translation: BAB14381.1. Different initiation.
AK024757 mRNA. Translation: BAB14988.1. Different initiation.
AK126103 mRNA. Translation: BAC86441.1. Different initiation.
AK128045 mRNA. Translation: BAC87248.1.
AL834302 mRNA. Translation: CAD38972.1.
BC112936 mRNA. Translation: AAI12937.1.
RefSeqiNP_073752.5. NM_022841.5.
XP_011520227.1. XM_011521925.1. [Q2KHR2-1]
XP_011520228.1. XM_011521926.1. [Q2KHR2-1]
UniGeneiHs.745089.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4QQIX-ray2.03X85-101[»]
4QQMX-ray1.78B/D85-101[»]
ProteinModelPortaliQ2KHR2.
SMRiQ2KHR2. Positions 14-86.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi122335. 3 interactions.
IntActiQ2KHR2. 3 interactions.
MINTiMINT-4720321.
STRINGi9606.ENSP00000397644.

PTM databases

iPTMnetiQ2KHR2.
PhosphoSiteiQ2KHR2.

Polymorphism and mutation databases

BioMutaiRFX7.
DMDMi121946796.

Proteomic databases

EPDiQ2KHR2.
MaxQBiQ2KHR2.
PaxDbiQ2KHR2.
PRIDEiQ2KHR2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000559447; ENSP00000453281; ENSG00000181827. [Q2KHR2-1]
GeneIDi64864.
KEGGihsa:64864.
UCSCiuc059jng.1. human. [Q2KHR2-1]

Organism-specific databases

CTDi64864.
GeneCardsiRFX7.
HGNCiHGNC:25777. RFX7.
HPAiHPA035462.
HPA057957.
MIMi612660. gene.
neXtProtiNX_Q2KHR2.
PharmGKBiPA162401255.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IT80. Eukaryota.
ENOG410XSVI. LUCA.
GeneTreeiENSGT00550000074532.
HOGENOMiHOG000168347.
HOVERGENiHBG098639.
InParanoidiQ2KHR2.
OMAiGDNQAQS.
PhylomeDBiQ2KHR2.
TreeFamiTF321340.

Miscellaneous databases

ChiTaRSiRFX7. human.
GenomeRNAii64864.
NextBioi67023.
PROiQ2KHR2.
SOURCEiSearch...

Gene expression databases

BgeeiQ2KHR2.
CleanExiHS_RFX7.
ExpressionAtlasiQ2KHR2. baseline and differential.
GenevisibleiQ2KHR2. HS.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
InterProiIPR003150. DNA-bd_RFX.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF02257. RFX_DNA_binding. 1 hit.
[Graphical view]
SUPFAMiSSF46785. SSF46785. 1 hit.
PROSITEiPS51526. RFX_DBD. 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] (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 187-1363 (ISOFORM 1).
    Tissue: Testis.
  2. "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] (ISOFORM 1).
    Tissue: Testis.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 968-1363 (ISOFORM 1).
    Tissue: Melanoma.
  4. "Identification and characterization of novel human tissue-specific RFX transcription factors."
    Aftab S., Semenec L., Chu J.S.-C., Chen N.
    BMC Evol. Biol. 8:226-226(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION.
  5. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
    Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
    J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  6. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "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-282; SER-358; THR-891; SER-1081 AND SER-1232, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  9. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-607, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "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-1081, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "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-1081, 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 nameiRFX7_HUMAN
AccessioniPrimary (citable) accession number: Q2KHR2
Secondary accession number(s): Q6ZRR1
, Q6ZTY6, Q8N3J0, Q9H7A9, Q9H956
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 2008
Last sequence update: March 7, 2006
Last modified: May 11, 2016
This is version 96 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 15
    Human chromosome 15: 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.