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

Anillin

Gene

ANLN

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

Functioni

Required for cytokinesis (PubMed:16040610). Essential for the structural integrity of the cleavage furrow and for completion of cleavage furrow ingression. May play a significant role in podocyte cell migration (PubMed:24676636).6 Publications

GO - Molecular functioni

  • actin binding Source: MGI
  • cadherin binding involved in cell-cell adhesion Source: BHF-UCL

GO - Biological processi

  • glomerular visceral epithelial cell migration Source: UniProtKB
  • hematopoietic progenitor cell differentiation Source: Ensembl
  • mitotic cytokinesis Source: MGI
  • mitotic nuclear division Source: UniProtKB-KW
  • regulation of exit from mitosis Source: ProtInc
  • septin ring assembly Source: ProtInc
Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, Mitosis

Keywords - Ligandi

Actin-binding

Enzyme and pathway databases

BioCyciZFISH:ENSG00000011426-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Anillin
Gene namesi
Name:ANLN
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 7

Organism-specific databases

HGNCiHGNC:14082. ANLN.

Subcellular locationi

  • Nucleus
  • Cytoplasmcytoskeleton
  • Cytoplasmcell cortex

  • Note: Mainly found in the nucleus during interphase. Colocalizes with cortical F-actin upon nuclear envelope breakdown in mitosis and subsequently concentrates in the area of the prospective contractile ring in anaphase. This pattern persists until telophase, when the protein becomes concentrated in the midbody.

GO - Cellular componenti

  • actin cytoskeleton Source: MGI
  • actomyosin contractile ring Source: MGI
  • cell-cell adherens junction Source: BHF-UCL
  • intracellular membrane-bounded organelle Source: HPA
  • nucleoplasm Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Nucleus

Pathology & Biotechi

Involvement in diseasei

Focal segmental glomerulosclerosis 8 (FSGS8)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA renal pathology defined by the presence of segmental sclerosis in glomeruli and resulting in proteinuria, reduced glomerular filtration rate and progressive decline in renal function. Renal insufficiency often progresses to end-stage renal disease, a highly morbid state requiring either dialysis therapy or kidney transplantation.
See also OMIM:616032
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_072418431R → C in FSGS8; results in decreased interaction with CD2AP. 1 PublicationCorresponds to variant rs587777741dbSNPEnsembl.1
Natural variantiVAR_072419618G → C in FSGS8. 1 Publication1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi32R → A: Abrogates interaction with CD2AP. 1 Publication1
Mutagenesisi41R → A: Abrogates ubiquitin-mediated proteolysis; when associated with A-44. 1 Publication1
Mutagenesisi44L → A: Abrogates ubiquitin-mediated proteolysis; when associated with A-41. 1 Publication1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNETi54443.
MalaCardsiANLN.
MIMi616032. phenotype.
OpenTargetsiENSG00000011426.
Orphaneti93213. Familial idiopathic steroid-resistant nephrotic syndrome with focal segmental hyalinosis.
PharmGKBiPA24809.

Polymorphism and mutation databases

BioMutaiANLN.
DMDMi90111962.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002279651 – 1124AnillinAdd BLAST1124

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineCombined sources1
Modified residuei54PhosphoserineCombined sources1
Modified residuei72PhosphoserineCombined sources1
Modified residuei97PhosphoserineBy similarity1
Modified residuei102PhosphoserineCombined sources1
Modified residuei172PhosphoserineCombined sources1
Modified residuei182PhosphoserineCombined sources1
Modified residuei194PhosphothreonineCombined sources1
Modified residuei225PhosphoserineCombined sources1
Modified residuei252PhosphoserineCombined sources1
Cross-linki254Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)Combined sources
Modified residuei261PhosphoserineBy similarity1
Modified residuei320PhosphothreonineCombined sources1
Modified residuei323PhosphoserineCombined sources1
Modified residuei339PhosphoserineCombined sources1
Modified residuei364PhosphothreonineCombined sources1
Modified residuei371N6-acetyllysineCombined sources1
Modified residuei397PhosphothreonineCombined sources1
Modified residuei401PhosphothreonineCombined sources1
Modified residuei417PhosphoserineCombined sources1
Modified residuei419PhosphoserineCombined sources1
Modified residuei449PhosphoserineCombined sources1
Modified residuei485PhosphoserineCombined sources1
Modified residuei518PhosphoserineCombined sources1
Modified residuei553PhosphoserineCombined sources1
Modified residuei561PhosphoserineCombined sources1
Modified residuei637PhosphoserineCombined sources1
Modified residuei642PhosphoserineCombined sources1
Modified residuei658PhosphoserineCombined sources1
Modified residuei661PhosphoserineCombined sources1
Modified residuei664PhosphoserineCombined sources1
Modified residuei671PhosphotyrosineBy similarity1
Modified residuei678PhosphoserineCombined sources1
Modified residuei688PhosphoserineCombined sources1
Modified residuei792PhosphoserineCombined sources1
Modified residuei927PhosphoserineCombined sources1

