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Protein

Centromere protein T

Gene

CENPT

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

Functioni

Component of the CENPA-NAC (nucleosome-associated) complex, a complex that plays a central role in assembly of kinetochore proteins, mitotic progression and chromosome segregation. The CENPA-NAC complex recruits the CENPA-CAD (nucleosome distal) complex and may be involved in incorporation of newly synthesized CENPA into centromeres. Part of a nucleosome-associated complex that binds specifically to histone H3-containing nucleosomes at the centromere, as opposed to nucleosomes containing CENPA. Component of the heterotetrameric CENP-T-W-S-X complex that binds and supercoils DNA, and plays an important role in kinetochore assembly. CENPT has a fundamental role in kinetochore assembly and function. It is one of the inner kinetochore proteins, with most further proteins binding downstream. Required for normal chromosome organization and normal progress through mitosis.3 Publications

GO - Molecular functioni

  1. DNA binding Source: UniProtKB-KW

GO - Biological processi

  1. cell division Source: UniProtKB-KW
  2. CENP-A containing nucleosome assembly Source: Reactome
  3. chromosome organization Source: UniProtKB
  4. chromosome segregation Source: UniProtKB
  5. kinetochore assembly Source: UniProtKB
  6. mitotic cell cycle Source: UniProtKB
  7. mitotic nuclear division Source: UniProtKB-KW
  8. nucleosome assembly Source: Reactome
Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, Mitosis

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiREACT_150425. Resolution of Sister Chromatid Cohesion.
REACT_150471. Separation of Sister Chromatids.
REACT_682. Mitotic Prometaphase.

Names & Taxonomyi

Protein namesi
Recommended name:
Centromere protein T
Short name:
CENP-T
Alternative name(s):
Interphase centromere complex protein 22
Gene namesi
Name:CENPT
Synonyms:C16orf56, ICEN22
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 16

Organism-specific databases

HGNCiHGNC:25787. CENPT.

Subcellular locationi

Nucleus. Chromosomecentromerekinetochore
Note: Constitutively localizes to centromeres throughout the cell cycle, and to kinetochores during mitosis. Localizes to the inner kinetochore, and may connect it to the outer kinetochore via its N-terminus.

GO - Cellular componenti

  1. chromosome, centromeric region Source: UniProtKB
  2. condensed chromosome kinetochore Source: UniProtKB-SubCell
  3. cytosol Source: Reactome
  4. kinetochore Source: UniProtKB
  5. nucleoplasm Source: Reactome
  6. nucleus Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Centromere, Chromosome, Kinetochore, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA142672263.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 561561Centromere protein TPRO_0000249514Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei47 – 471Phosphoserine2 Publications
Modified residuei85 – 851Phosphothreonine1 Publication
Modified residuei373 – 3731Phosphoserine1 Publication
Modified residuei385 – 3851Phosphoserine1 Publication
Modified residuei386 – 3861Phosphoserine1 Publication
Modified residuei397 – 3971Phosphoserine3 Publications

Post-translational modificationi

Dynamically phosphorylated at Ser-47 and probably also other sites during the cell cycle. Phosphorylated at Ser-47 during G2 phase, metaphase and anaphase, but not during telophase or G1 phase.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ96BT3.
PaxDbiQ96BT3.
PRIDEiQ96BT3.

PTM databases

PhosphoSiteiQ96BT3.

Expressioni

Gene expression databases

BgeeiQ96BT3.
CleanExiHS_CENPT.
ExpressionAtlasiQ96BT3. baseline and differential.
GenevestigatoriQ96BT3.

Organism-specific databases

HPAiHPA058036.

