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Protein

Molybdenum cofactor sulfurase

Gene

MOCOS

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

Functioni

Sulfurates the molybdenum cofactor. Sulfation of molybdenum is essential for xanthine dehydrogenase (XDH) and aldehyde oxidase (ADO) enzymes in which molybdenum cofactor is liganded by 1 oxygen and 1 sulfur atom in active form. In vitro, the C-terminal domain is able to reduce N-hydroxylated prodrugs, such as benzamidoxime.UniRule annotation1 Publication

Catalytic activityi

Molybdenum cofactor + L-cysteine + 2 H+ = thio-molybdenum cofactor + L-alanine + H2O.UniRule annotation

Cofactori

pyridoxal 5'-phosphateUniRule annotation

Kineticsi

  1. KM=15 µM for benzamidoxime1 Publication
  1. Vmax=0.24 nmol/min/mg enzyme1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei424 – 4241UniRule annotation

GO - Molecular functioni

  • lyase activity Source: UniProtKB-HAMAP
  • molybdenum ion binding Source: UniProtKB-HAMAP
  • Mo-molybdopterin cofactor sulfurase activity Source: UniProtKB
  • pyridoxal phosphate binding Source: UniProtKB-HAMAP
  • transferase activity Source: UniProtKB-KW

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Molybdenum cofactor biosynthesis

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

ReactomeiREACT_25073. Molybdenum cofactor biosynthesis.

Names & Taxonomyi

Protein namesi
Recommended name:
Molybdenum cofactor sulfuraseUniRule annotation (EC:2.8.1.9UniRule annotation)
Short name:
MCSUniRule annotation
Short name:
MOSUniRule annotation
Short name:
MoCo sulfuraseUniRule annotation
Short name:
hMCS
Alternative name(s):
Molybdenum cofactor sulfurtransferaseUniRule annotation
Gene namesi
Name:MOCOSUniRule annotation
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 18

Organism-specific databases

HGNCiHGNC:18234. MOCOS.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Pathology & Biotechi

Involvement in diseasei

Xanthinuria 2 (XU2)4 Publications

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA disorder characterized by excretion of very large amounts of xanthine in the urine and a tendency to form xanthine stones. Uric acid is strikingly diminished in serum and urine. In addition, patients suffering of xanthinuria 2 cannot metabolize allopurinol into oxypurinol due to dual deficiency of xanthine dehydrogenase and aldehyde oxidase.

See also OMIM:603592
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti57 – 571A → P in XU2. 1 Publication
VAR_027528
Natural varianti294 – 2941T → I in XU2. 1 Publication
VAR_027533
Natural varianti776 – 7761R → C in XU2. 1 Publication
VAR_045899

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi603592. phenotype.
Orphaneti93602. Xanthinuria type II.
PharmGKBiPA134964534.

Polymorphism and mutation databases

BioMutaiMOCOS.
DMDMi296438294.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 888888Molybdenum cofactor sulfurasePRO_0000249952Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei34 – 341Phosphoserine1 Publication
Modified residuei264 – 2641N6-(pyridoxal phosphate)lysineUniRule annotation
Modified residuei528 – 5281Phosphoserine2 Publications
Modified residuei530 – 5301Phosphoserine2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ96EN8.
PaxDbiQ96EN8.
PRIDEiQ96EN8.

PTM databases

PhosphoSiteiQ96EN8.

Expressioni

Gene expression databases

BgeeiQ96EN8.
CleanExiHS_MOCOS.
GenevisibleiQ96EN8. HS.

Organism-specific databases

HPAiHPA039412.
HPA047958.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
PARVAQ9NVD74EBI-1220583,EBI-747655

Protein-protein interaction databases

BioGridi120363. 10 interactions.
IntActiQ96EN8. 2 interactions.
STRINGi9606.ENSP00000261326.