Post-translational modificationi

Phosphorylated during mitosis.2 Publications
Ubiquitinated, and this requires FZR1/CDH1.1 Publication

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ9NQW6.
MaxQBiQ9NQW6.
PaxDbiQ9NQW6.
PeptideAtlasiQ9NQW6.
PRIDEiQ9NQW6.

PTM databases

iPTMnetiQ9NQW6.
PhosphoSitePlusiQ9NQW6.

Expressioni

Tissue specificityi

Ubiquitously expressed. Present at highest levels in the brain, at high levels in the placenta and testis, at intermediate levels in the intestine, ovary, skeletal muscle and thymus and at lower levels in heart, kidney, liver, lung, pancreas, prostate and spleen. In the kidney, it is widely expressed in tubules, but sparsely expressed in the glomerulus (PubMed:24676636). Expression is significantly increased in renal biopsy specimens from idiopathic FSGS (PubMed:24676636). Overexpressed in many tumor types including breast, colorectal, endometrial, hepatic, kidney, lung, ovarian and pancreatic tumors.2 Publications

Developmental stagei

Expressed in fetal brain, heart, kidney, liver, lung, skeletal muscle, spleen and thymus. In dividing cells expression increases during S and G2 phases, peaks at mitosis and subsequently drops as cells enter G1 phase.4 Publications

Gene expression databases

BgeeiENSG00000011426.
CleanExiHS_ANLN.
ExpressionAtlasiQ9NQW6. baseline and differential.
GenevisibleiQ9NQW6. HS.

Organism-specific databases

HPAiCAB033902.
CAB062547.
CAB068175.
HPA005680.
HPA050556.

Interactioni

Subunit structurei

Interacts with F-actin. Interacts with CD2AP. May interact with RHOA. Interacts with FZR1/CDH1 during mitotic exit.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
MARCH10Q8NA823EBI-10312488,EBI-2341554

GO - Molecular functioni

  • actin binding Source: MGI
  • cadherin binding involved in cell-cell adhesion Source: BHF-UCL

Protein-protein interaction databases

BioGridi119959. 144 interactors.
IntActiQ9NQW6. 141 interactors.
MINTiMINT-3072308.
STRINGi9606.ENSP00000265748.

Structurei

Secondary structure

11124
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi716 – 742Combined sources27
Helixi747 – 749Combined sources3
Turni750 – 752Combined sources3
Helixi754 – 781Combined sources28
Beta strandi802 – 813Combined sources12
Helixi815 – 823Combined sources9
Beta strandi827 – 845Combined sources19
Turni851 – 853Combined sources3
Beta strandi854 – 856Combined sources3
Beta strandi859 – 861Combined sources3
Beta strandi866 – 871Combined sources6
Beta strandi877 – 887Combined sources11
Beta strandi940 – 947Combined sources8
Helixi949 – 951Combined sources3
Beta strandi956 – 958Combined sources3
Beta strandi970 – 979Combined sources10
Beta strandi986 – 996Combined sources11
Beta strandi999 – 1010Combined sources12
Beta strandi1013 – 1019Combined sources7
Helixi1020 – 1023Combined sources4
Beta strandi1029 – 1033Combined sources5
Helixi1034 – 1036Combined sources3
Beta strandi1039 – 1041Combined sources3
Turni1047 – 1049Combined sources3
Beta strandi1055 – 1063Combined sources9
Beta strandi1072 – 1077Combined sources6
Beta strandi1080 – 1088Combined sources9
Helixi1092 – 1110Combined sources19

