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Q96FJ0

- STALP_HUMAN

UniProt

Q96FJ0 - STALP_HUMAN

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Protein
AMSH-like protease
Gene
STAMBPL1, AMSHLP, KIAA1373
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Zinc metalloprotease that specifically cleaves 'Lys-63'-linked polyubiquitin chains. Does not cleave 'Lys-48'-linked polyubiquitin chains.1 Publication

Cofactori

Binds 2 zinc ions per subunit.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei292 – 2921Indirect zinc-binding
Metal bindingi347 – 3471Zinc 1; catalytic
Metal bindingi349 – 3491Zinc 1; catalytic
Metal bindingi360 – 3601Zinc 1; catalytic
Metal bindingi362 – 3621Zinc 2
Metal bindingi402 – 4021Zinc 2
Metal bindingi408 – 4081Zinc 2
Metal bindingi410 – 4101Zinc 2

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. metallopeptidase activity Source: UniProtKB-KW
  3. protein binding Source: IntAct
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Biological processi

Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Protein family/group databases

MEROPSiM67.003.

Names & Taxonomyi

Protein namesi
Recommended name:
AMSH-like protease (EC:3.4.19.-)
Short name:
AMSH-LP
Alternative name(s):
STAM-binding protein-like 1
Gene namesi
Synonyms:AMSHLP, KIAA1373
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 10

Organism-specific databases

HGNCiHGNC:24105. STAMBPL1.

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi292 – 2921E → A: Complete loss of catalytic activity. 1 Publication
Mutagenesisi329 – 3291E → A: 3-fold decrease in substrate affinity. 1 Publication
Mutagenesisi332 – 3321F → A: 12-fold decrease in substrate affinity, little effect on catalytic activity. 1 Publication
Mutagenesisi353 – 3531T → A: 19-fold decrease in activity, no change in substrate affinity. 1 Publication
Mutagenesisi355 – 3551F → A: 161-fold decrease in activity, no change in substrate affinity. 1 Publication
Mutagenesisi357 – 3571S → A: 34-fold decrease in activity. 1 Publication
Mutagenesisi358 – 3581S → A: 10-fold decrease in activity, no change in substrate affinity. 1 Publication
Mutagenesisi360 – 3601D → A: Complete loss of catalytic activity. 1 Publication
Mutagenesisi370 – 3701M → A: 18-fold decrease in substrate affinity, little effect on catalytic activity. 1 Publication
Mutagenesisi402 – 4021C → S: 402-fold decrease in activity, slight increase in substrate affinity. 1 Publication
Mutagenesisi407 – 4071F → A: 35-fold decrease in activity, slight increase in substrate affinity. 1 Publication

Organism-specific databases

PharmGKBiPA142670864.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 436436AMSH-like protease
PRO_0000194874Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication
Modified residuei25 – 251Phosphoserine1 Publication
Modified residuei242 – 2421Phosphoserine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ96FJ0.
PaxDbiQ96FJ0.
PRIDEiQ96FJ0.

PTM databases

PhosphoSiteiQ96FJ0.

Expressioni

Tissue specificityi

Ubiquitously expressed.1 Publication

Gene expression databases

ArrayExpressiQ96FJ0.
BgeeiQ96FJ0.
CleanExiHS_STAMBPL1.
GenevestigatoriQ96FJ0.

Organism-specific databases

HPAiHPA040202.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
RNF32Q9H0A62EBI-745021,EBI-724829

Protein-protein interaction databases

BioGridi121614. 17 interactions.
IntActiQ96FJ0. 13 interactions.
MINTiMINT-1444179.
STRINGi9606.ENSP00000360992.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi269 – 2724
Helixi275 – 28713
Turni288 – 2903
Beta strandi294 – 3029
Beta strandi305 – 3139
Beta strandi316 – 3194
Beta strandi322 – 3254
Helixi328 – 33811
Beta strandi341 – 3488
Beta strandi350 – 3523
Helixi358 – 37013
Beta strandi375 – 3806
Helixi381 – 3833
Beta strandi385 – 3917
Helixi393 – 4019
Beta strandi416 – 4194
Beta strandi421 – 4266
Beta strandi431 – 4344

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2ZNRX-ray1.20A264-436[»]
2ZNVX-ray1.60A/D264-436[»]
ProteinModelPortaliQ96FJ0.
SMRiQ96FJ0. Positions 18-136, 263-436.

Miscellaneous databases

EvolutionaryTraceiQ96FJ0.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini264 – 373110MPN
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi347 – 36014JAMM motif
Add
BLAST

Domaini

The JAMM motif is essential for the protease activity By similarity.

Sequence similaritiesi

Belongs to the peptidase M67C family.

