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O00232

- PSD12_HUMAN

UniProt

O00232 - PSD12_HUMAN

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Protein
26S proteasome non-ATPase regulatory subunit 12
Gene
PSMD12
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Acts as a regulatory subunit of the 26S proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins.

GO - Biological processi

  1. DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest Source: Reactome
  2. G1/S transition of mitotic cell cycle Source: Reactome
  3. RNA metabolic process Source: Reactome
  4. anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process Source: Reactome
  5. antigen processing and presentation of exogenous peptide antigen via MHC class I Source: Reactome
  6. antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent Source: Reactome
  7. antigen processing and presentation of peptide antigen via MHC class I Source: Reactome
  8. apoptotic process Source: Reactome
  9. cellular nitrogen compound metabolic process Source: Reactome
  10. gene expression Source: Reactome
  11. mRNA metabolic process Source: Reactome
  12. mitotic cell cycle Source: Reactome
  13. negative regulation of apoptotic process Source: Reactome
  14. negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome
  15. positive regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome
  16. protein polyubiquitination Source: Reactome
  17. regulation of apoptotic process Source: Reactome
  18. regulation of cellular amino acid metabolic process Source: Reactome
  19. regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome
  20. small molecule metabolic process Source: Reactome
  21. viral process Source: Reactome
Complete GO annotation...

Enzyme and pathway databases

ReactomeiREACT_111056. Cross-presentation of soluble exogenous antigens (endosomes).
REACT_111178. ER-Phagosome pathway.
REACT_1156. Orc1 removal from chromatin.
REACT_118656. Activation of NF-kappaB in B cells.
REACT_1221. CDK-mediated phosphorylation and removal of Cdc6.
REACT_13464. Regulation of activated PAK-2p34 by proteasome mediated degradation.
REACT_13565. Regulation of ornithine decarboxylase (ODC).
REACT_150471. Separation of Sister Chromatids.
REACT_1614. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
REACT_172638. Asymmetric localization of PCP proteins.
REACT_1949. CDT1 association with the CDC6:ORC:origin complex.
REACT_200766. degradation of AXIN.
REACT_200841. degradation of DVL.
REACT_20549. Autodegradation of the E3 ubiquitin ligase COP1.
REACT_25325. AUF1 (hnRNP D0) destabilizes mRNA.
REACT_4. Ubiquitin-dependent degradation of Cyclin D1.
REACT_6761. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
REACT_6785. Autodegradation of Cdh1 by Cdh1:APC/C.
REACT_6821. SCF-beta-TrCP mediated degradation of Emi1.
REACT_6871. APC/C:Cdc20 mediated degradation of Securin.
REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
REACT_9003. SCF(Skp2)-mediated degradation of p27/p21.
REACT_9031. Vpu mediated degradation of CD4.
REACT_9453. Vif-mediated degradation of APOBEC3G.

Names & Taxonomyi

Protein namesi
Recommended name:
26S proteasome non-ATPase regulatory subunit 12
Alternative name(s):
26S proteasome regulatory subunit RPN5
26S proteasome regulatory subunit p55
Gene namesi
Name:PSMD12
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 17

Organism-specific databases

HGNCiHGNC:9557. PSMD12.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. extracellular vesicular exosome Source: UniProt
  3. nucleoplasm Source: Reactome
  4. proteasome accessory complex Source: UniProtKB
  5. proteasome regulatory particle Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Proteasome

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA33903.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 45645526S proteasome non-ATPase regulatory subunit 12
PRO_0000173861Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine2 Publications
Modified residuei221 – 2211N6-acetyllysine1 Publication
Modified residuei368 – 3681N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiO00232.
PaxDbiO00232.
PeptideAtlasiO00232.
PRIDEiO00232.

PTM databases

PhosphoSiteiO00232.

Expressioni

Gene expression databases

ArrayExpressiO00232.
BgeeiO00232.
CleanExiHS_PSMD12.
GenevestigatoriO00232.

Organism-specific databases

HPAiHPA023119.

Interactioni

Subunit structurei

Component of the PA700 complex.

Protein-protein interaction databases

BioGridi111690. 69 interactions.
DIPiDIP-27549N.
IntActiO00232. 22 interactions.
MINTiMINT-5003729.
STRINGi9606.ENSP00000348442.

Structurei

3D structure databases

ProteinModelPortaliO00232.
SMRiO00232. Positions 44-455.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini237 – 417181PCI
Add
BLAST

Sequence similaritiesi

Contains 1 PCI domain.

