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UniProtKB - O43683 (BUB1_HUMAN)

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Protein

Mitotic checkpoint serine/threonine-protein kinase BUB1

Gene

BUB1

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

Functioni

Serine/threonine-protein kinase that performs 2 crucial functions during mitosis: it is essential for spindle-assembly checkpoint signaling and for correct chromosome alignment. Has a key role in the assembly of checkpoint proteins at the kinetochore, being required for the subsequent localization of CENPF, BUB1B, CENPE and MAD2L1. Required for the kinetochore localization of PLK1. Required for centromeric enrichment of AUKRB in prometaphase. Plays an important role in defining SGO1 localization and thereby affects sister chromatid cohesion. Acts as a substrate for anaphase-promoting complex or cyclosome (APC/C) in complex with its activator CDH1 (APC/C-Cdh1). Necessary for ensuring proper chromosome segregation and binding to BUB3 is essential for this function. Can regulate chromosome segregation in a kinetochore-independent manner. Can phosphorylate BUB3. The BUB1-BUB3 complex plays a role in the inhibition of APC/C when spindle-assembly checkpoint is activated and inhibits the ubiquitin ligase activity of APC/C by phosphorylating its activator CDC20. This complex can also phosphorylate MAD1L1. Kinase activity is essential for inhibition of APC/CCDC20 and for chromosome alignment but does not play a major role in the spindle-assembly checkpoint activity. Mediates cell death in response to chromosome missegregation and acts to suppress spontaneous tumorigenesis.8 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulationi

Autophosphorylated when the cells enters mitosis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei821ATPPROSITE-ProRule annotation1
Active sitei917Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi793 – 801ATPPROSITE-ProRule annotation9

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • protein kinase activity Source: ProtInc
  • protein serine/threonine kinase activity Source: UniProtKB-KW
Complete GO annotation...

GO - Biological processi

  • apoptotic process Source: UniProtKB-KW
  • cell division Source: UniProtKB-KW
  • cell proliferation Source: Ensembl
  • meiotic sister chromatid cohesion, centromeric Source: GO_Central
  • mitotic cell cycle checkpoint Source: ProtInc
  • mitotic spindle assembly checkpoint Source: GO_Central
  • regulation of chromosome segregation Source: UniProtKB
  • regulation of sister chromatid cohesion Source: UniProtKB
  • sister chromatid cohesion Source: Reactome
  • spindle assembly checkpoint Source: UniProtKB
  • viral process Source: UniProtKB-KW
Complete GO annotation...

Keywordsi

Molecular functionKinase, Serine/threonine-protein kinase, Transferase
Biological processApoptosis, Cell cycle, Cell division, Chromosome partition, Host-virus interaction, Mitosis
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.11.1. 2681.
ReactomeiR-HSA-2467813. Separation of Sister Chromatids.
R-HSA-2500257. Resolution of Sister Chromatid Cohesion.
R-HSA-5663220. RHO GTPases Activate Formins.
R-HSA-68877. Mitotic Prometaphase.
SignaLinkiO43683.
SIGNORiO43683.

Names & Taxonomyi

Protein namesi
Recommended name:
Mitotic checkpoint serine/threonine-protein kinase BUB1 (EC:2.7.11.1)
Short name:
hBUB1
Alternative name(s):
BUB1A
Gene namesi
Name:BUB1
Synonyms:BUB1L
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
Proteomesi
  • UP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:1148. BUB1.

Subcellular locationi

  • Nucleus
  • Chromosome › centromere › kinetochore

    • Note: Nuclear in interphase cells. Accumulates gradually during G1 and S phase of the cell cycle, peaks at G2/M, and drops dramatically after mitosis. Localizes to the outer kinetochore. Kinetochore localization is required for normal mitotic timing and checkpoint response to spindle damage and occurs very early in prophase. AURKB, KNL1 and INCENP are required for kinetochore localization (By similarity).By similarity