Structurei

3D structure databases

ProteinModelPortaliQ96EN8.
SMRiQ96EN8. Positions 51-421, 591-706.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini706 – 867162MOSCUniRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family. MOCOS subfamily.UniRule annotation
Contains 1 MOSC domain.UniRule annotation

Phylogenomic databases

eggNOGiCOG3217.
GeneTreeiENSGT00530000063150.
HOGENOMiHOG000029698.
HOVERGENiHBG081980.
InParanoidiQ96EN8.
KOiK15631.
OMAiMSTFEDC.
OrthoDBiEOG7ZKS98.
PhylomeDBiQ96EN8.
TreeFamiTF105761.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
HAMAPiMF_03050. MOCOS.
InterProiIPR000192. Aminotrans_V_dom.
IPR005302. MoCF_Sase_C.
IPR028886. MoCo_sulfurase.
IPR005303. MOSC_N.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
IPR011037. Pyrv_Knase-like_insert_dom.
[Graphical view]
PfamiPF00266. Aminotran_5. 1 hit.
PF03473. MOSC. 1 hit.
PF03476. MOSC_N. 1 hit.
[Graphical view]
SUPFAMiSSF50800. SSF50800. 1 hit.
SSF53383. SSF53383. 2 hits.
PROSITEiPS51340. MOSC. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q96EN8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAGAAAESGR ELWTFAGSRD PSAPRLAYGY GPGSLRELRA REFSRLAGTV
60 70 80 90 100
YLDHAGATLF SQSQLESFTS DLMENTYGNP HSQNISSKLT HDTVEQVRYR
110 120 130 140 150
ILAHFHTTAE DYTVIFTAGS TAALKLVAEA FPWVSQGPES SGSRFCYLTD
160 170 180 190 200
SHTSVVGMRN VTMAINVIST PVRPEDLWSA EERSASASNP DCQLPHLFCY
210 220 230 240 250
PAQSNFSGVR YPLSWIEEVK SGRLHPVSTP GKWFVLLDAA SYVSTSPLDL
260 270 280 290 300
SAHQADFVPI SFYKIFGFPT GLGALLVHNR AAPLLRKTYF GGGTASAYLA
310 320 330 340 350
GEDFYIPRQS VAQRFEDGTI SFLDVIALKH GFDTLERLTG GMENIKQHTF
360 370 380 390 400
TLAQYTYVAL SSLQYPNGAP VVRIYSDSEF SSPEVQGPII NFNVLDDKGN
410 420 430 440 450
IIGYSQVDKM ASLYNIHLRT GCFCNTGACQ RHLGISNEMV RKHFQAGHVC
460 470 480 490 500
GDNMDLIDGQ PTGSVRISFG YMSTLDDVQA FLRFIIDTRL HSSGDWPVPQ
510 520 530 540 550
AHADTGETGA PSADSQADVI PAVMGRRSLS PQEDALTGSR VWNNSSTVNA
560 570 580 590 600
VPVAPPVCDV ARTQPTPSEK AAGVLEGALG PHVVTNLYLY PIKSCAAFEV
610 620 630 640 650
TRWPVGNQGL LYDRSWMVVN HNGVCLSQKQ EPRLCLIQPF IDLRQRIMVI
660 670 680 690 700
KAKGMEPIEV PLEENSERTQ IRQSRVCADR VSTYDCGEKI SSWLSTFFGR
710 720 730 740 750
PCHLIKQSSN SQRNAKKKHG KDQLPGTMAT LSLVNEAQYL LINTSSILEL
760 770 780 790 800
HRQLNTSDEN GKEELFSLKD LSLRFRANII INGKRAFEEE KWDEISIGSL
810 820 830 840 850
RFQVLGPCHR CQMICIDQQT GQRNQHVFQK LSESRETKVN FGMYLMHASL
860 870 880
DLSSPCFLSV GSQVLPVLKE NVEGHDLPAS EKHQDVTS
Length:888
Mass (Da):98,120
Last modified:May 18, 2010 - v2
Checksum:i07DB9457516E8C06
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti119 – 1191G → E in BAD96606 (PubMed:14702039).Curated
Sequence conflicti689 – 6891K → E in BAD96606 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti57 – 571A → P in XU2. 1 Publication
VAR_027528
Natural varianti120 – 1201S → N.
Corresponds to variant rs3744900 [ dbSNP | Ensembl ].
VAR_027529
Natural varianti170 – 1701T → I.2 Publications
Corresponds to variant rs623053 [ dbSNP | Ensembl ].
VAR_027530
Natural varianti184 – 1841S → G.3 Publications
Corresponds to variant rs540967 [ dbSNP | Ensembl ].
VAR_027531
Natural varianti225 – 2251H → R.4 Publications
Corresponds to variant rs623558 [ dbSNP | Ensembl ].
VAR_027532
Natural varianti294 – 2941T → I in XU2. 1 Publication
VAR_027533
Natural varianti358 – 3581V → M.3 Publications
Corresponds to variant rs678560 [ dbSNP | Ensembl ].
VAR_027534
Natural varianti495 – 4951D → N.
Corresponds to variant rs8088347 [ dbSNP | Ensembl ].
VAR_027535
Natural varianti541 – 5411V → L.
Corresponds to variant rs672924 [ dbSNP | Ensembl ].
VAR_027536
Natural varianti703 – 7031H → N.2 Publications
Corresponds to variant rs594445 [ dbSNP | Ensembl ].
VAR_027537
Natural varianti776 – 7761R → C in XU2. 1 Publication
VAR_045899
Natural varianti867 – 8671V → A.
Corresponds to variant rs1057251 [ dbSNP | Ensembl ].
VAR_027538