Interactioni

Subunit structurei

Component of the CENPA-NAC complex, at least composed of CENPA, CENPC, CENPH, CENPM, CENPN, CENPT and CENPU. The CENPA-NAC complex interacts with the CENPA-CAD complex, composed of CENPI, CENPK, CENPL, CENPO, CENPP, CENPQ, CENPR and CENPS. Part of a centromere complex consisting of CENPA, CENPT and CENPW. Part of a centromere complex consisting of histone H3, CENPT and CENPW. Interacts (via N-terminus) with the NDC80 complex (Probable). Component of a heterotetrameric CENP-T-W-S-X complex composed of APITD1/CENPS, STRA13/CENPX, CENPT and CENPW. Interacts directly with CENPW. Binds DNA.Curated7 Publications

Protein-protein interaction databases

BioGridi123143. 9 interactions.
IntActiQ96BT3. 6 interactions.
MINTiMINT-1376718.
STRINGi9606.ENSP00000219172.

Structurei

3D structure databases

ProteinModelPortaliQ96BT3.
SMRiQ96BT3. Positions 465-551.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni93 – 421329Flexible stalk domainBy similarityAdd
BLAST

Domaini

The largest part of the sequence forms an elongated and flexible stalk structure that is connected to a C-terminal globular domain with a histone-type fold.By similarity

Sequence similaritiesi

Belongs to the CENPT family.Curated

Phylogenomic databases

eggNOGiNOG26624.
GeneTreeiENSGT00390000003044.
HOGENOMiHOG000111545.
HOVERGENiHBG081089.
InParanoidiQ96BT3.
KOiK11512.
OMAiFSFYAKM.
OrthoDBiEOG7TQV2Z.
PhylomeDBiQ96BT3.
TreeFamiTF332946.

Family and domain databases

Gene3Di1.10.20.10. 1 hit.
InterProiIPR028255. CENP-T.
IPR009072. Histone-fold.
[Graphical view]
PANTHERiPTHR14857. PTHR14857. 1 hit.
SUPFAMiSSF47113. SSF47113. 1 hit.

Sequences (3)i

Sequence statusi: Complete.

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

Isoform 1 (identifier: Q96BT3-1) [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
MADHNPDSDS TPRTLLRRVL DTADPRTPRR PRSARAGARR ALLETASPRK
60 70 80 90 100
LSGQTRTIAR GRSHGARSVG RSAHIQASGH LEEQTPRTLL KNILLTAPES
110 120 130 140 150
SILMPESVVK PVPAPQAVQP SRQESSCGSL ELQLPELEPP TTLAPGLLAP
160 170 180 190 200
GRRKQRLRLS VFQQGVDQGL SLSQEPQGNA DASSLTRSLN LTFATPLQPQ
210 220 230 240 250
SVQRPGLARR PPARRAVDVG AFLRDLRDTS LAPPNIVLED TQPFSQPMVG
260 270 280 290 300
SPNVYHSLPC TPHTGAEDAE QAAGRKTQSS GPGLQKNSPG KPAQFLAGEA
310 320 330 340 350
EEVNAFALGF LSTSSGVSGE DEVEPLHDGV EEAEKKMEEE GVSVSEMEAT
360 370 380 390 400
GAQGPSRVEE AEGHTEVTEA EGSQGTAEAD GPGASSGDED ASGRAASPES
410 420 430 440 450
ASSTPESLQA RRHHQFLEPA PAPGAAVLSS EPAEPLLVRH PPRPRTTGPR
460 470 480 490 500
PRQDPHKAGL SHYVKLFSFY AKMPMERKAL EMVEKCLDKY FQHLCDDLEV
510 520 530 540 550
FAAHAGRKTV KPEDLELLMR RQGLVTDQVS LHVLVERHLP LEYRQLLIPC
560
AYSGNSVFPA Q
Length:561
Mass (Da):60,423
Last modified:March 1, 2004 - v2
Checksum:i295848C52AAF7DF1
GO
Isoform 2 (identifier: Q96BT3-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     289-299: PGKPAQFLAGE → ECVALVAWSQI
     300-561: Missing.

Note: No experimental confirmation available.

Show »
Length:299
Mass (Da):32,170
Checksum:i437895CBF0AD00DC
GO
Isoform 3 (identifier: Q96BT3-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     68-151: SVGRSAHIQA...TLAPGLLAPG → VSTQPTDPKG...NCPRIFHPDA
     152-561: Missing.

