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Protein

Myotubularin-related protein 8

Gene

MTMR8

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

Functioni

Phosphatase that acts on lipids with a phosphoinositol headgroup.Curated

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei338 – 3381Phosphocysteine intermediatePROSITE-ProRule annotation
Binding sitei384 – 3841SubstrateBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Enzyme and pathway databases

BRENDAi3.1.3.95. 2681.

Names & Taxonomyi

Protein namesi
Recommended name:
Myotubularin-related protein 8 (EC:3.1.3.-)
Gene namesi
Name:MTMR8
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome X

Organism-specific databases

HGNCiHGNC:16825. MTMR8.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134942633.

Polymorphism and mutation databases

BioMutaiMTMR8.
DMDMi74751838.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 704704Myotubularin-related protein 8PRO_0000330034Add
BLAST

Proteomic databases

PaxDbiQ96EF0.
PRIDEiQ96EF0.

PTM databases

DEPODiQ96EF0.
iPTMnetiQ96EF0.
PhosphoSiteiQ96EF0.

Expressioni

Gene expression databases

BgeeiQ96EF0.
CleanExiHS_MTMR8.
GenevisibleiQ96EF0. HS.

Interactioni

Subunit structurei

Interacts with MTMR9.1 Publication

Protein-protein interaction databases

BioGridi120753. 4 interactions.
DIPiDIP-60046N.
IntActiQ96EF0. 1 interaction.
MINTiMINT-1484634.
STRINGi9606.ENSP00000363985.

Structurei

Secondary structure

1
704
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi126 – 1283Combined sources
Helixi134 – 1385Combined sources
Beta strandi142 – 1498Combined sources
Turni151 – 1544Combined sources
Beta strandi155 – 1573Combined sources
Beta strandi163 – 1686Combined sources
Helixi173 – 1808Combined sources
Helixi184 – 1863Combined sources
Beta strandi190 – 1945Combined sources
Turni196 – 1983Combined sources
Beta strandi201 – 2055Combined sources
Turni211 – 2133Combined sources
Helixi217 – 22711Combined sources
Beta strandi232 – 2343Combined sources
Beta strandi236 – 2405Combined sources
Helixi244 – 2529Combined sources
Turni260 – 2623Combined sources
Beta strandi266 – 2705Combined sources
Helixi276 – 29015Combined sources
Beta strandi292 – 2943Combined sources
Helixi297 – 30711Combined sources
Helixi309 – 32820Combined sources
Beta strandi334 – 3374Combined sources
Beta strandi339 – 3435Combined sources
Helixi344 – 35613Combined sources
Helixi358 – 3614Combined sources
Helixi363 – 37311Combined sources
Turni374 – 3785Combined sources
Helixi381 – 3844Combined sources
Helixi398 – 41215Combined sources
Turni414 – 4163Combined sources
Helixi421 – 43313Combined sources
Beta strandi441 – 4433Combined sources
Helixi444 – 4496Combined sources
Helixi452 – 4554Combined sources
Helixi459 – 4657Combined sources
Helixi467 – 4693Combined sources
Helixi490 – 4923Combined sources
Turni497 – 5015Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4Y7IX-ray2.80A/B122-505[»]
ProteinModelPortaliQ96EF0.
SMRiQ96EF0. Positions 4-505.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini126 – 500375Myotubularin phosphatasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni250 – 2534Substrate bindingBy similarity
Regioni275 – 2762Substrate bindingBy similarity
Regioni338 – 3447Substrate bindingBy similarity

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili515 – 54127Sequence analysisAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi338 – 3447Active site

Sequence similaritiesi

Contains 1 myotubularin phosphatase domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG1089. Eukaryota.
ENOG410XPTU. LUCA.
GeneTreeiENSGT00760000118832.
HOGENOMiHOG000210599.
HOVERGENiHBG000220.
InParanoidiQ96EF0.
KOiK18083.
OMAiFTMYGVL.
OrthoDBiEOG71RXJC.
PhylomeDBiQ96EF0.
TreeFamiTF315197.

