Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q96FJ0 (STALP_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 102. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
AMSH-like protease

Short name=AMSH-LP
EC=3.4.19.-
Alternative name(s):
STAM-binding protein-like 1
Gene names
Name:STAMBPL1
Synonyms:AMSHLP, KIAA1373
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length436 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Zinc metalloprotease that specifically cleaves 'Lys-63'-linked polyubiquitin chains. Does not cleave 'Lys-48'-linked polyubiquitin chains. Ref.9

Cofactor

Binds 2 zinc ions per subunit. Ref.9

Tissue specificity

Ubiquitously expressed. Ref.1

Domain

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

Sequence similarities

Belongs to the peptidase M67C family.

Contains 1 MPN (JAB/Mov34) domain.

Sequence caution

The sequence BAA92611.1 differs from that shown. Reason: Erroneous initiation.

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

Binary interactions

With

Entry

#Exp.

IntAct

Notes

RNF32Q9H0A62EBI-745021,EBI-724829

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q96FJ0-1)

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.
Isoform 2 (identifier: Q96FJ0-2)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 436436AMSH-like protease
PRO_0000194874

Regions

Domain264 – 373110MPN
Motif347 – 36014JAMM motif

Sites

Metal binding3471Zinc 1; catalytic
Metal binding3491Zinc 1; catalytic
Metal binding3601Zinc 1; catalytic
Metal binding3621Zinc 2
Metal binding4021Zinc 2
Metal binding4081Zinc 2
Metal binding4101Zinc 2
Site2921Indirect zinc-binding

Amino acid modifications

Modified residue11N-acetylmethionine Ref.8
Modified residue251Phosphoserine Ref.7
Modified residue2421Phosphoserine Ref.7

Natural variations

Alternative sequence420 – 43617CKHVL…VLDLR → QKFLSGIISGTALEMEPLKI GYGPNGFPLLGISRSSSPSE QL in isoform 2.
VSP_014648
Natural variant1961S → N.
Corresponds to variant rs12254856 [ dbSNP | Ensembl ].
VAR_051817
Natural variant2041E → K.
Corresponds to variant rs34270879 [ dbSNP | Ensembl ].
VAR_051818
Natural variant2101A → T.
Corresponds to variant rs9988723 [ dbSNP | Ensembl ].
VAR_051819

Experimental info

Mutagenesis2921E → A: Complete loss of catalytic activity. Ref.9
Mutagenesis3291E → A: 3-fold decrease in substrate affinity. Ref.9
Mutagenesis3321F → A: 12-fold decrease in substrate affinity, little effect on catalytic activity. Ref.9
Mutagenesis3531T → A: 19-fold decrease in activity, no change in substrate affinity. Ref.9
Mutagenesis3551F → A: 161-fold decrease in activity, no change in substrate affinity. Ref.9
Mutagenesis3571S → A: 34-fold decrease in activity. Ref.9
Mutagenesis3581S → A: 10-fold decrease in activity, no change in substrate affinity. Ref.9
Mutagenesis3601D → A: Complete loss of catalytic activity. Ref.9
Mutagenesis3701M → A: 18-fold decrease in substrate affinity, little effect on catalytic activity. Ref.9
Mutagenesis4021C → S: 402-fold decrease in activity, slight increase in substrate affinity. Ref.9
Mutagenesis4071F → A: 35-fold decrease in activity, slight increase in substrate affinity. Ref.9

Secondary structure

................................... 436
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 23, 2004. Version 2.
Checksum: 722662C76A734102

FASTA43649,783
        10         20         30         40         50         60 
MDQPFTVNSL KKLAAMPDHT DVSLSPEERV RALSKLGCNI TISEDITPRR YFRSGVEMER 

        70         80         90        100        110        120 
MASVYLEEGN LENAFVLYNK FITLFVEKLP NHRDYQQCAV PEKQDIMKKL KEIAFPRTDE 

       130        140        150        160        170        180 
LKNDLLKKYN VEYQEYLQSK NKYKAEILKK LEHQRLIEAE RKRIAQMRQQ QLESEQFLFF 

