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Protein

F-box only protein 44

Gene

FBXO44

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

Functioni

Substrate-recognition component of the SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex.

Keywords - Biological processi

Ubl conjugation pathway

Enzyme and pathway databases

ReactomeiR-HSA-983168. Antigen processing: Ubiquitination & Proteasome degradation.

Names & Taxonomyi

Protein namesi
Recommended name:
F-box only protein 44
Alternative name(s):
F-box protein FBX30
F-box/G-domain protein 3
Gene namesi
Name:FBXO44
Synonyms:FBG3, FBX30, FBX44, FBX6A, FBXO6A
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:24847. FBXO44.

Subcellular locationi

GO - Cellular componenti

  • SCF ubiquitin ligase complex Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134863106.

Polymorphism and mutation databases

BioMutaiFBXO44.
DMDMi61252661.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 255255F-box only protein 44PRO_0000119945Add
BLAST

Proteomic databases

EPDiQ9H4M3.
MaxQBiQ9H4M3.
PaxDbiQ9H4M3.
PRIDEiQ9H4M3.

PTM databases

PhosphoSiteiQ9H4M3.

Expressioni

Tissue specificityi

Abundantly expressed in brain and kidney. Expressed at lower levels in heart, spleen and liver.1 Publication

Gene expression databases

BgeeiQ9H4M3.
CleanExiHS_FBXO44.
ExpressionAtlasiQ9H4M3. baseline and differential.
GenevisibleiQ9H4M3. HS.

Organism-specific databases

HPAiHPA003363.

Interactioni

Subunit structurei

Part of a SCF (SKP1-cullin-F-box) protein ligase complex. Interacts with SKP1 and CUL1.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
C17orf59Q96GS44EBI-2322644,EBI-10193358
SERTAD3Q9UJW93EBI-2322644,EBI-748621
SKP1P632084EBI-2322644,EBI-307486

Protein-protein interaction databases

BioGridi125038. 16 interactions.
IntActiQ9H4M3. 4 interactions.
STRINGi9606.ENSP00000251547.

Structurei

Secondary structure

1
255
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi6 – 83Combined sources
Helixi11 – 199Combined sources
Helixi23 – 286Combined sources
Helixi30 – 323Combined sources
Helixi35 – 417Combined sources
Helixi44 – 5310Combined sources
Helixi68 – 7710Combined sources
Beta strandi82 – 843Combined sources
Turni88 – 936Combined sources
Beta strandi95 – 995Combined sources
Beta strandi105 – 1084Combined sources
Helixi111 – 1144Combined sources
Beta strandi117 – 1204Combined sources
Beta strandi124 – 1274Combined sources
Beta strandi133 – 1408Combined sources
Helixi142 – 1443Combined sources
Helixi148 – 1547Combined sources
Beta strandi157 – 1659Combined sources
Beta strandi171 – 18111Combined sources
Beta strandi187 – 1915Combined sources
Helixi195 – 2017Combined sources
Beta strandi203 – 2053Combined sources
Beta strandi207 – 2137Combined sources
Beta strandi222 – 23110Combined sources
Beta strandi242 – 25110Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3WSOX-ray2.60A1-255[»]
ProteinModelPortaliQ9H4M3.
SMRiQ9H4M3. Positions 2-253.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini3 – 5048F-boxPROSITE-ProRule annotationAdd
BLAST
Domaini71 – 252182FBAPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 F-box domain.PROSITE-ProRule annotation
Contains 1 FBA (F-box associated) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG410IK6V. Eukaryota.
ENOG4111MF5. LUCA.
GeneTreeiENSGT00390000003865.
HOVERGENiHBG003593.
InParanoidiQ9H4M3.
KOiK10103.
OrthoDBiEOG7DRJ3R.
PhylomeDBiQ9H4M3.
TreeFamiTF320527.

Family and domain databases

Gene3Di2.60.120.260. 1 hit.
InterProiIPR007397. F-box-assoc_dom.
IPR001810. F-box_dom.
IPR008979. Galactose-bd-like.
[Graphical view]
PfamiPF12937. F-box-like. 1 hit.
PF04300. FBA. 1 hit.
[Graphical view]
SMARTiSM01198. FBA. 1 hit.
SM00256. FBOX. 1 hit.
[Graphical view]
SUPFAMiSSF49785. SSF49785. 1 hit.
SSF81383. SSF81383. 1 hit.
PROSITEiPS51114. FBA. 1 hit.
PS50181. FBOX. 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: Q9H4M3-1) [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
MAVGNINELP ENILLELFTH VPARQLLLNC RLVCSLWRDL IDLVTLWKRK
60 70 80 90 100
CLREGFITED WDQPVADWKI FYFLRSLHRN LLHNPCAEEG FEFWSLDVNG
110 120 130 140 150
GDEWKVEDLS RDQRKEFPND QVKKYFVTSY YTCLKSQVVD LKAEGYWEEL
160 170 180 190 200
MDTTRPDIEV KDWFAARPDC GSKYQLCVQL LSSAHAPLGT FQPDPATIQQ
210 220 230 240 250
KSDAKWREVS HTFSNYPPGV RYIWFQHGGV DTHYWAGWYG PRVTNSSITI

