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Q9H9J4

- UBP42_HUMAN

UniProt

Q9H9J4 - UBP42_HUMAN

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Protein

Ubiquitin carboxyl-terminal hydrolase 42

Gene

USP42

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

Functioni

Deubiquitinating enzyme which may play an important role during spermatogenesis.By similarity

Catalytic activityi

Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei120 – 1201NucleophilePROSITE-ProRule annotation
Active sitei371 – 3711Proton acceptorPROSITE-ProRule annotation

GO - Molecular functioni

  1. ubiquitin-specific protease activity Source: FlyBase

GO - Biological processi

  1. cell differentiation Source: UniProtKB-KW
  2. protein deubiquitination Source: UniProtKB
  3. spermatogenesis Source: UniProtKB-KW
  4. ubiquitin-dependent protein catabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Thiol protease

Keywords - Biological processi

Differentiation, Spermatogenesis, Ubl conjugation pathway

Protein family/group databases

MEROPSiC19.048.

Names & Taxonomyi

Protein namesi
Recommended name:
Ubiquitin carboxyl-terminal hydrolase 42 (EC:3.4.19.12)
Alternative name(s):
Deubiquitinating enzyme 42
Ubiquitin thioesterase 42
Ubiquitin-specific-processing protease 42
Gene namesi
Name:USP42
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 7

Organism-specific databases

HGNCiHGNC:20068. USP42.

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134902515.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 13241324Ubiquitin carboxyl-terminal hydrolase 42PRO_0000080672Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei856 – 8561Phosphoserine4 Publications
Modified residuei1226 – 12261Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9H9J4.
PaxDbiQ9H9J4.
PRIDEiQ9H9J4.

PTM databases

PhosphoSiteiQ9H9J4.

Miscellaneous databases

PMAP-CutDBQ9H9J4.

Expressioni

Tissue specificityi

Broadly expressed.1 Publication

Gene expression databases

BgeeiQ9H9J4.
CleanExiHS_USP42.
ExpressionAtlasiQ9H9J4. baseline and differential.
GenevestigatoriQ9H9J4.

Organism-specific databases

HPAiHPA006752.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
TP53P046372EBI-2513638,EBI-366083

Protein-protein interaction databases

BioGridi123904. 30 interactions.
IntActiQ9H9J4. 27 interactions.
MINTiMINT-7899498.
STRINGi9606.ENSP00000301962.

Structurei

3D structure databases

ProteinModelPortaliQ9H9J4.
SMRiQ9H9J4. Positions 111-409.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini111 – 412302USPAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi742 – 937196Pro-richAdd
BLAST
Compositional biasi946 – 1118173Arg-richAdd
BLAST
Compositional biasi1176 – 124671Lys-richAdd
BLAST

Sequence similaritiesi

Belongs to the peptidase C19 family.Curated
Contains 1 USP domain.Curated

Phylogenomic databases

eggNOGiCOG5533.
GeneTreeiENSGT00760000119279.
HOGENOMiHOG000236355.
HOVERGENiHBG080724.
InParanoidiQ9H9J4.
KOiK11855.
OMAiGKLMPAP.
OrthoDBiEOG72VH5K.
PhylomeDBiQ9H9J4.
TreeFamiTF315281.

