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Q70EL1 (UBP54_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 81. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | 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:
Inactive ubiquitin carboxyl-terminal hydrolase 54
Alternative name(s):
Inactive ubiquitin-specific peptidase 54
Gene names
Name:USP54
Synonyms:C10orf29
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1684 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Has no peptidase activity.

Tissue specificity

Weakly expressed in a few tissues. Ref.1

Sequence similarities

Belongs to the peptidase C19 family.

Contains 1 USP domain.

Caution

Although the active site residues are conserved, it lacks the conserved His residue which is normally found 9 residues before the catalytic His.

Sequence caution

The sequence BAC04393.1 differs from that shown. Reason: Erroneous initiation.

The sequence BAG53943.1 differs from that shown. Reason: Erroneous initiation.

The sequence BX649087 differs from that shown. Reason: Frameshift at position 508.

The sequence CAO03507.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence CAO03508.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence CAO03509.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainCoiled coil
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processubiquitin-dependent protein catabolic process

Inferred from electronic annotation. Source: InterPro

   Molecular_functionprotein binding

Inferred from physical interaction PubMed 16713569. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ATXN1P542533EBI-946185,EBI-930964

Alternative products

This entry describes 7 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q70EL1-1)

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: Q70EL1-4)

The sequence of this isoform differs from the canonical sequence as follows:
     383-403: REPSISSDTRTDSSTESYPYK → EQPGSLPLLSPHPMRSNSWDS
     404-1684: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: Q70EL1-6)

The sequence of this isoform differs from the canonical sequence as follows:
     893-893: S → R
     894-1684: Missing.
Note: No experimental confirmation available.
Isoform 4 (identifier: Q70EL1-7)

The sequence of this isoform differs from the canonical sequence as follows:
     126-275: Missing.
Note: No experimental confirmation available.
Isoform 5 (identifier: Q70EL1-8)

The sequence of this isoform differs from the canonical sequence as follows:
     1-912: Missing.
Isoform 6 (identifier: Q70EL1-9)

The sequence of this isoform differs from the canonical sequence as follows:
     1-912: Missing.
     1391-1437: Missing.
Isoform 7 (identifier: Q70EL1-10)

The sequence of this isoform differs from the canonical sequence as follows:
     1-912: Missing.
     1386-1390: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 16841684Inactive ubiquitin carboxyl-terminal hydrolase 54
PRO_0000249530

Regions

Domain31 – 352322USP
Coiled coil736 – 77035 Potential
Compositional bias559 – 57012Poly-Ser
Compositional bias866 – 8694Poly-Gln

Amino acid modifications

Modified residue6711Phosphoserine Ref.6

Natural variations

Alternative sequence1 – 912912Missing in isoform 5, isoform 6 and isoform 7.
VSP_035674
Alternative sequence126 – 275150Missing in isoform 4.
VSP_029922
Alternative sequence383 – 40321REPSI…SYPYK → EQPGSLPLLSPHPMRSNSWD S in isoform 2.
VSP_026525
Alternative sequence404 – 16841281Missing in isoform 2.
VSP_026526
Alternative sequence8931S → R in isoform 3.
VSP_035675
Alternative sequence894 – 1684791Missing in isoform 3.
VSP_035676
Alternative sequence1386 – 13905Missing in isoform 7.
VSP_035677
Alternative sequence1391 – 143747Missing in isoform 6.
VSP_035678
Natural variant5051L → V in a breast cancer sample; somatic mutation. Ref.8
VAR_036360
Natural variant9761K → E.
Corresponds to variant rs1618542 [ dbSNP | Ensembl ].
VAR_047258
Natural variant12311D → N.
Corresponds to variant rs4619071 [ dbSNP | Ensembl ].
VAR_047259
Natural variant13671G → D.
Corresponds to variant rs7083344 [ dbSNP | Ensembl ].
VAR_047260

Experimental info

Sequence conflict110 – 1112EQ → KE in BX649087. Ref.3
Sequence conflict1911C → S in CAE47747. Ref.1
Sequence conflict2261P → L in BX649087. Ref.3
Sequence conflict7331E → G in BX649087. Ref.3
Sequence conflict13451H → P in BAC04393. Ref.2
Sequence conflict14251S → P in BAC86566. Ref.2
Sequence conflict14381D → H in AAI30634. Ref.5

Sequences

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

Last modified November 25, 2008. Version 4.
Checksum: 853D9CFCB35C63C4

FASTA1,684187,388
        10         20         30         40         50         60 
MSWKRNYFSG GRGSVQGMFA PRSSTSIAPS KGLSNEPGQN SCFLNSALQV LWHLDIFRRS 

        70         80         90        100        110        120 
FRQLTTHKCM GDSCIFCALK GIFNQFQCSS EKVLPSDTLR SALAKTFQDE QRFQLGIMDD 

       130        140        150        160        170        180 
AAECFENLLM RIHFHIADET KEDICTAQHC ISHQKFAMTL FEQCVCTSCG ATSDPLPFIQ 

