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Protein

Histone-lysine N-methyltransferase PRDM9

Gene

PRDM9

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

Functioni

Histone methyltransferase that specifically trimethylates 'Lys-4' of histone H3 during meiotic prophase and is essential for proper meiotic progression. Does not have the ability to mono- and dimethylate 'Lys-4' of histone H3. H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation. Plays a central role in the transcriptional activation of genes during early meiotic prophase (By similarity).By similarity

Catalytic activityi

S-adenosyl-L-methionine + L-lysine-[histone] = S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone].

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri388 – 41124C2H2-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri524 – 54623C2H2-type 2; degeneratePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri552 – 57423C2H2-type 3PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri580 – 60223C2H2-type 4PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri608 – 63023C2H2-type 5PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri636 – 65823C2H2-type 6PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri664 – 68623C2H2-type 7PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri692 – 71423C2H2-type 8PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri720 – 74223C2H2-type 9PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri748 – 77023C2H2-type 10PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri776 – 79823C2H2-type 11PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri804 – 82623C2H2-type 12PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri832 – 85423C2H2-type 13PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri860 – 88223C2H2-type 14PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. histone methyltransferase activity (H3-K4 specific) Source: Ensembl
  2. metal ion binding Source: UniProtKB-KW
  3. recombination hotspot binding Source: Ensembl
  4. sequence-specific DNA binding Source: Ensembl

GO - Biological processi

  1. chromatin organization Source: Reactome
  2. meiotic gene conversion Source: MGI
  3. positive regulation of reciprocal meiotic recombination Source: MGI
  4. positive regulation of transcription from RNA polymerase II promoter Source: Ensembl
  5. spermatogenesis Source: Ensembl
  6. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator, Chromatin regulator, Methyltransferase, Transferase

Keywords - Biological processi

Meiosis, Transcription, Transcription regulation

Keywords - Ligandi

Metal-binding, S-adenosyl-L-methionine, Zinc

Enzyme and pathway databases

ReactomeiREACT_268728. PKMTs methylate histone lysines.
REACT_27271. Meiotic recombination.

Names & Taxonomyi

Protein namesi
Recommended name:
Histone-lysine N-methyltransferase PRDM9 (EC:2.1.1.43)
Alternative name(s):
PR domain zinc finger protein 9
PR domain-containing protein 9
Gene namesi
Name:PRDM9
Synonyms:PFM6
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 5

Organism-specific databases

HGNCiHGNC:13994. PRDM9.

Subcellular locationi

Nucleus By similarity. Chromosome By similarity

GO - Cellular componenti

  1. chromosome Source: UniProtKB-SubCell
  2. nucleoplasm Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA33721.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 894894Histone-lysine N-methyltransferase PRDM9PRO_0000047766Add
BLAST

Proteomic databases

PaxDbiQ9NQV7.
PRIDEiQ9NQV7.

PTM databases

PhosphoSiteiQ9NQV7.

Expressioni

Gene expression databases

BgeeiQ9NQV7.
CleanExiHS_PRDM9.
ExpressionAtlasiQ9NQV7. baseline.
GenevestigatoriQ9NQV7.

Organism-specific databases

HPAiHPA059555.

Interactioni

Protein-protein interaction databases

STRINGi9606.ENSP00000296682.

Structurei

Secondary structure

1
894
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi199 – 2013Combined sources
Beta strandi203 – 2053Combined sources
Turni206 – 2094Combined sources
Beta strandi210 – 2167Combined sources
Turni217 – 2193Combined sources
Helixi237 – 2404Combined sources
Beta strandi246 – 2505Combined sources
Beta strandi258 – 2625Combined sources
Beta strandi278 – 2814Combined sources
Helixi284 – 2863Combined sources
Beta strandi289 – 29810Combined sources
Beta strandi301 – 3066Combined sources
Turni310 – 3123Combined sources
Helixi315 – 3184Combined sources
Turni325 – 3273Combined sources
Beta strandi330 – 3356Combined sources
Beta strandi338 – 3458Combined sources
Beta strandi354 – 3563Combined sources
Helixi362 – 3676Combined sources
Turni368 – 3703Combined sources
Helixi373 – 3775Combined sources
Beta strandi391 – 3944Combined sources
Beta strandi396 – 3994Combined sources
Helixi400 – 41011Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4IJDX-ray2.15A/B195-415[»]
ProteinModelPortaliQ9NQV7.
SMRiQ9NQV7. Positions 195-411, 528-892.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini23 – 8664KRAB-relatedPROSITE-ProRule annotationAdd
BLAST
Domaini244 – 358115SETPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the class V-like SAM-binding methyltransferase superfamily.PROSITE-ProRule annotation
Contains 14 C2H2-type zinc fingers.PROSITE-ProRule annotation
Contains 1 KRAB-related domain.PROSITE-ProRule annotation
Contains 1 SET domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri388 – 41124C2H2-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri524 – 54623C2H2-type 2; degeneratePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri552 – 57423C2H2-type 3PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri580 – 60223C2H2-type 4PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri608 – 63023C2H2-type 5PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri636 – 65823C2H2-type 6PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri664 – 68623C2H2-type 7PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri692 – 71423C2H2-type 8PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri720 – 74223C2H2-type 9PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri748 – 77023C2H2-type 10PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri776 – 79823C2H2-type 11PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri804 – 82623C2H2-type 12PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri832 – 85423C2H2-type 13PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri860 – 88223C2H2-type 14PROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiCOG5048.
GeneTreeiENSGT00530000063157.
HOGENOMiHOG000234617.
HOVERGENiHBG108291.
InParanoidiQ9NQV7.
OMAiRECGWGF.
OrthoDBiEOG7KSX7Q.
PhylomeDBiQ9NQV7.
TreeFamiTF338096.