Note: No experimental confirmation available.

Show »
Length:151
Mass (Da):16,434
Checksum:i4A936224C3E78049
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti115 – 1151P → L.
Corresponds to variant rs12102580 [ dbSNP | Ensembl ].
VAR_027421

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei68 – 15184SVGRS…LLAPG → VSTQPTDPKGPWLPRGGGLR SSSALEPTLRKSQGRRTDWL LGASPIVCWQIGPYSGQWAL GGTDTSDAAEEHPTNCPRIF HPDA in isoform 3. 1 PublicationVSP_020455Add
BLAST
Alternative sequencei152 – 561410Missing in isoform 3. 1 PublicationVSP_020456Add
BLAST
Alternative sequencei289 – 29911PGKPAQFLAGE → ECVALVAWSQI in isoform 2. 1 PublicationVSP_020457Add
BLAST
Alternative sequencei300 – 561262Missing in isoform 2. 1 PublicationVSP_020458Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK023173 mRNA. Translation: BAB14445.1.
AK055237 mRNA. Translation: BAB70884.1.
BC007642 mRNA. Translation: AAH07642.1.
BC007864 mRNA. Translation: AAH07864.2.
BC015202 mRNA. Translation: AAH15202.2.
CCDSiCCDS42182.1. [Q96BT3-1]
RefSeqiNP_079358.3. NM_025082.3. [Q96BT3-1]
UniGeneiHs.288382.

Genome annotation databases

EnsembliENST00000440851; ENSP00000400140; ENSG00000102901. [Q96BT3-1]
ENST00000562787; ENSP00000457810; ENSG00000102901. [Q96BT3-1]
GeneIDi80152.
KEGGihsa:80152.
UCSCiuc002eun.4. human. [Q96BT3-1]

Polymorphism databases

DMDMi74760746.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK023173 mRNA. Translation: BAB14445.1.
AK055237 mRNA. Translation: BAB70884.1.
BC007642 mRNA. Translation: AAH07642.1.
BC007864 mRNA. Translation: AAH07864.2.
BC015202 mRNA. Translation: AAH15202.2.
CCDSiCCDS42182.1. [Q96BT3-1]
RefSeqiNP_079358.3. NM_025082.3. [Q96BT3-1]
UniGeneiHs.288382.

3D structure databases

ProteinModelPortaliQ96BT3.
SMRiQ96BT3. Positions 465-551.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi123143. 9 interactions.
IntActiQ96BT3. 6 interactions.
MINTiMINT-1376718.
STRINGi9606.ENSP00000219172.

PTM databases

PhosphoSiteiQ96BT3.

Polymorphism databases

DMDMi74760746.

Proteomic databases

MaxQBiQ96BT3.
PaxDbiQ96BT3.
PRIDEiQ96BT3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000440851; ENSP00000400140; ENSG00000102901. [Q96BT3-1]
ENST00000562787; ENSP00000457810; ENSG00000102901. [Q96BT3-1]
GeneIDi80152.
KEGGihsa:80152.
UCSCiuc002eun.4. human. [Q96BT3-1]

Organism-specific databases

CTDi80152.
GeneCardsiGC16M067862.
HGNCiHGNC:25787. CENPT.
HPAiHPA058036.
MIMi611510. gene.
neXtProtiNX_Q96BT3.
PharmGKBiPA142672263.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG26624.
GeneTreeiENSGT00390000003044.
HOGENOMiHOG000111545.
HOVERGENiHBG081089.
InParanoidiQ96BT3.
KOiK11512.
OMAiFSFYAKM.
OrthoDBiEOG7TQV2Z.
PhylomeDBiQ96BT3.
TreeFamiTF332946.

Enzyme and pathway databases

ReactomeiREACT_150425. Resolution of Sister Chromatid Cohesion.
REACT_150471. Separation of Sister Chromatids.
REACT_682. Mitotic Prometaphase.