       190        200        210        220        230        240 
MVHYISTTSL CNQAICMLER REKPSPSMFG ELLQNASTMG DLRNCPSNCG ERIRIRRVLM 

       250        260        270        280        290        300 
NAPQIITIGL VWDSDHSDLA EDVIHSLGTC LKLGDLFFRV TDDRAKQSEL YLVGMICYYG 

       310        320        330        340        350        360 
KHYSTFFFQT KIRKWMYFDD AHVKEIGPKW KDVVTKCIKG HYQPLLLLYA DPQGTPVSTQ 

       370        380        390        400        410        420 
DLPPQAEFQS YSRTCYDSED SGREPSISSD TRTDSSTESY PYKHSHHESV VSHFSSDSQG 

       430        440        450        460        470        480 
TVIYNVENDS MSQSSRDTGH LTDSECNQKH TSKKGSLIER KRSSGRVRRK GDEPQASGYH 

       490        500        510        520        530        540 
SEGETLKEKQ APRNASKPSS STNRLRDFKE TVSNMIHNRP SLASQTNVGS HCRGRGGDQP 

       550        560        570        580        590        600 
DKKPPRTLPL HSRDWEIEST SSESKSSSSS KYRPTWRPKR ESLNIDSIFS KDKRKHCGYT 

       610        620        630        640        650        660 
QLSPFSEDSA KEFIPDEPSK PPSYDIKFGG PSPQYKRWGP ARPGSHLLEQ HPRLIQRMES 

       670        680        690        700        710        720 
GYESSERNSS SPVSLDAALP ESSNVYRDPS AKRSAGLVPS WRHIPKSHSS SILEVDSTAS 

       730        740        750        760        770        780 
MGGWTKSQPF SGEEISSKSE LDELQEEVAR RAQEQELRRK REKELEAAKG FNPHPSRFMD 

       790        800        810        820        830        840 
LDELQNQGRS DGFERSLQEA ESVFEESLHL EQKGDCAAAL ALCNEAISKL RLALHGASCS 

       850        860        870        880        890        900 
THSRALVDKK LQISIRKARS LQDRMQQQQS PQQPSQPSAC LPTQAGTLSQ PTSEQPIPLQ 

       910        920        930        940        950        960 
VLLSQEAQLE SGMDTEFGAS SFFHSPASCH ESHSSLSPES SAPQHSSPSR SALKLLTSVE 

       970        980        990       1000       1010       1020 
VDNIEPSAFH RQGLPKAPGW TEKNSHHSWE PLDAPEGKLQ GSRCDNSSCS KLPPQEGRGI 

      1030       1040       1050       1060       1070       1080 
AQEQLFQEKK DPANPSPVMP GIATSERGDE HSLGCSPSNS SAQPSLPLYR TCHPIMPVAS 

      1090       1100       1110       1120       1130       1140 
SFVLHCPDPV QKTNQCLQGQ SLKTSLTLKV DRGSEETYRP EFPSTKGLVR SLAEQFQRMQ 

      1150       1160       1170       1180       1190       1200 
GVSMRDSTGF KDRSLSGSLR KNSSPSDSKP PFSQGQEKGH WPWAKQQSSL EGGDRPLSWE 

      1210       1220       1230       1240       1250       1260 
ESTEHSSLAL NSGLPNGETS SGGQPRLAEP DIYQEKLSQV RDVRSKDLGS STDLGTSLPL 

      1270       1280       1290       1300       1310       1320 
DSWVNITRFC DSQLKHGAPR PGMKSSPHDS HTCVTYPERN HILLHPHWNQ DTEQETSELE 

      1330       1340       1350       1360       1370       1380 
SLYQASLQAS QAGCSGWGQQ DTAWHPLSQT GSADGMGRRL HSAHDPGLSK TSTAEMEHGL 

      1390       1400       1410       1420       1430       1440 
HEARTVRTSQ ATPCRGLSRE CGEDEQYSAE NLRRISRSLS GTVVSEREEA PVSSHSFDSS 

      1450       1460       1470       1480       1490       1500 
NVRKPLETGH RCSSSSSLPV IHDPSVFLLG PQLYLPQPQF LSPDVLMPTM AGEPNRLPGT 

      1510       1520       1530       1540       1550       1560 
SRSVQQFLAM CDRGETSQGA KYTGRTLNYQ SLPHRSRTDN SWAPWSETNQ HIGTRFLTTP 

      1570       1580       1590       1600       1610       1620 
GCNPQLTYTA TLPERSKGLQ VPHTQSWSDL FHSPSHPPIV HPVYPPSSSL HVPLRSAWNS 

      1630       1640       1650       1660       1670       1680 
DPVPGSRTPG PRRVDMPPDD DWRQSSYASH SGHRRTVGEG FLFVLSDAPR REQIRARVLQ 


HSQW 

« Hide

Isoform 2 [UniParc].

Checksum: 2749CBBCC8AF37A9
Show »

FASTA40345,703
Isoform 3 [UniParc].