GO - Cellular componenti

  • condensed chromosome kinetochore Source: UniProtKB
  • condensed nuclear chromosome outer kinetochore Source: CACAO
  • cytosol Source: HPA
  • kinetochore Source: UniProtKB
  • membrane Source: UniProtKB
  • nucleoplasm Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Centromere, Chromosome, Kinetochore, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi106A → D or W: Loss of interaction with KNL1. 1 Publication1
Mutagenesisi122L → G: Loss of interaction with KNL1. 1 Publication1
Mutagenesisi130A → S: Partial rescue of the spindle-assembly checkpoint activity. Increased rate of chromosome congression errors. Impaired localization to kinetochores and loss of kinetochore binding of CENPF, SGO1 and BUBR1 but not of MCAK, MAD1L1 or MAD2L1. 1 Publication1
Mutagenesisi535K → A: Loss of ubiquitination and CDH1-dependent degradation; when associated with A-536 and A-537. 1 Publication1
Mutagenesisi536E → A: Loss of ubiquitination and CDH1-dependent degradation; when associated with A-535 and A-537. 1 Publication1
Mutagenesisi537N → A: Loss of ubiquitination and CDH1-dependent degradation; when associated with A-535 and A-536. 1 Publication1
Mutagenesisi609T → A: Diminished interaction with PLK1. 1 Publication1
Mutagenesisi625K → A: Loss of ubiquitination and CDH1-dependent degradation; when associated with A-626 and A-627. 1 Publication1
Mutagenesisi626E → A: Loss of ubiquitination and CDH1-dependent degradation; when associated with A-625 and A-627. 1 Publication1
Mutagenesisi627N → A: Loss of ubiquitination and CDH1-dependent degradation; when associated with A-625 and A-626. 1 Publication1
Mutagenesisi821K → A: Loss of activity. 1 Publication1

Organism-specific databases

DisGeNETi699.
MalaCardsiBUB1.
OpenTargetsiENSG00000169679.
Orphaneti1052. Mosaic variegated aneuploidy syndrome.
PharmGKBiPA81.

Chemistry databases

ChEMBLiCHEMBL1772932.
GuidetoPHARMACOLOGYi1949.

Polymorphism and mutation databases

BioMutaiBUB1.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000856711 – 1085Mitotic checkpoint serine/threonine-protein kinase BUB1Add BLAST1085

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei307PhosphoserineCombined sources1
Modified residuei314PhosphoserineCombined sources1
Modified residuei331PhosphoserineCombined sources1
Modified residuei375PhosphoserineCombined sources1
Modified residuei525PhosphoserineCombined sources1
Modified residuei563PhosphoserineCombined sources1
Modified residuei593PhosphoserineCombined sources1
Modified residuei596PhosphoserineCombined sources1
Modified residuei609Phosphothreonine; by CDK11 Publication1
Modified residuei655PhosphoserineCombined sources1
Modified residuei661PhosphoserineCombined sources1
Modified residuei668PhosphoserineCombined sources1
Modified residuei672PhosphoserineCombined sources1

Post-translational modificationi

Upon spindle-assembly checkpoint activation it is hyperphosphorylated and its kinase activity toward CDC20 is stimulated. Phosphorylation at Thr-609 is required for interaction with PLK1, phosphorylation at this site probably creates a binding site for the POLO-box domain of PLK1, thus enhancing the PLK1-BUB1 interaction.3 Publications
Ubiquitinated and degraded during mitotic exit by APC/C-Cdh1.1 Publication

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiO43683.
PaxDbiO43683.
PeptideAtlasiO43683.
PRIDEiO43683.

PTM databases

iPTMnetiO43683.
PhosphoSitePlusiO43683.

Expressioni

Tissue specificityi

High expression in testis and thymus, less in colon, spleen, lung and small intestine. Expressed in fetal thymus, bone marrow, heart, liver, spleen and thymus. Expression is associated with cells/tissues with a high mitotic index.

Inductioni

Inhibited by phorbol 12-myristate 13-acetate (PMA).

Gene expression databases

BgeeiENSG00000169679.
CleanExiHS_BUB1.
ExpressionAtlasiO43683. baseline and differential.
GenevisibleiO43683. HS.

Organism-specific databases

HPAiHPA006123.

