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Q99471

- PFD5_HUMAN

UniProt

Q99471 - PFD5_HUMAN

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Protein
Prefoldin subunit 5
Gene
PFDN5, MM1, PFD5
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Binds specifically to cytosolic chaperonin (c-CPN) and transfers target proteins to it. Binds to nascent polypeptide chain and promotes folding in an environment in which there are many competing pathways for nonnative proteins. Represses the transcriptional activity of MYC.1 Publication

GO - Molecular functioni

  1. protein binding Source: IntAct
  2. transcription corepressor activity Source: ProtInc

GO - Biological processi

  1. 'de novo' posttranslational protein folding Source: Reactome
  2. cellular protein metabolic process Source: Reactome
  3. negative regulation of canonical Wnt signaling pathway Source: BHF-UCL
  4. negative regulation of transcription, DNA-templated Source: BHF-UCL
  5. protein folding Source: Reactome
  6. regulation of transcription, DNA-templated Source: ProtInc
  7. retina development in camera-type eye Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Enzyme and pathway databases

ReactomeiREACT_16936. Prefoldin mediated transfer of substrate to CCT/TriC.

Names & Taxonomyi

Protein namesi
Recommended name:
Prefoldin subunit 5
Alternative name(s):
C-Myc-binding protein Mm-1
Myc modulator 1
Gene namesi
Name:PFDN5
Synonyms:MM1, PFD5
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 12

Organism-specific databases

HGNCiHGNC:8869. PFDN5.

Subcellular locationi

Isoform 1 : Nucleus 1 Publication
Isoform 2 : Cytoplasm 1 Publication
Isoform 3 : Nucleus 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. nucleus Source: ProtInc
  3. prefoldin complex Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA33210.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 154153Prefoldin subunit 5UniRule annotation
PRO_0000153661Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine2 Publications
Modified residuei42 – 421N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ99471.
PaxDbiQ99471.
PeptideAtlasiQ99471.
PRIDEiQ99471.

2D gel databases

OGPiQ99471.

PTM databases

PhosphoSiteiQ99471.

Expressioni

Tissue specificityi

Highly expressed in pancreas and skeletal muscle and moderately in other tissues.

Gene expression databases

BgeeiQ99471.
CleanExiHS_PFDN5.
GenevestigatoriQ99471.

Organism-specific databases

HPAiHPA008587.

Interactioni

Subunit structurei

Heterohexamer of two PFD-alpha type and four PFD-beta type subunits. Binds to MYC; interacts with its N-terminal domain.

Binary interactionsi

WithEntry#Exp.IntActNotes
vIRF-3Q9DUN18EBI-357275,EBI-1647907From a different organism.

Protein-protein interaction databases

BioGridi111226. 53 interactions.
DIPiDIP-28155N.
IntActiQ99471. 14 interactions.
MINTiMINT-5003456.
STRINGi9606.ENSP00000334188.

Structurei

3D structure databases

ProteinModelPortaliQ99471.
SMRiQ99471. Positions 11-149.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1730.
HOGENOMiHOG000207562.
HOVERGENiHBG004539.
InParanoidiQ99471.
KOiK04797.
OMAiFVECECI.
PhylomeDBiQ99471.
TreeFamiTF106509.

Family and domain databases

Gene3Di1.10.287.370. 1 hit.
HAMAPiMF_00308. PfdA.
InterProiIPR011599. PFD_alpha.
IPR009053. Prefoldin.
IPR004127. Prefoldin_subunit_alpha.
[Graphical view]
PfamiPF02996. Prefoldin. 1 hit.
[Graphical view]
SUPFAMiSSF46579. SSF46579. 1 hit.
TIGRFAMsiTIGR00293. TIGR00293. 1 hit.

Sequences (3)i

Sequence statusi: Complete.

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

This entry describes 3 isoformsi produced by alternative splicing. Align

Note: Additional isoforms seem to exist.

