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Q9BVP2

- GNL3_HUMAN

UniProt

Q9BVP2 - GNL3_HUMAN

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Protein

Guanine nucleotide-binding protein-like 3

Gene

GNL3

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

Functioni

May be required to maintain the proliferative capacity of stem cells. Stabilizes MDM2 by preventing its ubiquitination, and hence proteasomal degradation (By similarity).By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi178 – 1814GTPSequence Analysis
Nucleotide bindingi261 – 2688GTPSequence Analysis
Nucleotide bindingi305 – 3084GTPSequence Analysis

GO - Molecular functioni

  1. GTPase activity Source: RefGenome
  2. GTP binding Source: UniProtKB
  3. poly(A) RNA binding Source: UniProtKB

GO - Biological processi

  1. cell proliferation Source: Ensembl
  2. GTP catabolic process Source: GOC
  3. regulation of cell proliferation Source: UniProtKB
  4. ribosome biogenesis Source: RefGenome
Complete GO annotation...

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Guanine nucleotide-binding protein-like 3
Alternative name(s):
E2-induced gene 3 protein
Novel nucleolar protein 47
Short name:
NNP47
Nucleolar GTP-binding protein 3
Nucleostemin
Gene namesi
Name:GNL3
Synonyms:E2IG3, NS
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 3

Organism-specific databases

HGNCiHGNC:29931. GNL3.

Subcellular locationi

Nucleus By similarity. Nucleusnucleolus By similarity
Note: Shuttles between the nucleus and nucleolus.By similarity

GO - Cellular componenti

  1. extracellular space Source: UniProt
  2. membrane Source: UniProtKB
  3. nucleolus Source: UniProtKB
  4. nucleoplasm Source: Ensembl
  5. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134952132.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 549549Guanine nucleotide-binding protein-like 3PRO_0000122444Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei79 – 791N6-acetyllysine1 Publication
Modified residuei529 – 5291Phosphoserine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9BVP2.
PaxDbiQ9BVP2.
PRIDEiQ9BVP2.

2D gel databases

SWISS-2DPAGEQ9BVP2.

PTM databases

PhosphoSiteiQ9BVP2.

Expressioni

Tissue specificityi

Increased levels in lung tissue in cancer patients.1 Publication

Gene expression databases

BgeeiQ9BVP2.
CleanExiHS_GNL3.
ExpressionAtlasiQ9BVP2. baseline and differential.
GenevestigatoriQ9BVP2.

Organism-specific databases

HPAiCAB020770.

Interactioni

Subunit structurei

Interacts with MDM2; this interaction stabilizes MDM2. Interaction with MDM2 occurs in the nucleoplasm and is triggered by a nucleolar release mechanism, such as mitosis-induced nucleolar disassembly (By similarity). Indirectly interacts with TP53, via MDM2-binding (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
MDM2Q009873EBI-641642,EBI-389668
PPP2R5AQ151723EBI-641642,EBI-641666
STAT3P407632EBI-641642,EBI-518675

Protein-protein interaction databases

BioGridi117690. 65 interactions.
IntActiQ9BVP2. 18 interactions.
MINTiMINT-1405256.
STRINGi9606.ENSP00000395772.

Structurei

3D structure databases

ProteinModelPortaliQ9BVP2.
SMRiQ9BVP2. Positions 132-393.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini131 – 312182CP-type GPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 4645BasicBy similarityAdd
BLAST
Regioni282 – 456175IntermediateBy similarityAdd
BLAST
Regioni465 – 54379AcidicBy similarityAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili56 – 9540Sequence AnalysisAdd
BLAST

Domaini

The basic domain (B) allows nucleolar localization in the absence of GTP. The intermediate domain (I) inhibits nucleolar localization by the B domain and is required for exit from the nucleolus. Exit from the nucleolus to the nucleoplasm requires both the I and the acidic (A) domains, and may be triggered by GTP hydrolysis (By similarity).By similarity
In contrast to other GTP-binding proteins, this family is characterized by a circular permutation of the GTPase motifs described by a G4-G1-G3 pattern.