GPPLP
Length:255
Mass (Da):29,747
Last modified:March 15, 2005 - v3
Checksum:i3DA167B70E22A7E8
GO
Isoform 2 (identifier: Q9H4M3-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     123-224: KKYFVTSYYT...NYPPGVRYIW → RSQARLRVQV...TPPEPPSAEP
     225-255: Missing.

Show »
Length:224
Mass (Da):25,698
Checksum:i7016A8750CB6FB71
GO

Sequence cautioni

The sequence CAI20210.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence CAI20213.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti101 – 1011G → D in CAH18221 (PubMed:17974005).Curated
Sequence conflicti251 – 2511G → R in AAK77940 (PubMed:12383498).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei123 – 224102KKYFV…VRYIW → RSQARLRVQVPAVRSAPVVR ARASGDLPARPGDHPAEERC QVEGGLPHILQLPARRPLHL VSARRRGHSLLGRLVRPEGH QQQHHHRAPAALTPPEPPSA EP in isoform 2. 3 PublicationsVSP_011346Add
BLAST
Alternative sequencei225 – 25531Missing in isoform 2. 3 PublicationsVSP_011347Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY007380 mRNA. Translation: AAG09623.1.
AY040878 mRNA. Translation: AAK77940.1.
AK301418 mRNA. Translation: BAH13479.1.
AK055344 mRNA. Translation: BAG51504.1.
CR749368 mRNA. Translation: CAH18221.1.
AL031731 Genomic DNA. Translation: CAI20210.1. Sequence problems.
AL031731 Genomic DNA. Translation: CAI20211.1.
AL031731 Genomic DNA. Translation: CAI20212.1.
AL031731 Genomic DNA. Translation: CAI20213.1. Sequence problems.
CH471130 Genomic DNA. Translation: EAW71690.1.
CH471130 Genomic DNA. Translation: EAW71691.1.
BC007832 mRNA. Translation: AAH07832.1.
CCDSiCCDS131.1. [Q9H4M3-2]
CCDS132.1. [Q9H4M3-1]
RefSeqiNP_001014765.1. NM_001014765.1. [Q9H4M3-1]
NP_001291719.1. NM_001304790.1. [Q9H4M3-2]
NP_001291720.1. NM_001304791.1. [Q9H4M3-1]
NP_149438.2. NM_033182.5. [Q9H4M3-1]
NP_904319.1. NM_183412.2. [Q9H4M3-2]
NP_904320.1. NM_183413.2. [Q9H4M3-2]
XP_006711108.1. XM_006711045.2. [Q9H4M3-1]
UniGeneiHs.556006.

Genome annotation databases

EnsembliENST00000251546; ENSP00000251546; ENSG00000132879. [Q9H4M3-2]
ENST00000251547; ENSP00000251547; ENSG00000132879. [Q9H4M3-1]
ENST00000376760; ENSP00000365951; ENSG00000132879. [Q9H4M3-2]
ENST00000376762; ENSP00000365953; ENSG00000132879. [Q9H4M3-2]
ENST00000376770; ENSP00000365961; ENSG00000132879. [Q9H4M3-1]
GeneIDi93611.
KEGGihsa:93611.
UCSCiuc001ask.4. human. [Q9H4M3-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

Functional Glycomics Gateway - Glycan Binding

FLAG-FBG3

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY007380 mRNA. Translation: AAG09623.1.
AY040878 mRNA. Translation: AAK77940.1.
AK301418 mRNA. Translation: BAH13479.1.
AK055344 mRNA. Translation: BAG51504.1.
CR749368 mRNA. Translation: CAH18221.1.
AL031731 Genomic DNA. Translation: CAI20210.1. Sequence problems.
AL031731 Genomic DNA. Translation: CAI20211.1.
AL031731 Genomic DNA. Translation: CAI20212.1.
AL031731 Genomic DNA. Translation: CAI20213.1. Sequence problems.
CH471130 Genomic DNA. Translation: EAW71690.1.
CH471130 Genomic DNA. Translation: EAW71691.1.
BC007832 mRNA. Translation: AAH07832.1.
CCDSiCCDS131.1. [Q9H4M3-2]
CCDS132.1. [Q9H4M3-1]
RefSeqiNP_001014765.1. NM_001014765.1. [Q9H4M3-1]
NP_001291719.1. NM_001304790.1. [Q9H4M3-2]
NP_001291720.1. NM_001304791.1. [Q9H4M3-1]
NP_149438.2. NM_033182.5. [Q9H4M3-1]
NP_904319.1. NM_183412.2. [Q9H4M3-2]
NP_904320.1. NM_183413.2. [Q9H4M3-2]
XP_006711108.1. XM_006711045.2. [Q9H4M3-1]
UniGeneiHs.556006.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3WSOX-ray2.60A1-255[»]
ProteinModelPortaliQ9H4M3.
SMRiQ9H4M3. Positions 2-253.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi125038. 16 interactions.
IntActiQ9H4M3. 4 interactions.
STRINGi9606.ENSP00000251547.