Isoform 1 (identifier: Q99471-1) [UniParc]FASTAAdd to Basket

Also known as: MM1-alpha

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

MAQSINITEL NLPQLEMLKN QLDQEVEFLS TSIAQLKVVQ TKYVEAKDCL    50
NVLNKSNEGK ELLVPLTSSM YVPGKLHDVE HVLIDVGTGY YVEKTAEDAK 100
DFFKRKIDFL TKQMEKIQPA LQEKHAMKQA VMEMMSQKIQ QLTALGAAQA 150
TAKA 154
Length:154
Mass (Da):17,328
Last modified:January 11, 2001 - v2
Checksum:i0DA1F3644548CB14
GO
Isoform 2 (identifier: Q99471-2) [UniParc]FASTAAdd to Basket

Also known as: MM1-beta

The sequence of this isoform differs from the canonical sequence as follows:
     59-154: GKELLVPLTS...LGAAQATAKA → DVCPWEAA

Note: Does not repress transcription activity of MYC.

Show »
Length:66
Mass (Da):7,481
Checksum:iC07E3472E5BD2A76
GO
Isoform 3 (identifier: Q99471-3) [UniParc]FASTAAdd to Basket

Also known as: MM1-gamma

The sequence of this isoform differs from the canonical sequence as follows:
     25-69: Missing.

Show »
Length:109
Mass (Da):12,379
Checksum:i899AFF472DCC00D7
GO

Sequence cautioni

The sequence BAA14006.1 differs from that shown. Reason: Erroneous initiation.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei25 – 6945Missing in isoform 3.
VSP_043103Add
BLAST
Alternative sequencei59 – 15496GKELL…ATAKA → DVCPWEAA in isoform 2.
VSP_043104Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D89667 mRNA. Translation: BAA14006.1. Different initiation.
AB055802 Genomic DNA. Translation: BAB32643.1.
AB055803 mRNA. Translation: BAB32644.1.
AB055804 mRNA. Translation: BAB32645.1.
AB055805 mRNA. Translation: BAB32646.1.
BT007195 mRNA. Translation: AAP35859.1.
AK292623 mRNA. Translation: BAF85312.1.
AC073611 Genomic DNA. No translation available.
CH471054 Genomic DNA. Translation: EAW96683.1.
CH471054 Genomic DNA. Translation: EAW96685.1.
BC003373 mRNA. No translation available.
BC062671 mRNA. Translation: AAH62671.1.
CCDSiCCDS8853.1. [Q99471-1]
CCDS8854.1. [Q99471-3]
RefSeqiNP_002615.2. NM_002624.3. [Q99471-1]
NP_665904.1. NM_145897.2. [Q99471-3]
UniGeneiHs.655327.

Genome annotation databases

EnsembliENST00000243040; ENSP00000243040; ENSG00000123349. [Q99471-2]
ENST00000334478; ENSP00000334188; ENSG00000123349. [Q99471-1]
ENST00000351500; ENSP00000266964; ENSG00000123349. [Q99471-3]
ENST00000551018; ENSP00000447942; ENSG00000123349. [Q99471-1]
GeneIDi5204.
KEGGihsa:5204.
UCSCiuc001scl.3. human. [Q99471-1]
uc001scm.3. human. [Q99471-3]

Polymorphism databases

DMDMi12231038.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D89667 mRNA. Translation: BAA14006.1 . Different initiation.
AB055802 Genomic DNA. Translation: BAB32643.1 .
AB055803 mRNA. Translation: BAB32644.1 .
AB055804 mRNA. Translation: BAB32645.1 .
AB055805 mRNA. Translation: BAB32646.1 .
BT007195 mRNA. Translation: AAP35859.1 .
AK292623 mRNA. Translation: BAF85312.1 .
AC073611 Genomic DNA. No translation available.
CH471054 Genomic DNA. Translation: EAW96683.1 .
CH471054 Genomic DNA. Translation: EAW96685.1 .
BC003373 mRNA. No translation available.
BC062671 mRNA. Translation: AAH62671.1 .
CCDSi CCDS8853.1. [Q99471-1 ]
CCDS8854.1. [Q99471-3 ]
RefSeqi NP_002615.2. NM_002624.3. [Q99471-1 ]
NP_665904.1. NM_145897.2. [Q99471-3 ]
UniGenei Hs.655327.

3D structure databases

ProteinModelPortali Q99471.
SMRi Q99471. Positions 11-149.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111226. 53 interactions.
DIPi DIP-28155N.
IntActi Q99471. 14 interactions.
MINTi MINT-5003456.
STRINGi 9606.ENSP00000334188.