Family and domain databases

InterProiIPR018200. Pept_C19ubi-hydrolase_C_CS.
IPR001394. Peptidase_C19_UCH.
IPR028889. UCH/PAN2.
[Graphical view]
PfamiPF00443. UCH. 1 hit.
[Graphical view]
PROSITEiPS00972. USP_1. 1 hit.
PS00973. USP_2. 1 hit.
PS50235. USP_3. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9H9J4-1) [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
MTIVDKASES SDPSAYQNQP GSSEAVSPGD MDAGSASWGA VSSLNDVSNH
60 70 80 90 100
TLSLGPVPGA VVYSSSSVPD KSKPSPQKDQ ALGDGIAPPQ KVLFPSEKIC
110 120 130 140 150
LKWQQTHRVG AGLQNLGNTC FANAALQCLT YTPPLANYML SHEHSKTCHA
160 170 180 190 200
EGFCMMCTMQ AHITQALSNP GDVIKPMFVI NEMRRIARHF RFGNQEDAHE
210 220 230 240 250
FLQYTVDAMQ KACLNGSNKL DRHTQATTLV CQIFGGYLRS RVKCLNCKGV
260 270 280 290 300
SDTFDPYLDI TLEIKAAQSV NKALEQFVKP EQLDGENSYK CSKCKKMVPA
310 320 330 340 350
SKRFTIHRSS NVLTLSLKRF ANFTGGKIAK DVKYPEYLDI RPYMSQPNGE
360 370 380 390 400
PIVYVLYAVL VHTGFNCHAG HYFCYIKASN GLWYQMNDSI VSTSDIRSVL
410 420 430 440 450
SQQAYVLFYI RSHDVKNGGE LTHPTHSPGQ SSPRPVISQR VVTNKQAAPG
460 470 480 490 500
FIGPQLPSHM IKNPPHLNGT GPLKDTPSSS MSSPNGNSSV NRASPVNASA
510 520 530 540 550
SVQNWSVNRS SVIPEHPKKQ KITISIHNKL PVRQCQSQPN LHSNSLENPT
560 570 580 590 600
KPVPSSTITN SAVQSTSNAS TMSVSSKVTK PIPRSESCSQ PVMNGKSKLN
610 620 630 640 650
SSVLVPYGAE SSEDSDEESK GLGKENGIGT IVSSHSPGQD AEDEEATPHE
660 670 680 690 700
LQEPMTLNGA NSADSDSDPK ENGLAPDGAS CQGQPALHSE NPFAKANGLP
710 720 730 740 750
GKLMPAPLLS LPEDKILETF RLSNKLKGST DEMSAPGAER GPPEDRDAEP
760 770 780 790 800
QPGSPAAESL EEPDAAAGLS STKKAPPPRD PGTPATKEGA WEAMAVAPEE
810 820 830 840 850
PPPSAGEDIV GDTAPPDLCD PGSLTGDASP LSQDAKGMIA EGPRDSALAE
860 870 880 890 900
APEGLSPAPP ARSEEPCEQP LLVHPSGDHA RDAQDPSQSL GAPEAAERPP
910 920 930 940 950
APVLDMAPAG HPEGDAEPSP GERVEDAAAP KAPGPSPAKE KIGSLRKVDR
960 970 980 990 1000
GHYRSRRERS SSGEPARESR SKTEGHRHRR RRTCPRERDR QDRHAPEHHP
1010 1020 1030 1040 1050
GHGDRLSPGE RRSLGRCSHH HSRHRSGVEL DWVRHHYTEG ERGWGREKFY
1060 1070 1080 1090 1100
PDRPRWDRCR YYHDRYALYA ARDWKPFHGG REHERAGLHE RPHKDHNRGR
1110 1120 1130 1140 1150
RGCEPARERE RHRPSSPRAG APHALAPHPD RFSHDRTALV AGDNCNLSDR
1160 1170 1180 1190 1200
FHEHENGKSR KRRHDSVENS DSHVEKKARR SEQKDPLEEP KAKKHKKSKK
1210 1220 1230 1240 1250
KKKSKDKHRD RDSRHQQDSD LSAACSDADL HRHKKKKKKK KRHSRKSEDF
1260 1270 1280 1290 1300
VKDSELHLPR VTSLETVAQF RRAQGGFPLS GGPPLEGVGP FREKTKHLRM
1310 1320
ESRDDRCRLF EYGQGKRRYL ELGR
Length:1,324
Mass (Da):145,392
Last modified:February 8, 2011 - v3
Checksum:i6EB4975521ABF516
GO
Isoform 2 (identifier: Q9H9J4-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1316-1324: KRRYLELGR → D

Show »
Length:1,316
Mass (Da):144,335
Checksum:i28998E673C8EFE3B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti655 – 6551M → T in CAE53097. (PubMed:14715245)Curated
Sequence conflicti655 – 6551M → T in BAB14232. (PubMed:14702039)Curated
Sequence conflicti1214 – 12141R → RR in CAE53097. (PubMed:14715245)Curated
Sequence conflicti1217 – 12171Q → R in AAT67238. (PubMed:15489334)Curated
Sequence conflicti1294 – 12941K → E in AAT67238. (PubMed:15489334)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti1030 – 10301L → P.
Corresponds to variant rs6463529 [ dbSNP | Ensembl ].
VAR_059754

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1316 – 13249KRRYLELGR → D in isoform 2. 1 PublicationVSP_040529

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ601395 mRNA. Translation: CAE53097.1.
AY618868 mRNA. Translation: AAT67238.1.
AC004895 Genomic DNA. No translation available.
BC060846 mRNA. Translation: AAH60846.2.
BC132862 mRNA. Translation: AAI32863.1.
AK022759 mRNA. Translation: BAB14232.1.
CCDSiCCDS47535.1. [Q9H9J4-2]
RefSeqiNP_115548.1. NM_032172.2. [Q9H9J4-2]
XP_005249939.1. XM_005249882.2. [Q9H9J4-1]
UniGeneiHs.31856.