       190        200        210        220        230        240 
EDQLKKQELA RGQMRSQQTS GLSEQIDGSA LSCFSTHQNN SLLNVFADQP NKSDATNYAS 

       250        260        270        280        290        300 
HSPPVNRALT PAATLSAVQN LVVEGLRCVV LPEDLCHKFL QLAESNTVRG IETCGILCGK 

       310        320        330        340        350        360 
LTHNEFTITH VIVPKQSAGP DYCDMENVEE LFNVQDQHDL LTLGWIHTHP TQTAFLSSVD 

       370        380        390        400        410        420 
LHTHCSYQLM LPEAIAIVCS PKHKDTGIFR LTNAGMLEVS ACKKKGFHPH TKEPRLFSIC 

       430 
KHVLVKDIKI IVLDLR 

« Hide

Isoform 2 [UniParc].

Checksum: 266828EB12055970
Show »

FASTA46152,199

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25 AND SER-242, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[8]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
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.
[10]Erratum
Sato Y., Yoshikawa A., Yamagata A., Mimura H., Yamashita M., Ookata K., Nureki O., Iwai K., Komada M., Fukai S.
Nature 456:274-274(2008)
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS7391.1. [Q96FJ0-1]
RefSeqNP_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]
UniGeneHs.16229.
Hs.701879.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2ZNRX-ray1.20A264-436[»]
2ZNVX-ray1.60A/D264-436[»]
ProteinModelPortalQ96FJ0.
SMRQ96FJ0. Positions 18-136, 263-436.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid121614. 16 interactions.
IntActQ96FJ0. 13 interactions.
MINTMINT-1444179.
STRING9606.ENSP00000360992.

Protein family/group databases

MEROPSM67.003.

PTM databases

PhosphoSiteQ96FJ0.

Polymorphism databases

DMDM71153542.

Proteomic databases

MaxQBQ96FJ0.
PaxDbQ96FJ0.
PRIDEQ96FJ0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000371924; ENSP00000360992; ENSG00000138134. [Q96FJ0-1]
ENST00000371926; ENSP00000360994; ENSG00000138134. [Q96FJ0-1]
ENST00000371927; ENSP00000360995; ENSG00000138134. [Q96FJ0-2]
GeneID57559.
KEGGhsa:57559.
UCSCuc001kfk.4. human. [Q96FJ0-1]
uc010qmx.2. human. [Q96FJ0-2]

Organism-specific databases

CTD57559.
GeneCardsGC10P090630.
H-InvDBHIX0009014.
HGNCHGNC:24105. STAMBPL1.
HPAHPA040202.
MIM612352. gene.
neXtProtNX_Q96FJ0.
PharmGKBPA142670864.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1310.
HOGENOMHOG000195792.
HOVERGENHBG058519.
KOK11867.
OMADLCHKFL.
OrthoDBEOG7NW698.
PhylomeDBQ96FJ0.
TreeFamTF323215.

Gene expression databases

ArrayExpressQ96FJ0.
BgeeQ96FJ0.
CleanExHS_STAMBPL1.
GenevestigatorQ96FJ0.

Family and domain databases

InterProIPR000555. JAMM/MPN+_dom.
IPR015063. USP8_dimer.
[Graphical view]
PfamPF01398. JAB. 1 hit.
PF08969. USP8_dimer. 1 hit.
[Graphical view]
SMARTSM00232. JAB_MPN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSTAMBPL1. human.
EvolutionaryTraceQ96FJ0.
GeneWikiSTAMBPL1.
GenomeRNAi57559.
NextBio64054.
PROQ96FJ0.
SOURCESearch...

Entry information

Entry nameSTALP_HUMAN
AccessionPrimary (citable) accession number: Q96FJ0
Secondary accession number(s): B3KPA7 expand/collapse secondary AC list , Q5T9N4, Q5T9N9, Q7Z420, Q9P2H4
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2005
Last sequence update: November 23, 2004
Last modified: July 9, 2014
This is version 102 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 10

Human chromosome 10: entries, gene names and cross-references to MIM