Family and domain databases

InterProiIPR030591. MTMR8.
IPR010569. Myotubularin-like_Pase_dom.
IPR030564. Myotubularin_fam.
IPR011993. PH_dom-like.
IPR029021. Prot-tyrosine_phosphatase-like.
IPR016130. Tyr_Pase_AS.
IPR003595. Tyr_Pase_cat.
[Graphical view]
PANTHERiPTHR10807. PTHR10807. 1 hit.
PTHR10807:SF36. PTHR10807:SF36. 1 hit.
PfamiPF06602. Myotub-related. 1 hit.
[Graphical view]
SMARTiSM00404. PTPc_motif. 1 hit.
[Graphical view]
SUPFAMiSSF50729. SSF50729. 1 hit.
SSF52799. SSF52799. 1 hit.
PROSITEiPS51339. PPASE_MYOTUBULARIN. 1 hit.
PS00383. TYR_PHOSPHATASE_1. 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: Q96EF0-1) [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
MDHITVPKVE NVKLVDRYVS KKPANGILYL TATHLIYVEA SGAARKETWI
60 70 80 90 100
ALHHIATVEK LPITSLGCPL TLRCKNFRVA HFVLDSDLVC HEVYISLLKL
110 120 130 140 150
SQPALPEDLY AFSYNPKSSK EMRESGWKLI DPISDFGRMG IPNRNWTITD
160 170 180 190 200
ANRNYEICST YPPEIVVPKS VTLGTVVGSS KFRSKERVPV LSYLYKENNA
210 220 230 240 250
AICRCSQPLS GFYTRCVDDE LLLEAISQTN PGSQFMYVVD TRPKLNAMAN
260 270 280 290 300
RAAGKGYENE DNYANIRFRF MGIENIHVMR SSLQKLLEVC ELKTPTMSEF
310 320 330 340 350
LSGLESSGWL RHIKAIMDAG IFITKAVKVE KASVLVHCSD GWDRTAQVCS
360 370 380 390 400
VASILLDPFY RTFKGLMILI EKEWISMGHK FSQRCGHLDG DSKEVSPIFT
410 420 430 440 450
QFLDCIWQLM EQFPCAFEFN ENFLLEIHDH VFSCQFGNFL GNCQKDREDL
460 470 480 490 500
RVYEKTHSVW PFLVQRKPDF RNPLYKGFTM YGVLNPSTVP YNIQFWCGMY
510 520 530 540 550
NRFDKGLQPK QSMLESLLEI KKQRAMLETD VHELEKKLKV RDEPPEEICT
560 570 580 590 600
CSQLGNILSQ HLGSPLTNPL GFMGINGDLN TLMENGTLSR EGGLRAQMDQ
610 620 630 640 650
VKSQGADLHH NCCEIVGSLR AINISGDVGI SEAMGISGDM CTFEATGFSK
660 670 680 690 700
DLGICGAMDI SEATGISGNL GISEARGFSG DMGILGDTGI SKASTKEADY

SKHQ
Length:704
Mass (Da):78,919
Last modified:December 1, 2001 - v1
Checksum:i515BE817C9AEA961
GO
Isoform 2 (identifier: Q96EF0-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     153-265: Missing.

Note: No experimental confirmation available.
Show »
Length:591
Mass (Da):66,312
Checksum:iD7E38C5FDAC096E9
GO

Sequence cautioni

The sequence BAA90964.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti130 – 1301I → S in BAA90964 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti127 – 1271W → R in a breast cancer sample; somatic mutation. 1 Publication
VAR_042688
Natural varianti454 – 4541E → K in a breast cancer sample; somatic mutation. 1 Publication
VAR_042689

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei153 – 265113Missing in isoform 2. 1 PublicationVSP_033007Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL356317, AL034408 Genomic DNA. Translation: CAI39933.1.
AL356317, AL034408 Genomic DNA. Translation: CAI39934.1.
AL034408 Genomic DNA. Translation: CAI43024.1.
AL034408 Genomic DNA. Translation: CAI43025.1.
CH471132 Genomic DNA. Translation: EAX05411.1.
BC012399 mRNA. Translation: AAH12399.1.
AK000133 mRNA. Translation: BAA90964.1. Different initiation.
CCDSiCCDS14379.1. [Q96EF0-1]
RefSeqiNP_060147.2. NM_017677.3. [Q96EF0-1]
UniGeneiHs.442892.