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK000740 mRNA. Translation: BAA91353.1.
AK222886 mRNA. Translation: BAD96606.1.
AC023043 Genomic DNA. No translation available.
BC012079 mRNA. Translation: AAH12079.1.
AL834481 mRNA. Translation: CAD39140.1.
CCDSiCCDS11919.1.
PIRiJC7680.
RefSeqiNP_060417.2. NM_017947.2.
UniGeneiHs.405028.

Genome annotation databases

EnsembliENST00000261326; ENSP00000261326; ENSG00000075643.
GeneIDi55034.
KEGGihsa:55034.
UCSCiuc002kzq.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK000740 mRNA. Translation: BAA91353.1.
AK222886 mRNA. Translation: BAD96606.1.
AC023043 Genomic DNA. No translation available.
BC012079 mRNA. Translation: AAH12079.1.
AL834481 mRNA. Translation: CAD39140.1.
CCDSiCCDS11919.1.
PIRiJC7680.
RefSeqiNP_060417.2. NM_017947.2.
UniGeneiHs.405028.

3D structure databases

ProteinModelPortaliQ96EN8.
SMRiQ96EN8. Positions 51-421, 591-706.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi120363. 10 interactions.
IntActiQ96EN8. 2 interactions.
STRINGi9606.ENSP00000261326.

PTM databases

PhosphoSiteiQ96EN8.

Polymorphism and mutation databases

BioMutaiMOCOS.
DMDMi296438294.

Proteomic databases

MaxQBiQ96EN8.
PaxDbiQ96EN8.
PRIDEiQ96EN8.

Protocols and materials databases

DNASUi55034.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000261326; ENSP00000261326; ENSG00000075643.
GeneIDi55034.
KEGGihsa:55034.
UCSCiuc002kzq.4. human.

Organism-specific databases

CTDi55034.
GeneCardsiGC18P033767.
H-InvDBHIX0202662.
HGNCiHGNC:18234. MOCOS.
HPAiHPA039412.
HPA047958.
MIMi603592. phenotype.
613274. gene.
neXtProtiNX_Q96EN8.
Orphaneti93602. Xanthinuria type II.
PharmGKBiPA134964534.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG3217.
GeneTreeiENSGT00530000063150.
HOGENOMiHOG000029698.
HOVERGENiHBG081980.
InParanoidiQ96EN8.
KOiK15631.
OMAiMSTFEDC.
OrthoDBiEOG7ZKS98.
PhylomeDBiQ96EN8.
TreeFamiTF105761.