Family and domain databases

Gene3Di3.30.160.60. 13 hits.
InterProiIPR001909. Krueppel-associated_box.
IPR003655. Krueppel-associated_box-rel.
IPR001214. SET_dom.
IPR019041. SSXRD_motif.
IPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR013087. Znf_C2H2/integrase_DNA-bd.
[Graphical view]
PfamiPF01352. KRAB. 1 hit.
PF09514. SSXRD. 1 hit.
[Graphical view]
SMARTiSM00349. KRAB. 1 hit.
SM00317. SET. 1 hit.
SM00355. ZnF_C2H2. 14 hits.
[Graphical view]
SUPFAMiSSF109640. SSF109640. 1 hit.
PROSITEiPS50806. KRAB_RELATED. 1 hit.
PS50280. SET. 1 hit.
PS00028. ZINC_FINGER_C2H2_1. 13 hits.
PS50157. ZINC_FINGER_C2H2_2. 14 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9NQV7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSPEKSQEES PEEDTERTER KPMVKDAFKD ISIYFTKEEW AEMGDWEKTR
60 70 80 90 100
YRNVKRNYNA LITIGLRATR PAFMCHRRQA IKLQVDDTED SDEEWTPRQQ
110 120 130 140 150
VKPPWMALRV EQRKHQKGMP KASFSNESSL KELSRTANLL NASGSEQAQK
160 170 180 190 200
PVSPSGEAST SGQHSRLKLE LRKKETERKM YSLRERKGHA YKEVSEPQDD
210 220 230 240 250
DYLYCEMCQN FFIDSCAAHG PPTFVKDSAV DKGHPNRSAL SLPPGLRIGP
260 270 280 290 300
SGIPQAGLGV WNEASDLPLG LHFGPYEGRI TEDEEAANNG YSWLITKGRN
310 320 330 340 350
CYEYVDGKDK SWANWMRYVN CARDDEEQNL VAFQYHRQIF YRTCRVIRPG
360 370 380 390 400
CELLVWYGDE YGQELGIKWG SKWKKELMAG REPKPEIHPC PSCCLAFSSQ
410 420 430 440 450
KFLSQHVERN HSSQNFPGPS ARKLLQPENP CPGDQNQEQQ YPDPHSRNDK
460 470 480 490 500
TKGQEIKERS KLLNKRTWQR EISRAFSSPP KGQMGSCRVG KRIMEEESRT
510 520 530 540 550
GQKVNPGNTG KLFVGVGISR IAKVKYGECG QGFSVKSDVI THQRTHTGEK
560 570 580 590 600
LYVCRECGRG FSWKSHLLIH QRIHTGEKPY VCRECGRGFS WQSVLLTHQR
610 620 630 640 650
THTGEKPYVC RECGRGFSRQ SVLLTHQRRH TGEKPYVCRE CGRGFSRQSV
660 670 680 690 700
LLTHQRRHTG EKPYVCRECG RGFSWQSVLL THQRTHTGEK PYVCRECGRG
710 720 730 740 750
FSWQSVLLTH QRTHTGEKPY VCRECGRGFS NKSHLLRHQR THTGEKPYVC
760 770 780 790 800
RECGRGFRDK SHLLRHQRTH TGEKPYVCRE CGRGFRDKSN LLSHQRTHTG
810 820 830 840 850
EKPYVCRECG RGFSNKSHLL RHQRTHTGEK PYVCRECGRG FRNKSHLLRH
860 870 880 890
QRTHTGEKPY VCRECGRGFS DRSSLCYHQR THTGEKPYVC REDE
Length:894
Mass (Da):103,376
Last modified:November 4, 2008 - v2
Checksum:iDE53094C32EFF83B
GO

Sequence cautioni

The sequence AAF87242.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti295 – 2951I → VRRACHF in AAF87242 (PubMed:10668202).Curated
Sequence conflicti377 – 3815Missing in AAF87242 (PubMed:10668202).Curated
Sequence conflicti681 – 6811T → S in BAG63234 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti335 – 3351Y → H Common polymorphism; may be a genetic risk for patients with azoospermia caused by meiotic arrest. 1 Publication
VAR_054417

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ388610 mRNA. Translation: ABD47939.1.
AK301776 mRNA. Translation: BAG63234.1.
AC025451 Genomic DNA. No translation available.
AF275816 mRNA. Translation: AAF87242.1. Different initiation.
CCDSiCCDS43307.1.
RefSeqiNP_064612.2. NM_020227.2.
UniGeneiHs.283096.