PTM databases

PhosphoSitei Q99471.

Polymorphism databases

DMDMi 12231038.

2D gel databases

OGPi Q99471.

Proteomic databases

MaxQBi Q99471.
PaxDbi Q99471.
PeptideAtlasi Q99471.
PRIDEi Q99471.

Protocols and materials databases

DNASUi 5204.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000243040 ; ENSP00000243040 ; ENSG00000123349 . [Q99471-2 ]
ENST00000334478 ; ENSP00000334188 ; ENSG00000123349 . [Q99471-1 ]
ENST00000351500 ; ENSP00000266964 ; ENSG00000123349 . [Q99471-3 ]
ENST00000551018 ; ENSP00000447942 ; ENSG00000123349 . [Q99471-1 ]
GeneIDi 5204.
KEGGi hsa:5204.
UCSCi uc001scl.3. human. [Q99471-1 ]
uc001scm.3. human. [Q99471-3 ]

Organism-specific databases

CTDi 5204.
GeneCardsi GC12P053689.
HGNCi HGNC:8869. PFDN5.
HPAi HPA008587.
MIMi 604899. gene.
neXtProti NX_Q99471.
PharmGKBi PA33210.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1730.
HOGENOMi HOG000207562.
HOVERGENi HBG004539.
InParanoidi Q99471.
KOi K04797.
OMAi FVECECI.
PhylomeDBi Q99471.
TreeFami TF106509.

Enzyme and pathway databases

Reactomei REACT_16936. Prefoldin mediated transfer of substrate to CCT/TriC.

Miscellaneous databases

ChiTaRSi PFDN5. human.
GeneWikii PFDN5.
GenomeRNAii 5204.
NextBioi 20126.
PROi Q99471.
SOURCEi Search...

Gene expression databases

Bgeei Q99471.
CleanExi HS_PFDN5.
Genevestigatori Q99471.

Family and domain databases

Gene3Di 1.10.287.370. 1 hit.
HAMAPi MF_00308. PfdA.
InterProi IPR011599. PFD_alpha.
IPR009053. Prefoldin.
IPR004127. Prefoldin_subunit_alpha.
[Graphical view ]
Pfami PF02996. Prefoldin. 1 hit.
[Graphical view ]
SUPFAMi SSF46579. SSF46579. 1 hit.
TIGRFAMsi TIGR00293. TIGR00293. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "MM-1, a novel c-Myc-associating protein that represses transcriptional activity of c-Myc."
    Mori K., Maeda Y., Kitaura H., Taira T., Iguchi-Ariga S.M., Ariga H.
    J. Biol. Chem. 273:29794-29800(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Brain.
  2. "MM-1, a c-Myc-binding protein, is a candidate for a tumor suppressor in leukemia/lymphoma and tongue cancer."
    Fujioka Y., Taira T., Maeda Y., Tanaka S., Nishihara H., Iguchi-Ariga S.M.M., Nagashima K., Ariga H.
    J. Biol. Chem. 276:45137-45144(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
    Tissue: Blood and Fibroblast.
  3. "Distinct localizations and repression activities of MM-1 isoforms toward c-Myc."
    Hagio Y., Kimura Y., Taira T., Fujioka Y., Iguchi-Ariga S.M.M., Ariga H.
    J. Cell. Biochem. 97:145-155(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), SUBCELLULAR LOCATION, ALTERNATIVE SPLICING.
    Tissue: B-cell and Placenta.
  4. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  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] (ISOFORM 1).
    Tissue: Thymus.
  6. "The finished DNA sequence of human chromosome 12."
    Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
    , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
    Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "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: Placenta.
  9. "Prefoldin, a chaperone that delivers unfolded proteins to cytosolic chaperonin."
    Vainberg I.E., Lewis S.A., Rommelaere H., Ampe C., Vandekerckhove J., Klein H.L., Cowan N.J.
    Cell 93:863-873(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  10. "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], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  11. "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-42, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiPFD5_HUMAN
AccessioniPrimary (citable) accession number: Q99471
Secondary accession number(s): A8K9A8
, Q54AA8, Q9C083, Q9C084
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 11, 2001
Last modified: September 3, 2014
This is version 130 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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