Interactioni

Subunit structurei

Interacts with BUB3 and KNL1. Interacts (when phosphorylated) with PLK1. The BUB1-BUB3 complex interacts with MAD1L1. Interacts with SV40 Large T antigen; this interaction induces activation of a DNA damage response and promotes p53/TP53 stabilization and phosphorylation (Probable).5 Publications

Binary interactionsi

Show more details

Protein-protein interaction databases

BioGridi107164. 49 interactors.
DIPiDIP-24206N.
IntActiO43683. 84 interactors.
MINTiMINT-1460788.
STRINGi9606.ENSP00000302530.

Chemistry databases

BindingDBiO43683.

Structurei

Secondary structure

11085
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi3 – 14Combined sources12
Helixi23 – 35Combined sources13
Helixi43 – 56Combined sources14
Helixi60 – 62Combined sources3
Helixi66 – 76Combined sources11
Helixi82 – 90Combined sources9
Turni91 – 97Combined sources7
Helixi99 – 111Combined sources13
Helixi115 – 127Combined sources13
Helixi133 – 145Combined sources13
Beta strandi737 – 739Combined sources3
Helixi744 – 752Combined sources9
Helixi758 – 760Combined sources3
Beta strandi764 – 766Combined sources3
Beta strandi778 – 782Combined sources5
Beta strandi785 – 795Combined sources11
Beta strandi797 – 805Combined sources9
Beta strandi817 – 825Combined sources9
Helixi828 – 840Combined sources13
Turni843 – 845Combined sources3
Helixi846 – 848Combined sources3
Beta strandi852 – 857Combined sources6
Beta strandi862 – 866Combined sources5
Helixi874 – 882Combined sources9
Beta strandi884 – 886Combined sources3
Helixi891 – 910Combined sources20
Helixi920 – 922Combined sources3
Beta strandi923 – 925Combined sources3
Helixi927 – 930Combined sources4
Beta strandi938 – 941Combined sources4
Beta strandi942 – 944Combined sources3
Helixi953 – 955Combined sources3
Beta strandi967 – 971Combined sources5
Helixi976 – 978Combined sources3
Helixi985 – 1000Combined sources16
Beta strandi1006 – 1009Combined sources4
Beta strandi1012 – 1015Combined sources4
Helixi1025 – 1036Combined sources12
Helixi1047 – 1061Combined sources15
Turni1063 – 1065Combined sources3
Helixi1066 – 1082Combined sources17

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2LAHNMR-A1-150[»]
4A1GX-ray2.60A/B/C/D1-150[»]
4QPMX-ray2.20A/B740-1085[»]
4R8QX-ray2.31A724-1085[»]
5DMZX-ray2.40A/B726-1085[»]
ProteinModelPortaliO43683.
SMRiO43683.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO43683.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini11 – 182BUB1 N-terminalPROSITE-ProRule annotationAdd BLAST172
Domaini787 – 1085Protein kinasePROSITE-ProRule annotationAdd BLAST299

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 146Necessary for kinetochore localizationAdd BLAST146
Regioni99 – 132Necessary for interaction with KNL11 PublicationAdd BLAST34
Regioni229 – 256Necessary for interaction with BUB3Add BLAST28
Regioni458 – 476Essential for loading of BUBR1, MAD1L1 and MAD2L1 to kinetochoresAdd BLAST19

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi58 – 65Nuclear localization signalSequence analysis8
Motifi535 – 537KEN box 13
Motifi625 – 627KEN box 23

Domaini

The KEN box is required for its ubiquitination and degradation.1 Publication
BUB1 N-terminal domain directs kinetochore localization and binding to BUB3.1 Publication

Sequence similaritiesi

Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. BUB1 subfamily.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG1166. Eukaryota.
ENOG410XQ67. LUCA.
GeneTreeiENSGT00520000055622.
HOGENOMiHOG000231751.
HOVERGENiHBG003709.
InParanoidiO43683.
KOiK02178.
OMAiRNNHETW.
OrthoDBiEOG091G00MB.
PhylomeDBiO43683.
TreeFamiTF105455.