Phylogenomic databases

eggNOGiCOG1310.
HOGENOMiHOG000195792.
HOVERGENiHBG058519.
KOiK11867.
OMAiDLCHKFL.
OrthoDBiEOG7NW698.
PhylomeDBiQ96FJ0.
TreeFamiTF323215.

Family and domain databases

InterProiIPR000555. JAMM/MPN+_dom.
IPR015063. USP8_dimer.
[Graphical view]
PfamiPF01398. JAB. 1 hit.
PF08969. USP8_dimer. 1 hit.
[Graphical view]
SMARTiSM00232. JAB_MPN. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q96FJ0-1) [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

MDQPFTVNSL KKLAAMPDHT DVSLSPEERV RALSKLGCNI TISEDITPRR    50
YFRSGVEMER MASVYLEEGN LENAFVLYNK FITLFVEKLP NHRDYQQCAV 100
PEKQDIMKKL KEIAFPRTDE LKNDLLKKYN VEYQEYLQSK NKYKAEILKK 150
LEHQRLIEAE RKRIAQMRQQ QLESEQFLFF EDQLKKQELA RGQMRSQQTS 200
GLSEQIDGSA LSCFSTHQNN SLLNVFADQP NKSDATNYAS HSPPVNRALT 250
PAATLSAVQN LVVEGLRCVV LPEDLCHKFL QLAESNTVRG IETCGILCGK 300
LTHNEFTITH VIVPKQSAGP DYCDMENVEE LFNVQDQHDL LTLGWIHTHP 350
TQTAFLSSVD LHTHCSYQLM LPEAIAIVCS PKHKDTGIFR LTNAGMLEVS 400
ACKKKGFHPH TKEPRLFSIC KHVLVKDIKI IVLDLR 436
Length:436
Mass (Da):49,783
Last modified:November 23, 2004 - v2
Checksum:i722662C76A734102
GO
Isoform 2 (identifier: Q96FJ0-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     420-436: CKHVLVKDIKIIVLDLR → QKFLSGIISGTALEMEPLKIGYGPNGFPLLGISRSSSPSEQL

Show »
Length:461
Mass (Da):52,199
Checksum:i266828EB12055970
GO

Sequence cautioni

The sequence BAA92611.1 differs from that shown. Reason: Erroneous initiation.
The sequence CAI13863.1 differs from that shown. Reason: Erroneous gene model prediction.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti196 – 1961S → N.
Corresponds to variant rs12254856 [ dbSNP | Ensembl ].
VAR_051817
Natural varianti204 – 2041E → K.
Corresponds to variant rs34270879 [ dbSNP | Ensembl ].
VAR_051818
Natural varianti210 – 2101A → T.
Corresponds to variant rs9988723 [ dbSNP | Ensembl ].
VAR_051819

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei420 – 43617CKHVL…VLDLR → QKFLSGIISGTALEMEPLKI GYGPNGFPLLGISRSSSPSE QL in isoform 2.
VSP_014648Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB010120 mRNA. Translation: BAC77766.1.
AB037794 mRNA. Translation: BAA92611.1. Different initiation.
AK056086 mRNA. Translation: BAG51619.1.
AL157394 Genomic DNA. Translation: CAI13861.1.
AL157394 Genomic DNA. Translation: CAI13862.1.
AL157394 Genomic DNA. Translation: CAI13863.1. Sequence problems.
CH471066 Genomic DNA. Translation: EAW50156.1.
BC010846 mRNA. Translation: AAH10846.2.
CCDSiCCDS7391.1. [Q96FJ0-1]
RefSeqiNP_065850.1. NM_020799.3. [Q96FJ0-1]
XP_006717991.1. XM_006717928.1. [Q96FJ0-1]
XP_006717992.1. XM_006717929.1. [Q96FJ0-1]
XP_006717993.1. XM_006717930.1. [Q96FJ0-1]
UniGeneiHs.16229.
Hs.701879.

Genome annotation databases

EnsembliENST00000371924; ENSP00000360992; ENSG00000138134. [Q96FJ0-1]
ENST00000371926; ENSP00000360994; ENSG00000138134. [Q96FJ0-1]
ENST00000371927; ENSP00000360995; ENSG00000138134. [Q96FJ0-2]
GeneIDi57559.
KEGGihsa:57559.
UCSCiuc001kfk.4. human. [Q96FJ0-1]
uc010qmx.2. human. [Q96FJ0-2]