Enzyme and pathway databases

ReactomeiREACT_25073. Molybdenum cofactor biosynthesis.

Miscellaneous databases

GeneWikiiMOCOS.
GenomeRNAii55034.
NextBioi58459.
PROiQ96EN8.
SOURCEiSearch...

Gene expression databases

BgeeiQ96EN8.
CleanExiHS_MOCOS.
GenevisibleiQ96EN8. HS.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
HAMAPiMF_03050. MOCOS.
InterProiIPR000192. Aminotrans_V_dom.
IPR005302. MoCF_Sase_C.
IPR028886. MoCo_sulfurase.
IPR005303. MOSC_N.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
IPR011037. Pyrv_Knase-like_insert_dom.
[Graphical view]
PfamiPF00266. Aminotran_5. 1 hit.
PF03473. MOSC. 1 hit.
PF03476. MOSC_N. 1 hit.
[Graphical view]
SUPFAMiSSF50800. SSF50800. 1 hit.
SSF53383. SSF53383. 2 hits.
PROSITEiPS51340. MOSC. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Mutation of human molybdenum cofactor sulfurase gene is responsible to classical xanthinuria type II."
    Ichida K., Matsumura T., Sakuma R., Hosoya T., Nishino T.
    Biochem. Biophys. Res. Commun. 282:1194-1200(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], INVOLVEMENT IN XU2, VARIANTS ARG-225 AND ASN-703.
  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(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANTS ILE-170; GLY-184; ARG-225; MET-358 AND ASN-703.
    Tissue: Liver.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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], VARIANTS ILE-170; GLY-184; ARG-225 AND MET-358.
    Tissue: Lung.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 95-888, VARIANTS ILE-170 GLY-184; ARG-225 AND MET-358.
    Tissue: Melanoma.
  6. "Identification of the missing component in the mitochondrial benzamidoxime prodrug converting system as a novel molybdenum enzyme."
    Havemeyer A., Bittner F., Wollers S., Mendel R., Kunze T., Clement B.
    J. Biol. Chem. 281:34796-34802(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES.
  7. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
    Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
    Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-528 AND SER-530, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-528 AND SER-530, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-34, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  11. "Classical xanthinuria type 2 associated with a missense mutation in HMCS, the gene encoding molybdenum cofactor sulfurase."
    Finckh U., Haddad M., Lukacs Z., Wagener C., Gal A.
    (In) EUREGIO congress of clinical chemistry and laboratory medicine, pp.36-37, Aachen (2003)
    Cited for: VARIANT XU2 ILE-294.
  12. "Identification of a new point mutation in the human molybdenum cofactor sulferase gene that is responsible for xanthinuria type II."
    Yamamoto T., Moriwaki Y., Takahashi S., Tsutsumi Z., Tuneyoshi K., Matsui K., Cheng J., Hada T.
    Metabolism 52:1501-1504(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT XU2 PRO-57.
  13. "Identification and characterization of the first mutation (Arg776Cys) in the C-terminal domain of the human molybdenum cofactor sulfurase (HMCS) associated with type II classical xanthinuria."
    Peretz H., Naamati M.S., Levartovsky D., Lagziel A., Shani E., Horn I., Shalev H., Landau D.
    Mol. Genet. Metab. 91:23-29(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT XU2 CYS-776.

Entry informationi

Entry nameiMOCOS_HUMAN
AccessioniPrimary (citable) accession number: Q96EN8
Secondary accession number(s): Q53GP5, Q8N3A4, Q9NWM7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 19, 2006
Last sequence update: May 18, 2010
Last modified: July 22, 2015
This is version 112 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 18
    Human chromosome 18: 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.