Genome annotation databases

EnsembliENST00000306177; ENSP00000301962; ENSG00000106346. [Q9H9J4-2]
GeneIDi84132.
KEGGihsa:84132.
UCSCiuc011jwo.1. human. [Q9H9J4-1]
uc011jwp.2. human. [Q9H9J4-2]

Polymorphism databases

DMDMi322510098.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ601395 mRNA. Translation: CAE53097.1 .
AY618868 mRNA. Translation: AAT67238.1 .
AC004895 Genomic DNA. No translation available.
BC060846 mRNA. Translation: AAH60846.2 .
BC132862 mRNA. Translation: AAI32863.1 .
AK022759 mRNA. Translation: BAB14232.1 .
CCDSi CCDS47535.1. [Q9H9J4-2 ]
RefSeqi NP_115548.1. NM_032172.2. [Q9H9J4-2 ]
XP_005249939.1. XM_005249882.2. [Q9H9J4-1 ]
UniGenei Hs.31856.

3D structure databases

ProteinModelPortali Q9H9J4.
SMRi Q9H9J4. Positions 111-409.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 123904. 30 interactions.
IntActi Q9H9J4. 27 interactions.
MINTi MINT-7899498.
STRINGi 9606.ENSP00000301962.

Protein family/group databases

MEROPSi C19.048.

PTM databases

PhosphoSitei Q9H9J4.

Polymorphism databases

DMDMi 322510098.

Proteomic databases

MaxQBi Q9H9J4.
PaxDbi Q9H9J4.
PRIDEi Q9H9J4.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000306177 ; ENSP00000301962 ; ENSG00000106346 . [Q9H9J4-2 ]
GeneIDi 84132.
KEGGi hsa:84132.
UCSCi uc011jwo.1. human. [Q9H9J4-1 ]
uc011jwp.2. human. [Q9H9J4-2 ]

Organism-specific databases

CTDi 84132.
GeneCardsi GC07P006144.
H-InvDB HIX0006462.
HGNCi HGNC:20068. USP42.
HPAi HPA006752.
neXtProti NX_Q9H9J4.
PharmGKBi PA134902515.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5533.
GeneTreei ENSGT00760000119279.
HOGENOMi HOG000236355.
HOVERGENi HBG080724.
InParanoidi Q9H9J4.
KOi K11855.
OMAi GKLMPAP.
OrthoDBi EOG72VH5K.
PhylomeDBi Q9H9J4.
TreeFami TF315281.

Miscellaneous databases

ChiTaRSi USP42. human.
GeneWikii USP42.
GenomeRNAii 84132.
NextBioi 73425.
PMAP-CutDB Q9H9J4.
PROi Q9H9J4.

Gene expression databases

Bgeei Q9H9J4.
CleanExi HS_USP42.
ExpressionAtlasi Q9H9J4. baseline and differential.
Genevestigatori Q9H9J4.

Family and domain databases

InterProi IPR018200. Pept_C19ubi-hydrolase_C_CS.
IPR001394. Peptidase_C19_UCH.
IPR028889. UCH/PAN2.
[Graphical view ]
Pfami PF00443. UCH. 1 hit.
[Graphical view ]
PROSITEi PS00972. USP_1. 1 hit.
PS00973. USP_2. 1 hit.
PS50235. USP_3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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 1), TISSUE SPECIFICITY, ENZYME ACTIVITY.
  2. "A discovery of a novel deubiquitinating enzyme human USP42."
    Baek K.-H., Yoo K.-J.
    Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  3. "The DNA sequence of human chromosome 7."
    Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
    , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
    Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
    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] (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1202 (ISOFORM 1).
    Tissue: Placenta.
  5. "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 1-1198.
  6. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1226, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-856, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-856, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  10. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-856, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-856, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiUBP42_HUMAN
AccessioniPrimary (citable) accession number: Q9H9J4
Secondary accession number(s): A2RUE3
, B5MDA5, Q0VIN8, Q3C166, Q6P9B4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 10, 2003
Last sequence update: February 8, 2011
Last modified: November 26, 2014
This is version 120 of the entry and version 3 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 7
    Human chromosome 7: 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. Peptidase families
    Classification of peptidase families and list of entries
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3