Checksum: 7D1C84A450FEB447
Show »

FASTA893100,476
Isoform 4 [UniParc].

Checksum: B00DC48D0DE75BC3
Show »

FASTA1,534170,581
Isoform 5 [UniParc].

Checksum: A41B0ACF854B4AF2
Show »

FASTA77284,938
Isoform 6 [UniParc].

Checksum: 98EFA86D1005C89F
Show »

FASTA72579,771
Isoform 7 [UniParc].

Checksum: C622D8C5CE11DDF3
Show »

FASTA76784,366

References

« Hide 'large scale' references
[1]"Cloning and enzymatic analysis of 22 novel human ubiquitin-specific proteases."
Quesada V., Diaz-Perales A., Gutierrez-Fernandez A., Garabaya C., Cal S., Lopez-Otin C.
Biochem. Biophys. Res. Commun. 314:54-62(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), LACK OF ENZYME ACTIVITY, TISSUE SPECIFICITY.
[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. 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] (ISOFORMS 5; 6 AND 7).
Tissue: Amygdala, Hippocampus, Lung and Uterus.
[3]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
Tissue: Fetal liver.
[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]"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 6).
Tissue: Skin.
[6]"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-671, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[7]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[8]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] VAL-505.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ583820 mRNA. Translation: CAE47747.1.
AK094637 mRNA. Translation: BAC04393.1. Different initiation.
AK123711 mRNA. Translation: BAG53943.1. Different initiation.
AK126497 mRNA. Translation: BAC86566.1.
AK127213 mRNA. Translation: BAC86886.1.
AK127267 mRNA. Translation: BAC86907.1.
BX649087 mRNA. No translation available.
AC073389 Genomic DNA. No translation available.
AL359074 Genomic DNA. Translation: CAO03506.1.
AL359074 Genomic DNA. Translation: CAO03507.1. Sequence problems.
AL359074 Genomic DNA. Translation: CAO03508.1. Sequence problems.
AL359074 Genomic DNA. Translation: CAO03509.1. Sequence problems.
BC064967 mRNA. Translation: AAH64967.1.
BC130633 mRNA. Translation: AAI30634.1.
CCDSCCDS7329.2. [Q70EL1-1]
RefSeqNP_689799.3. NM_152586.3. [Q70EL1-1]
UniGeneHs.657355.

3D structure databases

ProteinModelPortalQ70EL1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid127739. 10 interactions.
IntActQ70EL1. 20 interactions.
MINTMINT-6946944.

Protein family/group databases

MEROPSC19.080.

Polymorphism databases

DMDM215274237.

Proteomic databases

MaxQBQ70EL1.
PaxDbQ70EL1.
PRIDEQ70EL1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000339859; ENSP00000345216; ENSG00000166348. [Q70EL1-1]
ENST00000394811; ENSP00000378290; ENSG00000166348. [Q70EL1-9]
ENST00000408019; ENSP00000386080; ENSG00000166348. [Q70EL1-1]
ENST00000428547; ENSP00000408714; ENSG00000166348. [Q70EL1-7]
GeneID159195.
KEGGhsa:159195.
UCSCuc001juk.3. human. [Q70EL1-8]
uc001jul.3. human. [Q70EL1-9]
uc001juo.3. human. [Q70EL1-1]
uc001jup.3. human. [Q70EL1-6]

Organism-specific databases

CTD159195.
GeneCardsGC10M075257.
HGNCHGNC:23513. USP54.
HPAHPA047663.
neXtProtNX_Q70EL1.
PharmGKBPA134959960.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG291259.
HOVERGENHBG108646.
InParanoidQ70EL1.
OMANCGERIR.
PhylomeDBQ70EL1.
TreeFamTF336130.

Gene expression databases

ArrayExpressQ70EL1.
BgeeQ70EL1.
CleanExHS_USP54.
GenevestigatorQ70EL1.

Family and domain databases

Gene3D1.20.58.280. 1 hit.
InterProIPR007330. MIT.
IPR001394. Peptidase_C19_UCH.
IPR028889. UCH/PAN2.
[Graphical view]
PfamPF00443. UCH. 1 hit.
[Graphical view]
PROSITEPS50235. USP_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSUSP54. human.
GenomeRNAi159195.
NextBio87894.
PROQ70EL1.

Entry information

Entry nameUBP54_HUMAN
AccessionPrimary (citable) accession number: Q70EL1
Secondary accession number(s): A1L4Q4 expand/collapse secondary AC list , A3KFK3, A3KFK5, A3KFK6, A3KFK7, A6PVS4, A6PVS5, A6PVS6, A6PVS7, B3KVY1, B9ZVM1, Q5F2F4, Q6P1N6, Q6ZSP1, Q6ZSR1, Q6ZTM0, Q8N1X2
Entry history
Integrated into UniProtKB/Swiss-Prot: September 19, 2006
Last sequence update: November 25, 2008
Last modified: July 9, 2014
This is version 81 of the entry and version 4 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

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