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2Y7BX-ray1.90A980-1113[»]
4XH3X-ray2.10A712-1124[»]
4XOIX-ray2.09B/D712-981[»]
ProteinModelPortaliQ9NQW6.
SMRiQ9NQW6.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini983 – 1107PHPROSITE-ProRule annotationAdd BLAST125

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 230Nuclear localizationAdd BLAST230
Regioni1 – 155Interaction with CD2AP1 PublicationAdd BLAST155
Regioni1 – 45Required for ubiquitinationAdd BLAST45
Regioni231 – 676Interaction with F-actinAdd BLAST446
Regioni730 – 1124Localization to the cleavage furrowAdd BLAST395

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili569 – 604Sequence analysisAdd BLAST36

Sequence similaritiesi

Contains 1 PH domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG3640. Eukaryota.
ENOG4110J5Z. LUCA.
GeneTreeiENSGT00390000008749.
HOGENOMiHOG000033950.
HOVERGENiHBG059477.
InParanoidiQ9NQW6.
KOiK18621.
OMAiHSKESPA.
OrthoDBiEOG091G01HH.
PhylomeDBiQ9NQW6.
TreeFamiTF106494.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
InterProiIPR012966. AHD.
IPR031970. Anillin_N.
IPR011993. PH_dom-like.
IPR001849. PH_domain.
[Graphical view]
PfamiPF08174. Anillin. 1 hit.
PF16018. Anillin_N. 2 hits.
PF00169. PH. 1 hit.
[Graphical view]
SMARTiSM00233. PH. 1 hit.
[Graphical view]
SUPFAMiSSF50729. SSF50729. 1 hit.
PROSITEiPS50003. PH_DOMAIN. 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: Q9NQW6-1) [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
MDPFTEKLLE RTRARRENLQ RKMAERPTAA PRSMTHAKRA RQPLSEASNQ
60 70 80 90 100
QPLSGGEEKS CTKPSPSKKR CSDNTEVEVS NLENKQPVES TSAKSCSPSP
110 120 130 140 150
VSPQVQPQAA DTISDSVAVP ASLLGMRRGL NSRLEATAAS SVKTRMQKLA
160 170 180 190 200
EQRRRWDNDD MTDDIPESSL FSPMPSEEKA ASPPRPLLSN ASATPVGRRG
210 220 230 240 250
RLANLAATIC SWEDDVNHSF AKQNSVQEQP GTACLSKFSS ASGASARINS
260 270 280 290 300
SSVKQEATFC SQRDGDASLN KALSSSADDA SLVNASISSS VKATSPVKST
310 320 330 340 350
TSITDAKSCE GQNPELLPKT PISPLKTGVS KPIVKSTLSQ TVPSKGELSR
360 370 380 390 400
EICLQSQSKD KSTTPGGTGI KPFLERFGER CQEHSKESPA RSTPHRTPII
410 420 430 440 450
TPNTKAIQER LFKQDTSSST THLAQQLKQE RQKELACLRG RFDKGNIWSA
460 470 480 490 500
EKGGNSKSKQ LETKQETHCQ STPLKKHQGV SKTQSLPVTE KVTENQIPAK
510 520 530 540 550
NSSTEPKGFT ECEMTKSSPL KITLFLEEDK SLKVTSDPKV EQKIEVIREI
560 570 580 590 600
EMSVDDDDIN SSKVINDLFS DVLEEGELDM EKSQEEMDQA LAESSEEQED
610 620 630 640 650
ALNISSMSLL APLAQTVGVV SPESLVSTPR LELKDTSRSD ESPKPGKFQR
660 670 680 690 700
TRVPRAESGD SLGSEDRDLL YSIDAYRSQR FKETERPSIK QVIVRKEDVT
710 720 730 740 750
SKLDEKNNAF PCQVNIKQKM QELNNEINMQ QTVIYQASQA LNCCVDEEHG
760 770 780 790 800
KGSLEEAEAE RLLLIATGKR TLLIDELNKL KNEGPQRKNK ASPQSEFMPS
810 820 830 840 850
KGSVTLSEIR LPLKADFVCS TVQKPDAANY YYLIILKAGA ENMVATPLAS
860 870 880 890 900
TSNSLNGDAL TFTTTFTLQD VSNDFEINIE VYSLVQKKDP SGLDKKKKTS
910 920 930 940 950
KSKAITPKRL LTSITTKSNI HSSVMASPGG LSAVRTSNFA LVGSYTLSLS
960 970 980 990 1000
SVGNTKFVLD KVPFLSSLEG HIYLKIKCQV NSSVEERGFL TIFEDVSGFG
1010 1020 1030 1040 1050
AWHRRWCVLS GNCISYWTYP DDEKRKNPIG RINLANCTSR QIEPANREFC
1060 1070 1080 1090 1100
ARRNTFELIT VRPQREDDRE TLVSQCRDTL CVTKNWLSAD TKEERDLWMQ
1110 1120
KLNQVLVDIR LWQPDACYKP IGKP
Length:1,124
Mass (Da):124,199
Last modified:March 21, 2006 - v2
Checksum:i79A8CC25C950DB2D
GO
Isoform 2 (identifier: Q9NQW6-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     508-544: Missing.