Polymorphism databases

DMDMi71153542.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB010120 mRNA. Translation: BAC77766.1 .
AB037794 mRNA. Translation: BAA92611.1 . Different initiation.
AK056086 mRNA. Translation: BAG51619.1 .
AL157394 Genomic DNA. Translation: CAI13861.1 .
AL157394 Genomic DNA. Translation: CAI13862.1 .
AL157394 Genomic DNA. Translation: CAI13863.1 . Sequence problems.
CH471066 Genomic DNA. Translation: EAW50156.1 .
BC010846 mRNA. Translation: AAH10846.2 .
CCDSi CCDS7391.1. [Q96FJ0-1 ]
RefSeqi NP_065850.1. NM_020799.3. [Q96FJ0-1 ]
XP_006717991.1. XM_006717928.1. [Q96FJ0-1 ]
XP_006717992.1. XM_006717929.1. [Q96FJ0-1 ]
XP_006717993.1. XM_006717930.1. [Q96FJ0-1 ]
UniGenei Hs.16229.
Hs.701879.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2ZNR X-ray 1.20 A 264-436 [» ]
2ZNV X-ray 1.60 A/D 264-436 [» ]
ProteinModelPortali Q96FJ0.
SMRi Q96FJ0. Positions 18-136, 263-436.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 121614. 17 interactions.
IntActi Q96FJ0. 13 interactions.
MINTi MINT-1444179.
STRINGi 9606.ENSP00000360992.

Protein family/group databases

MEROPSi M67.003.

PTM databases

PhosphoSitei Q96FJ0.

Polymorphism databases

DMDMi 71153542.

Proteomic databases

MaxQBi Q96FJ0.
PaxDbi Q96FJ0.
PRIDEi Q96FJ0.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000371924 ; ENSP00000360992 ; ENSG00000138134 . [Q96FJ0-1 ]
ENST00000371926 ; ENSP00000360994 ; ENSG00000138134 . [Q96FJ0-1 ]
ENST00000371927 ; ENSP00000360995 ; ENSG00000138134 . [Q96FJ0-2 ]
GeneIDi 57559.
KEGGi hsa:57559.
UCSCi uc001kfk.4. human. [Q96FJ0-1 ]
uc010qmx.2. human. [Q96FJ0-2 ]

Organism-specific databases

CTDi 57559.
GeneCardsi GC10P090630.
H-InvDB HIX0009014.
HGNCi HGNC:24105. STAMBPL1.
HPAi HPA040202.
MIMi 612352. gene.
neXtProti NX_Q96FJ0.
PharmGKBi PA142670864.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1310.
HOGENOMi HOG000195792.
HOVERGENi HBG058519.
KOi K11867.
OMAi DLCHKFL.
OrthoDBi EOG7NW698.
PhylomeDBi Q96FJ0.
TreeFami TF323215.

Miscellaneous databases

ChiTaRSi STAMBPL1. human.
EvolutionaryTracei Q96FJ0.
GeneWikii STAMBPL1.
GenomeRNAii 57559.
NextBioi 64054.
PROi Q96FJ0.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q96FJ0.
Bgeei Q96FJ0.
CleanExi HS_STAMBPL1.
Genevestigatori Q96FJ0.

Family and domain databases

InterProi IPR000555. JAMM/MPN+_dom.
IPR015063. USP8_dimer.
[Graphical view ]
Pfami PF01398. JAB. 1 hit.
PF08969. USP8_dimer. 1 hit.
[Graphical view ]
SMARTi SM00232. JAB_MPN. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of AMSH-LP containing a Jab1/MPN domain metalloenzyme motif."
    Kikuchi K., Ishii N., Asano H., Sugamura K.
    Biochem. Biophys. Res. Commun. 306:637-643(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
    Tissue: Peripheral blood lymphocyte.
  2. "Prediction of the coding sequences of unidentified human genes. XVI. The complete sequences of 150 new cDNA clones from brain which code for large proteins in vitro."
    Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.
    DNA Res. 7:65-73(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Brain.
  3. "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] (ISOFORM 1).
  4. "The DNA sequence and comparative analysis of human chromosome 10."
    Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
    , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
    Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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: Pancreas.
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25 AND SER-242, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "Structural basis for specific cleavage of Lys 63-linked polyubiquitin chains."
    Sato Y., Yoshikawa A., Yamagata A., Mimura H., Yamashita M., Ookata K., Nureki O., Iwai K., Komada M., Fukai S.
    Nature 455:358-362(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.2 ANGSTROMS) OF 263-436 IN COMPLEXES WITH ZINC IONS AND WITH LYS-63-LINKED DI-UBIQUITIN, FUNCTION, COFACTOR, MUTAGENESIS OF GLU-292; GLU-329; PHE-332; THR-353; PHE-355; SER-357; SER-358; ASP-360; MET-370; CYS-402 AND PHE-407.

Entry informationi

Entry nameiSTALP_HUMAN
AccessioniPrimary (citable) accession number: Q96FJ0
Secondary accession number(s): B3KPA7
, Q5T9N4, Q5T9N9, Q7Z420, Q9P2H4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2005
Last sequence update: November 23, 2004
Last modified: September 3, 2014
This is version 103 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 10
    Human chromosome 10: 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. Peptidase families
    Classification of peptidase families and list of entries
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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