Genome annotation databases

EnsembliENST00000374852; ENSP00000363985; ENSG00000102043. [Q96EF0-1]
GeneIDi55613.
KEGGihsa:55613.
UCSCiuc004dvs.4. human. [Q96EF0-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL356317, AL034408 Genomic DNA. Translation: CAI39933.1.
AL356317, AL034408 Genomic DNA. Translation: CAI39934.1.
AL034408 Genomic DNA. Translation: CAI43024.1.
AL034408 Genomic DNA. Translation: CAI43025.1.
CH471132 Genomic DNA. Translation: EAX05411.1.
BC012399 mRNA. Translation: AAH12399.1.
AK000133 mRNA. Translation: BAA90964.1. Different initiation.
CCDSiCCDS14379.1. [Q96EF0-1]
RefSeqiNP_060147.2. NM_017677.3. [Q96EF0-1]
UniGeneiHs.442892.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4Y7IX-ray2.80A/B122-505[»]
ProteinModelPortaliQ96EF0.
SMRiQ96EF0. Positions 4-505.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi120753. 4 interactions.
DIPiDIP-60046N.
IntActiQ96EF0. 1 interaction.
MINTiMINT-1484634.
STRINGi9606.ENSP00000363985.

PTM databases

DEPODiQ96EF0.
iPTMnetiQ96EF0.
PhosphoSiteiQ96EF0.

Polymorphism and mutation databases

BioMutaiMTMR8.
DMDMi74751838.

Proteomic databases

PaxDbiQ96EF0.
PRIDEiQ96EF0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000374852; ENSP00000363985; ENSG00000102043. [Q96EF0-1]
GeneIDi55613.
KEGGihsa:55613.
UCSCiuc004dvs.4. human. [Q96EF0-1]

Organism-specific databases

CTDi55613.
GeneCardsiMTMR8.
HGNCiHGNC:16825. MTMR8.
neXtProtiNX_Q96EF0.
PharmGKBiPA134942633.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1089. Eukaryota.
ENOG410XPTU. LUCA.
GeneTreeiENSGT00760000118832.
HOGENOMiHOG000210599.
HOVERGENiHBG000220.
InParanoidiQ96EF0.
KOiK18083.
OMAiFTMYGVL.
OrthoDBiEOG71RXJC.
PhylomeDBiQ96EF0.
TreeFamiTF315197.

Enzyme and pathway databases

BRENDAi3.1.3.95. 2681.

Miscellaneous databases

ChiTaRSiMTMR8. human.
GenomeRNAii55613.
NextBioi60188.
PROiQ96EF0.

Gene expression databases

BgeeiQ96EF0.
CleanExiHS_MTMR8.
GenevisibleiQ96EF0. HS.

Family and domain databases

InterProiIPR030591. MTMR8.
IPR010569. Myotubularin-like_Pase_dom.
IPR030564. Myotubularin_fam.
IPR011993. PH_dom-like.
IPR029021. Prot-tyrosine_phosphatase-like.
IPR016130. Tyr_Pase_AS.
IPR003595. Tyr_Pase_cat.
[Graphical view]
PANTHERiPTHR10807. PTHR10807. 1 hit.
PTHR10807:SF36. PTHR10807:SF36. 1 hit.
PfamiPF06602. Myotub-related. 1 hit.
[Graphical view]
SMARTiSM00404. PTPc_motif. 1 hit.
[Graphical view]
SUPFAMiSSF50729. SSF50729. 1 hit.
SSF52799. SSF52799. 1 hit.
PROSITEiPS51339. PPASE_MYOTUBULARIN. 1 hit.
PS00383. TYR_PHOSPHATASE_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The DNA sequence of the human X chromosome."
    Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
    , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
    Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "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: Ovary.
  4. "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] OF 85-704 (ISOFORM 2).
    Tissue: Colon.
  5. "Systematic analysis of myotubularins: heteromeric interactions, subcellular localisation and endosome related functions."
    Lorenzo O., Urbe S., Clague M.J.
    J. Cell Sci. 119:2953-2959(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INTERACTION WITH MTMR9.
  6. Cited for: VARIANTS [LARGE SCALE ANALYSIS] ARG-127 AND LYS-454.

Entry informationi

Entry nameiMTMR8_HUMAN
AccessioniPrimary (citable) accession number: Q96EF0
Secondary accession number(s): Q5JT99, Q9NXP6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 29, 2008
Last sequence update: December 1, 2001
Last modified: May 11, 2016
This is version 122 of the entry and version 1 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 X
    Human chromosome X: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. 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.