Genome annotation databases

EnsembliENST00000296682; ENSP00000296682; ENSG00000164256.
GeneIDi56979.
KEGGihsa:56979.
UCSCiuc003jgo.3. human.

Polymorphism databases

DMDMi212276459.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ388610 mRNA. Translation: ABD47939.1.
AK301776 mRNA. Translation: BAG63234.1.
AC025451 Genomic DNA. No translation available.
AF275816 mRNA. Translation: AAF87242.1. Different initiation.
CCDSiCCDS43307.1.
RefSeqiNP_064612.2. NM_020227.2.
UniGeneiHs.283096.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4IJDX-ray2.15A/B195-415[»]
ProteinModelPortaliQ9NQV7.
SMRiQ9NQV7. Positions 195-411, 528-892.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9606.ENSP00000296682.

PTM databases

PhosphoSiteiQ9NQV7.

Polymorphism databases

DMDMi212276459.

Proteomic databases

PaxDbiQ9NQV7.
PRIDEiQ9NQV7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000296682; ENSP00000296682; ENSG00000164256.
GeneIDi56979.
KEGGihsa:56979.
UCSCiuc003jgo.3. human.

Organism-specific databases

CTDi56979.
GeneCardsiGC05P023558.
HGNCiHGNC:13994. PRDM9.
HPAiHPA059555.
MIMi609760. gene.
neXtProtiNX_Q9NQV7.
PharmGKBiPA33721.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5048.
GeneTreeiENSGT00530000063157.
HOGENOMiHOG000234617.
HOVERGENiHBG108291.
InParanoidiQ9NQV7.
OMAiRECGWGF.
OrthoDBiEOG7KSX7Q.
PhylomeDBiQ9NQV7.
TreeFamiTF338096.

Enzyme and pathway databases

ReactomeiREACT_268728. PKMTs methylate histone lysines.
REACT_27271. Meiotic recombination.

Miscellaneous databases

GeneWikiiPRDM9.
GenomeRNAii56979.
NextBioi62639.
PROiQ9NQV7.
SOURCEiSearch...

Gene expression databases

BgeeiQ9NQV7.
CleanExiHS_PRDM9.
ExpressionAtlasiQ9NQV7. baseline.
GenevestigatoriQ9NQV7.

Family and domain databases

Gene3Di3.30.160.60. 13 hits.
InterProiIPR001909. Krueppel-associated_box.
IPR003655. Krueppel-associated_box-rel.
IPR001214. SET_dom.
IPR019041. SSXRD_motif.
IPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR013087. Znf_C2H2/integrase_DNA-bd.
[Graphical view]
PfamiPF01352. KRAB. 1 hit.
PF09514. SSXRD. 1 hit.
[Graphical view]
SMARTiSM00349. KRAB. 1 hit.
SM00317. SET. 1 hit.
SM00355. ZnF_C2H2. 14 hits.
[Graphical view]
SUPFAMiSSF109640. SSF109640. 1 hit.
PROSITEiPS50806. KRAB_RELATED. 1 hit.
PS50280. SET. 1 hit.
PS00028. ZINC_FINGER_C2H2_1. 13 hits.
PS50157. ZINC_FINGER_C2H2_2. 14 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and characterization of PR domain-containing 9 (PRDM9)."
    Ying J., Wong A.H.Y., Li H., Wang Y., Tao Q.
    Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Testis.
  3. "The DNA sequence and comparative analysis of human chromosome 5."
    Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.
    , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
    Nature 431:268-274(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "The yin-yang of PR-domain family genes in tumorigenesis."
    Jiang G.L., Huang S.
    Histol. Histopathol. 15:109-117(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 205-894.
  5. "Two single nucleotide polymorphisms in PRDM9 (MEISETZ) gene may be a genetic risk factor for Japanese patients with azoospermia by meiotic arrest."
    Miyamoto T., Koh E., Sakugawa N., Sato H., Hayashi H., Namiki M., Sengoku K.
    J. Assist. Reprod. Genet. 25:553-557(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT HIS-335.

Entry informationi

Entry nameiPRDM9_HUMAN
AccessioniPrimary (citable) accession number: Q9NQV7
Secondary accession number(s): B4DX22, Q27Q50
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 16, 2001
Last sequence update: November 4, 2008
Last modified: April 1, 2015
This is version 122 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 5
    Human chromosome 5: 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

External Data

Dasty 3

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 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.