Miscellaneous databases

ChiTaRSiCENPT. human.
GeneWikiiCENPT.
GenomeRNAii80152.
NextBioi70440.
PROiQ96BT3.
SOURCEiSearch...

Gene expression databases

BgeeiQ96BT3.
CleanExiHS_CENPT.
ExpressionAtlasiQ96BT3. baseline and differential.
GenevestigatoriQ96BT3.

Family and domain databases

Gene3Di1.10.20.10. 1 hit.
InterProiIPR028255. CENP-T.
IPR009072. Histone-fold.
[Graphical view]
PANTHERiPTHR14857. PTHR14857. 1 hit.
SUPFAMiSSF47113. SSF47113. 1 hit.
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] (ISOFORMS 2 AND 3).
    Tissue: Brain and Lung.
  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: Lung and Uterus.
  3. "Comprehensive analysis of the ICEN (Interphase Centromere Complex) components enriched in the CENP-A chromatin of human cells."
    Izuta H., Ikeno M., Suzuki N., Tomonaga T., Nozaki N., Obuse C., Kisu Y., Goshima N., Nomura F., Nomura N., Yoda K.
    Genes Cells 11:673-684(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  4. Cited for: IDENTIFICATION IN THE CENPA-NAC COMPLEX WITH CENPA; CENPC; CENPH; CENPM; CENPN AND CENPU.
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-373; SER-385 AND SER-386, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-397, 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. "Cancer-upregulated gene 2 (CUG2), a new component of centromere complex, is required for kinetochore function."
    Kim H., Lee M., Lee S., Park B., Koh W., Lee D.J., Lim D.S., Lee S.
    Mol. Cells 27:697-701(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN COMPLEX WITH CENPA AND CENPW.
  9. "CCAN makes multiple contacts with centromeric DNA to provide distinct pathways to the outer kinetochore."
    Hori T., Amano M., Suzuki A., Backer C.B., Welburn J.P., Dong Y., McEwen B.F., Shang W.-H., Suzuki E., Okawa K., Cheeseman I.M., Fukagawa T.
    Cell 135:1039-1052(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INTERACTION WITH CENPW.
  10. "Live-cell imaging reveals sustained centromere binding of CENP-T via CENP-A and CENP-B."
    Hellwig D., Muench S., Orthaus S., Hoischen C., Hemmerich P., Diekmann S.
    J. Biophotonics 1:245-254(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INTERACTION WITH CENPA AND CENPB.
  11. "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-397, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  12. "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-47; THR-85 AND SER-397, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. "Induced ectopic kinetochore assembly bypasses the requirement for CENP-A nucleosomes."
    Gascoigne K.E., Takeuchi K., Suzuki A., Hori T., Fukagawa T., Cheeseman I.M.
    Cell 145:410-422(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CENPW, PHOSPHORYLATION AT SER-47.
  14. "Premitotic assembly of human CENPs -T and -W switches centromeric chromatin to a mitotic state."
    Prendergast L., van Vuuren C., Kaczmarczyk A., Doering V., Hellwig D., Quinn N., Hoischen C., Diekmann S., Sullivan K.F.
    PLoS Biol. 9:E1001082-E1001082(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION IN A COMPLEX WITH HISTONE H3, INTERACTION WITH CENPW, SUBCELLULAR LOCATION.
  15. "CENP-T-W-S-X forms a unique centromeric chromatin structure with a histone-like fold."
    Nishino T., Takeuchi K., Gascoigne K.E., Suzuki A., Hori T., Oyama T., Morikawa K., Cheeseman I.M., Fukagawa T.
    Cell 148:487-501(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, SUBUNIT.

Entry informationi

Entry nameiCENPT_HUMAN
AccessioniPrimary (citable) accession number: Q96BT3
Secondary accession number(s): Q96I29
, Q96IC6, Q96NK9, Q9H901
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 19, 2006
Last sequence update: March 1, 2004
Last modified: March 4, 2015
This is version 121 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 16
    Human chromosome 16: 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. 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.