Phylogenomic databases

eggNOGiCOG5071.
HOGENOMiHOG000194265.
HOVERGENiHBG053739.
InParanoidiO00232.
KOiK03035.
OMAiDNEQSDM.
OrthoDBiEOG7SJD4B.
PhylomeDBiO00232.
TreeFamiTF105721.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
InterProiIPR000717. PCI_dom.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF01399. PCI. 1 hit.
[Graphical view]
SMARTiSM00088. PINT. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: O00232-1) [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

MADGGSERAD GRIVKMEVDY SATVDQRLPE CAKLAKEGRL QEVIETLLSL    50
EKQTRTASDM VSTSRILVAV VKMCYEAKEW DLLNENIMLL SKRRSQLKQA 100
VAKMVQQCCT YVEEITDLPI KLRLIDTLRM VTEGKIYVEI ERARLTKTLA 150
TIKEQNGDVK EAASILQELQ VETYGSMEKK ERVEFILEQM RLCLAVKDYI 200
RTQIISKKIN TKFFQEENTE KLKLKYYNLM IQLDQHEGSY LSICKHYRAI 250
YDTPCIQAES EKWQQALKSV VLYVILAPFD NEQSDLVHRI SGDKKLEEIP 300
KYKDLLKLFT TMELMRWSTL VEDYGMELRK GSLESPATDV FGSTEEGEKR 350
WKDLKNRVVE HNIRIMAKYY TRITMKRMAQ LLDLSVDESE AFLSNLVVNK 400
TIFAKVDRLA GIINFQRPKD PNNLLNDWSQ KLNSLMSLVN KTTHLIAKEE 450
MIHNLQ 456
Length:456
Mass (Da):52,904
Last modified:January 23, 2007 - v3
Checksum:i97D0BDBDB0C96195
GO
Isoform 2 (identifier: O00232-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     37-56: Missing.

Note: No experimental confirmation available.

Show »
Length:436
Mass (Da):50,579
Checksum:i01DCBC0BF3EC3718
GO

Sequence cautioni

The sequence AAH65826.1 differs from that shown. Reason: Erroneous initiation.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti358 – 3581V → A.
Corresponds to variant rs2230680 [ dbSNP | Ensembl ].
VAR_051558

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei37 – 5620Missing in isoform 2.
VSP_042718Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti300 – 3001P → S in BAD96399. 1 Publication
Sequence conflicti398 – 3981V → D in BAD96399. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB003103 mRNA. Translation: BAA19749.1.
AK091198 mRNA. Translation: BAG52303.1.
AK222679 mRNA. Translation: BAD96399.1.
AC110921 Genomic DNA. No translation available.
CH471099 Genomic DNA. Translation: EAW89028.1.
BC019062 mRNA. Translation: AAH19062.1.
BC065826 mRNA. Translation: AAH65826.1. Different initiation.
CCDSiCCDS11669.1. [O00232-1]
CCDS11670.1. [O00232-2]
PIRiPC6501. JC6523.
RefSeqiNP_002807.1. NM_002816.3. [O00232-1]
NP_777360.1. NM_174871.2. [O00232-2]
UniGeneiHs.592689.

Genome annotation databases

EnsembliENST00000356126; ENSP00000348442; ENSG00000197170. [O00232-1]
ENST00000357146; ENSP00000349667; ENSG00000197170. [O00232-2]
GeneIDi5718.
KEGGihsa:5718.
UCSCiuc002jfy.3. human. [O00232-1]
uc002jga.3. human. [O00232-2]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB003103 mRNA. Translation: BAA19749.1 .
AK091198 mRNA. Translation: BAG52303.1 .
AK222679 mRNA. Translation: BAD96399.1 .
AC110921 Genomic DNA. No translation available.
CH471099 Genomic DNA. Translation: EAW89028.1 .
BC019062 mRNA. Translation: AAH19062.1 .
BC065826 mRNA. Translation: AAH65826.1 . Different initiation.
CCDSi CCDS11669.1. [O00232-1 ]
CCDS11670.1. [O00232-2 ]
PIRi PC6501. JC6523.
RefSeqi NP_002807.1. NM_002816.3. [O00232-1 ]
NP_777360.1. NM_174871.2. [O00232-2 ]
UniGenei Hs.592689.

3D structure databases

ProteinModelPortali O00232.
SMRi O00232. Positions 44-455.
ModBasei Search...