Family and domain databases

Gene3Di1.25.40.10. 1 hit.
InterProiView protein in InterPro
IPR015661. Bub1/Mad3.
IPR011009. Kinase-like_dom.
IPR013212. Mad3/Bub1_I.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
IPR011990. TPR-like_helical_dom.
PANTHERiPTHR14030. PTHR14030. 1 hit.
PfamiView protein in Pfam
PF08311. Mad3_BUB1_I. 1 hit.
PF00069. Pkinase. 1 hit.
SMARTiView protein in SMART
SM00777. Mad3_BUB1_I. 1 hit.
SM00220. S_TKc. 1 hit.
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiView protein in PROSITE
PS51489. BUB1_N. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.

Sequences (3)i

Sequence statusi: Complete.

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

Isoform 1 (identifier: O43683-1) [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
MDTPENVLQM LEAHMQSYKG NDPLGEWERY IQWVEENFPE NKEYLITLLE 
        60         70         80         90        100
HLMKEFLDKK KYHNDPRFIS YCLKFAEYNS DLHQFFEFLY NHGIGTLSSP 
       110        120        130        140        150
LYIAWAGHLE AQGELQHASA VLQRGIQNQA EPREFLQQQY RLFQTRLTET 
       160        170        180        190        200
HLPAQARTSE PLHNVQVLNQ MITSKSNPGN NMACISKNQG SELSGVISSA 
       210        220        230        240        250
CDKESNMERR VITISKSEYS VHSSLASKVD VEQVVMYCKE KLIRGESEFS 
       260        270        280        290        300
FEELRAQKYN QRRKHEQWVN EDRHYMKRKE ANAFEEQLLK QKMDELHKKL 
       310        320        330        340        350
HQVVETSHED LPASQERSEV NPARMGPSVG SQQELRAPCL PVTYQQTPVN 
       360        370        380        390        400
MEKNPREAPP VVPPLANAIS AALVSPATSQ SIAPPVPLKA QTVTDSMFAV 
       410        420        430        440        450
ASKDAGCVNK STHEFKPQSG AEIKEGCETH KVANTSSFHT TPNTSLGMVQ 
       460        470        480        490        500
ATPSKVQPSP TVHTKEALGF IMNMFQAPTL PDISDDKDEW QSLDQNEDAF 
       510        520        530        540        550
EAQFQKNVRS SGAWGVNKII SSLSSAFHVF EDGNKENYGL PQPKNKPTGA 
       560        570        580        590        600
RTFGERSVSR LPSKPKEEVP HAEEFLDDST VWGIRCNKTL APSPKSPGDF 
       610        620        630        640        650
TSAAQLASTP FHKLPVESVH ILEDKENVVA KQCTQATLDS CEENMVVPSR 
       660        670        680        690        700
DGKFSPIQEK SPKQALSSHM YSASLLRLSQ PAAGGVLTCE AELGVEACRL 
       710        720        730        740        750
TDTDAAIAED PPDAIAGLQA EWMQMSSLGT VDAPNFIVGN PWDDKLIFKL 
       760        770        780        790        800
LSGLSKPVSS YPNTFEWQCK LPAIKPKTEF QLGSKLVYVH HLLGEGAFAQ 
       810        820        830        840        850
VYEATQGDLN DAKNKQKFVL KVQKPANPWE FYIGTQLMER LKPSMQHMFM 
       860        870        880        890        900
KFYSAHLFQN GSVLVGELYS YGTLLNAINL YKNTPEKVMP QGLVISFAMR 
       910        920        930        940        950
MLYMIEQVHD CEIIHGDIKP DNFILGNGFL EQDDEDDLSA GLALIDLGQS 
       960        970        980        990       1000
IDMKLFPKGT IFTAKCETSG FQCVEMLSNK PWNYQIDYFG VAATVYCMLF 
      1010       1020       1030       1040       1050
GTYMKVKNEG GECKPEGLFR RLPHLDMWNE FFHVMLNIPD CHHLPSLDLL 
      1060       1070       1080 
RQKLKKVFQQ HYTNKIRALR NRLIVLLLEC KRSRK
Length:1,085
Mass (Da):122,375
Last modified:June 1, 1998 - v1
Checksum:i38AE5E1F88C53BDC
GO
Isoform 2 (identifier: O43683-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     876-932: Missing.