Show »
Length:1,087
Mass (Da):120,016
Checksum:i5B45A0FFA334747F
GO

Sequence cautioni

The sequence AAH34692 differs from that shown. Reason: Erroneous initiation.Curated
The sequence BAA91710 differs from that shown. Reason: Erroneous initiation.Curated
The sequence BAA91711 differs from that shown. Reason: Erroneous initiation.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti53L → F in AAF75796 (PubMed:10931866).Curated1
Sequence conflicti62T → S in AAF75796 (PubMed:10931866).Curated1
Sequence conflicti294T → TS (PubMed:10931866).Curated1
Sequence conflicti294T → TS (PubMed:17974005).Curated1
Sequence conflicti410R → K in AAH70066 (PubMed:15489334).Curated1
Sequence conflicti625L → S in BAA91711 (PubMed:14702039).Curated1
Sequence conflicti1035A → V in CAI56788 (PubMed:17974005).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_02566165S → W.Corresponds to variant rs3735400dbSNPEnsembl.1
Natural variantiVAR_025662185R → K.Combined sources1 PublicationCorresponds to variant rs197367dbSNPEnsembl.1
Natural variantiVAR_072418431R → C in FSGS8; results in decreased interaction with CD2AP. 1 PublicationCorresponds to variant rs587777741dbSNPEnsembl.1
Natural variantiVAR_072419618G → C in FSGS8. 1 Publication1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_017617508 – 544Missing in isoform 2. 2 PublicationsAdd BLAST37

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF273437 mRNA. Translation: AAF75796.1.
BC034692 mRNA. Translation: AAH34692.1. Different initiation.
BC070066 mRNA. Translation: AAH70066.1.
CR936650 mRNA. Translation: CAI56788.1.
AK001468 mRNA. Translation: BAA91710.1. Different initiation.
AK001472 mRNA. Translation: BAA91711.1. Different initiation.
AK023208 mRNA. Translation: BAB14463.1.
CCDSiCCDS5447.1. [Q9NQW6-1]
CCDS64628.1. [Q9NQW6-2]
RefSeqiNP_001271230.1. NM_001284301.2. [Q9NQW6-2]
NP_001271231.1. NM_001284302.2.
NP_061155.2. NM_018685.4. [Q9NQW6-1]
UniGeneiHs.62180.