Protein-protein interaction databases

BioGridi 111690. 69 interactions.
DIPi DIP-27549N.
IntActi O00232. 22 interactions.
MINTi MINT-5003729.
STRINGi 9606.ENSP00000348442.

PTM databases

PhosphoSitei O00232.

Proteomic databases

MaxQBi O00232.
PaxDbi O00232.
PeptideAtlasi O00232.
PRIDEi O00232.

Protocols and materials databases

DNASUi 5718.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000356126 ; ENSP00000348442 ; ENSG00000197170 . [O00232-1 ]
ENST00000357146 ; ENSP00000349667 ; ENSG00000197170 . [O00232-2 ]
GeneIDi 5718.
KEGGi hsa:5718.
UCSCi uc002jfy.3. human. [O00232-1 ]
uc002jga.3. human. [O00232-2 ]

Organism-specific databases

CTDi 5718.
GeneCardsi GC17M065334.
HGNCi HGNC:9557. PSMD12.
HPAi HPA023119.
MIMi 604450. gene.
neXtProti NX_O00232.
PharmGKBi PA33903.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5071.
HOGENOMi HOG000194265.
HOVERGENi HBG053739.
InParanoidi O00232.
KOi K03035.
OMAi DNEQSDM.
OrthoDBi EOG7SJD4B.
PhylomeDBi O00232.
TreeFami TF105721.

Enzyme and pathway databases

Reactomei REACT_111056. Cross-presentation of soluble exogenous antigens (endosomes).
REACT_111178. ER-Phagosome pathway.
REACT_1156. Orc1 removal from chromatin.
REACT_118656. Activation of NF-kappaB in B cells.
REACT_1221. CDK-mediated phosphorylation and removal of Cdc6.
REACT_13464. Regulation of activated PAK-2p34 by proteasome mediated degradation.
REACT_13565. Regulation of ornithine decarboxylase (ODC).
REACT_150471. Separation of Sister Chromatids.
REACT_1614. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
REACT_172638. Asymmetric localization of PCP proteins.
REACT_1949. CDT1 association with the CDC6:ORC:origin complex.
REACT_200766. degradation of AXIN.
REACT_200841. degradation of DVL.
REACT_20549. Autodegradation of the E3 ubiquitin ligase COP1.
REACT_25325. AUF1 (hnRNP D0) destabilizes mRNA.
REACT_4. Ubiquitin-dependent degradation of Cyclin D1.
REACT_6761. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
REACT_6785. Autodegradation of Cdh1 by Cdh1:APC/C.
REACT_6821. SCF-beta-TrCP mediated degradation of Emi1.
REACT_6871. APC/C:Cdc20 mediated degradation of Securin.
REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
REACT_9003. SCF(Skp2)-mediated degradation of p27/p21.
REACT_9031. Vpu mediated degradation of CD4.
REACT_9453. Vif-mediated degradation of APOBEC3G.

Miscellaneous databases

GeneWikii PSMD12.
GenomeRNAii 5718.
NextBioi 22216.
PROi O00232.
SOURCEi Search...

Gene expression databases

ArrayExpressi O00232.
Bgeei O00232.
CleanExi HS_PSMD12.
Genevestigatori O00232.

Family and domain databases

Gene3Di 1.10.10.10. 1 hit.
InterProi IPR000717. PCI_dom.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view ]
Pfami PF01399. PCI. 1 hit.
[Graphical view ]
SMARTi SM00088. PINT. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "cDNA cloning and functional analysis of p44.5 and p55, two regulatory subunits of the 26S proteasome."
    Saito A., Watanabe T.K., Shimada Y., Fujiwara T., Slaughter C.A., DeMartino G.N., Tanahashi N., Tanaka K.
    Gene 203:241-250(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  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] (ISOFORM 2).
    Tissue: Tongue.
  3. Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
    Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Brain.
  4. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
    Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
    , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
    Nature 440:1045-1049(2006) [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: Muscle and Testis.
  7. "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
    Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
    Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-12, ACETYLATION AT ALA-2.
    Tissue: Platelet.
  8. "Mass spectrometric characterization of the affinity-purified human 26S proteasome complex."
    Wang X., Chen C.-F., Baker P.R., Chen P.-L., Kaiser P., Huang L.
    Biochemistry 46:3553-3565(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  9. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-221 AND LYS-368, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiPSD12_HUMAN
AccessioniPrimary (citable) accession number: O00232
Secondary accession number(s): A6NP15, Q53HA2, Q6P053
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 15, 2002
Last sequence update: January 23, 2007
Last modified: September 3, 2014
This is version 128 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: 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

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