Note: No experimental confirmation available. Gene prediction based on EST data.
Show »
Length:1,028
Mass (Da):115,843
Checksum:i9D5F967383751D9C
GO
Isoform 3 (identifier: O43683-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     10-29: Missing.

Note: No experimental confirmation available. Gene prediction based on EST data.
Show »
Length:1,065
Mass (Da):120,002
Checksum:iE6BD9A1AA4ADAA71
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti70S → T in AAC06259 (PubMed:10366450).Curated1
Sequence conflicti276 – 279MKRK → IRHE in AAC39546 (PubMed:9441741).Curated4

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_04040020G → D1 PublicationCorresponds to variant dbSNP:rs35890336Ensembl.1
Natural variantiVAR_00884936E → D in colorectal cancer. 1 PublicationCorresponds to variant dbSNP:rs1801328Ensembl.1
Natural variantiVAR_015687259Y → C in pancreatic cancer; associated with N-265; failure to rescue the spindle-assembly checkpoint activity as a result of a deficient recruitment of MAD2L1 and BUBR1 to kinetochores; efficient restoration of chromosome congression; reduced binding to BUB3; rescue of the ability of kinetochores to bind SGO1 and CENPF but not MCAK. 2 Publications1
Natural variantiVAR_015688265H → N in pancreatic cancer; associated with C-259; complete rescue of the spindle-assembly checkpoint activity; increased rate of chromosome congression errors. 2 Publications1
Natural variantiVAR_008850492S → Y in colorectal cancer. 1 PublicationCorresponds to variant dbSNP:rs121909055Ensembl.1
Natural variantiVAR_040401534N → D1 PublicationCorresponds to variant dbSNP:rs36109304Ensembl.1
Natural variantiVAR_008851648P → R in colorectal cancer. 1 PublicationCorresponds to variant dbSNP:rs376649190Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_05476010 – 29Missing in isoform 3. CuratedAdd BLAST20
Alternative sequenceiVSP_054761876 – 932Missing in isoform 2. CuratedAdd BLAST57

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF046078 mRNA. Translation: AAC12729.1.
AF043294 mRNA. Translation: AAB97855.2.
AF053305 mRNA. Translation: AAC06259.1.
AF047471 mRNA. Translation: AAC03122.1.
AF139363
, AF139349, AF139350, AF139351, AF139352, AF139353, AF139354, AF139355, AF139356, AF139357, AF139358, AF139359, AF139360, AF139361, AF139362 Genomic DNA. Translation: AAD43675.1.
AC114776 Genomic DNA. Translation: AAY14706.1.
AC226101 Genomic DNA. No translation available.
CH471237 Genomic DNA. Translation: EAW50355.1.
BC028201 mRNA. Translation: AAH28201.1.
AF011387 mRNA. Translation: AAC39546.1.
CCDSiCCDS33273.1. [O43683-1]
CCDS62984.1. [O43683-3]
CCDS62985.1. [O43683-2]
RefSeqiNP_001265546.1. NM_001278617.1. [O43683-2]
NP_004327.1. NM_004336.4. [O43683-1]
UniGeneiHs.469649.

Genome annotation databases

EnsembliENST00000302759; ENSP00000302530; ENSG00000169679. [O43683-1]
ENST00000409311; ENSP00000386701; ENSG00000169679. [O43683-2]
ENST00000535254; ENSP00000441013; ENSG00000169679. [O43683-3]
GeneIDi699.
KEGGihsa:699.
UCSCiuc002tgc.5. human. [O43683-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

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.

Entry informationi

Entry nameiBUB1_HUMAN
AccessioniPrimary (citable) accession number: O43683
Secondary accession number(s): E9PC26
, F5GXI5, O43430, O43643, O60626, Q53QE4
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: June 1, 1998
Last modified: July 5, 2017
This is version 170 of the entry and version 1 of the sequence. See 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 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. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  7. SIMILARITY comments
    Index of protein domains and families