Genome annotation databases

EnsembliENST00000265748; ENSP00000265748; ENSG00000011426. [Q9NQW6-1]
ENST00000396068; ENSP00000379380; ENSG00000011426. [Q9NQW6-2]
GeneIDi54443.
KEGGihsa:54443.
UCSCiuc003tff.4. human. [Q9NQW6-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF273437 mRNA. Translation: AAF75796.1.
BC034692 mRNA. Translation: AAH34692.1. Different initiation.
BC070066 mRNA. Translation: AAH70066.1.
CR936650 mRNA. Translation: CAI56788.1.
AK001468 mRNA. Translation: BAA91710.1. Different initiation.
AK001472 mRNA. Translation: BAA91711.1. Different initiation.
AK023208 mRNA. Translation: BAB14463.1.
CCDSiCCDS5447.1. [Q9NQW6-1]
CCDS64628.1. [Q9NQW6-2]
RefSeqiNP_001271230.1. NM_001284301.2. [Q9NQW6-2]
NP_001271231.1. NM_001284302.2.
NP_061155.2. NM_018685.4. [Q9NQW6-1]
UniGeneiHs.62180.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2Y7BX-ray1.90A980-1113[»]
4XH3X-ray2.10A712-1124[»]
4XOIX-ray2.09B/D712-981[»]
ProteinModelPortaliQ9NQW6.
SMRiQ9NQW6.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi119959. 144 interactors.
IntActiQ9NQW6. 141 interactors.
MINTiMINT-3072308.
STRINGi9606.ENSP00000265748.

PTM databases

iPTMnetiQ9NQW6.
PhosphoSitePlusiQ9NQW6.

Polymorphism and mutation databases

BioMutaiANLN.
DMDMi90111962.

Proteomic databases

EPDiQ9NQW6.
MaxQBiQ9NQW6.
PaxDbiQ9NQW6.
PeptideAtlasiQ9NQW6.
PRIDEiQ9NQW6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000265748; ENSP00000265748; ENSG00000011426. [Q9NQW6-1]
ENST00000396068; ENSP00000379380; ENSG00000011426. [Q9NQW6-2]
GeneIDi54443.
KEGGihsa:54443.
UCSCiuc003tff.4. human. [Q9NQW6-1]

Organism-specific databases

CTDi54443.
DisGeNETi54443.
GeneCardsiANLN.
H-InvDBHIX0006603.
HGNCiHGNC:14082. ANLN.
HPAiCAB033902.
CAB062547.
CAB068175.
HPA005680.
HPA050556.
MalaCardsiANLN.
MIMi616027. gene.
616032. phenotype.
neXtProtiNX_Q9NQW6.
OpenTargetsiENSG00000011426.
Orphaneti93213. Familial idiopathic steroid-resistant nephrotic syndrome with focal segmental hyalinosis.
PharmGKBiPA24809.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3640. Eukaryota.
ENOG4110J5Z. LUCA.
GeneTreeiENSGT00390000008749.
HOGENOMiHOG000033950.
HOVERGENiHBG059477.
InParanoidiQ9NQW6.
KOiK18621.
OMAiHSKESPA.
OrthoDBiEOG091G01HH.
PhylomeDBiQ9NQW6.
TreeFamiTF106494.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000011426-MONOMER.

Miscellaneous databases

ChiTaRSiANLN. human.
GeneWikiiANLN.
GenomeRNAii54443.
PROiQ9NQW6.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000011426.
CleanExiHS_ANLN.
ExpressionAtlasiQ9NQW6. baseline and differential.
GenevisibleiQ9NQW6. HS.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
InterProiIPR012966. AHD.
IPR031970. Anillin_N.
IPR011993. PH_dom-like.
IPR001849. PH_domain.
[Graphical view]
PfamiPF08174. Anillin. 1 hit.
PF16018. Anillin_N. 2 hits.
PF00169. PH. 1 hit.
[Graphical view]
SMARTiSM00233. PH. 1 hit.
[Graphical view]
SUPFAMiSSF50729. SSF50729. 1 hit.
PROSITEiPS50003. PH_DOMAIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiANLN_HUMAN
AccessioniPrimary (citable) accession number: Q9NQW6
Secondary accession number(s): Q5CZ78
, Q6NSK5, Q9H8Y4, Q9NVN9, Q9NVP0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 21, 2006
Last sequence update: March 21, 2006
Last modified: November 2, 2016
This is version 128 of the entry and version 2 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 7
    Human chromosome 7: 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.