PTM databases

PhosphoSiteiQ9H4M3.

Polymorphism and mutation databases

BioMutaiFBXO44.
DMDMi61252661.

Proteomic databases

EPDiQ9H4M3.
MaxQBiQ9H4M3.
PaxDbiQ9H4M3.
PRIDEiQ9H4M3.

Protocols and materials databases

DNASUi93611.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000251546; ENSP00000251546; ENSG00000132879. [Q9H4M3-2]
ENST00000251547; ENSP00000251547; ENSG00000132879. [Q9H4M3-1]
ENST00000376760; ENSP00000365951; ENSG00000132879. [Q9H4M3-2]
ENST00000376762; ENSP00000365953; ENSG00000132879. [Q9H4M3-2]
ENST00000376770; ENSP00000365961; ENSG00000132879. [Q9H4M3-1]
GeneIDi93611.
KEGGihsa:93611.
UCSCiuc001ask.4. human. [Q9H4M3-1]

Organism-specific databases

CTDi93611.
GeneCardsiFBXO44.
HGNCiHGNC:24847. FBXO44.
HPAiHPA003363.
MIMi609111. gene.
neXtProtiNX_Q9H4M3.
PharmGKBiPA134863106.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IK6V. Eukaryota.
ENOG4111MF5. LUCA.
GeneTreeiENSGT00390000003865.
HOVERGENiHBG003593.
InParanoidiQ9H4M3.
KOiK10103.
OrthoDBiEOG7DRJ3R.
PhylomeDBiQ9H4M3.
TreeFamiTF320527.

Enzyme and pathway databases

ReactomeiR-HSA-983168. Antigen processing: Ubiquitination & Proteasome degradation.

Miscellaneous databases

ChiTaRSiFBXO44. human.
GenomeRNAii93611.
NextBioi78147.
PROiQ9H4M3.
SOURCEiSearch...

Gene expression databases

BgeeiQ9H4M3.
CleanExiHS_FBXO44.
ExpressionAtlasiQ9H4M3. baseline and differential.
GenevisibleiQ9H4M3. HS.

Family and domain databases

Gene3Di2.60.120.260. 1 hit.
InterProiIPR007397. F-box-assoc_dom.
IPR001810. F-box_dom.
IPR008979. Galactose-bd-like.
[Graphical view]
PfamiPF12937. F-box-like. 1 hit.
PF04300. FBA. 1 hit.
[Graphical view]
SMARTiSM01198. FBA. 1 hit.
SM00256. FBOX. 1 hit.
[Graphical view]
SUPFAMiSSF49785. SSF49785. 1 hit.
SSF81383. SSF81383. 1 hit.
PROSITEiPS51114. FBA. 1 hit.
PS50181. FBOX. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Fbx30: a novel member of NFB42 class of Fbx genes."
    Paulson H.L., Koppenhafer S.L.
    Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    Tissue: Brain.
  2. "A new subfamily of structurally related human F-box proteins."
    Ilyin G.P., Serandour A.L., Pigeon C., Rialland M., Glaise D., Guguen-Guillouzo C.
    Gene 296:11-20(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
  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] (ISOFORMS 1 AND 2).
    Tissue: Brain and Synovium.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Retina.
  5. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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 2).
    Tissue: B-cell.
  8. "Diversity in tissue expression, substrate binding, and SCF complex formation for a lectin family of ubiquitin ligases."
    Glenn K.A., Nelson R.F., Wen H.M., Mallinger A.J., Paulson H.L.
    J. Biol. Chem. 283:12717-12729(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: LACK OF SUGAR-BINDING, INTERACTION WITH CUL1 AND SKP1, IDENTIFICATION IN SCF-COMPLEX.

Entry informationi

Entry nameiFBX44_HUMAN
AccessioniPrimary (citable) accession number: Q9H4M3
Secondary accession number(s): B3KNZ2
, B7Z743, Q5TGX2, Q5TGX4, Q5TGX5, Q68DJ9, Q8WWY2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 26, 2001
Last sequence update: March 15, 2005
Last modified: May 11, 2016
This is version 124 of the entry and version 3 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

Miscellaneous

In contrast to other FBA domain containing proteins, FBXO44 demonstrates no significant binding to any of the 200 glycans tested.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.