Sequence similaritiesi

Belongs to the TRAFAC class YlqF/YawG GTPase family.PROSITE-ProRule annotation
Contains 1 CP-type G (guanine nucleotide-binding) domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiCOG1161.
GeneTreeiENSGT00550000074731.
HOGENOMiHOG000207716.
HOVERGENiHBG051747.
InParanoidiQ9BVP2.
KOiK14538.
OMAiPKKLYCQ.
OrthoDBiEOG7J9VPR.
PhylomeDBiQ9BVP2.
TreeFamiTF313085.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR014813. Gnl3_N_dom.
IPR006073. GTP_binding_domain.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF08701. GN3L_Grn1. 1 hit.
PF01926. MMR_HSR1. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
PROSITEiPS51721. G_CP. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9BVP2-1) [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
MKRPKLKKAS KRMTCHKRYK IQKKVREHHR KLRKEAKKRG HKKPRKDPGV
60 70 80 90 100
PNSAPFKEAL LREAELRKQR LEELKQQQKL DRQKELEKKR KLETNPDIKP
110 120 130 140 150
SNVEPMEKEF GLCKTENKAK SGKQNSKKLY CQELKKVIEA SDVVLEVLDA
160 170 180 190 200
RDPLGCRCPQ VEEAIVQSGQ KKLVLILNKS DLVPKENLES WLNYLKKELP
210 220 230 240 250
TVVFRASTKP KDKGKITKRV KAKKNAAPFR SEVCFGKEGL WKLLGGFQET
260 270 280 290 300
CSKAIRVGVI GFPNVGKSSI INSLKQEQMC NVGVSMGLTR SMQVVPLDKQ
310 320 330 340 350
ITIIDSPSFI VSPLNSSSAL ALRSPASIEV VKPMEAASAI LSQADARQVV
360 370 380 390 400
LKYTVPGYRN SLEFFTVLAQ RRGMHQKGGI PNVEGAAKLL WSEWTGASLA
410 420 430 440 450
YYCHPPTSWT PPPYFNESIV VDMKSGFNLE ELEKNNAQSI RAIKGPHLAN
460 470 480 490 500
SILFQSSGLT NGIIEEKDIH EELPKRKERK QEEREDDKDS DQETVDEEVD
510 520 530 540
ENSSGMFAAE ETGEALSEET TAGEQSTRSF ILDKIIEEDD AYDFSTDYV
Length:549
Mass (Da):61,993
Last modified:May 5, 2009 - v2
Checksum:iF3928FE1C77C77F4
GO
Isoform 2 (identifier: Q9BVP2-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-12: Missing.

Show »
Length:537
Mass (Da):60,540
Checksum:i342BCB22B4234056
GO

Sequence cautioni

The sequence AAF09482.1 differs from that shown. Reason: Frameshift at position 516.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti3 – 31R → K in AAV74413. (PubMed:16012751)Curated
Sequence conflicti86 – 861L → Q in AAV74413. (PubMed:16012751)Curated
Sequence conflicti436 – 4361N → D in AAV74413. (PubMed:16012751)Curated
Sequence conflicti463 – 4631I → M in BAB55169. (PubMed:14702039)Curated
Sequence conflicti495 – 4951V → A in AAV74413. (PubMed:16012751)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti39 – 391R → Q.3 Publications
Corresponds to variant rs11177 [ dbSNP | Ensembl ].
VAR_022160
Natural varianti367 – 3671V → M.4 Publications
Corresponds to variant rs2289247 [ dbSNP | Ensembl ].
VAR_022161

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 1212Missing in isoform 2. 1 PublicationVSP_013411Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF191018 mRNA. Translation: AAF09482.1. Frameshift.
AY825265 mRNA. Translation: AAV74413.1.
AK027514 mRNA. Translation: BAB55168.1.
AK027516 mRNA. Translation: BAB55169.1.
AK315484 mRNA. Translation: BAG37868.1.
AC104446 Genomic DNA. No translation available.
BC001024 mRNA. Translation: AAH01024.1.
CCDSiCCDS2861.1. [Q9BVP2-1]
CCDS43100.1. [Q9BVP2-2]
RefSeqiNP_055181.3. NM_014366.4. [Q9BVP2-1]
NP_996561.1. NM_206825.1. [Q9BVP2-2]
NP_996562.1. NM_206826.1. [Q9BVP2-2]
UniGeneiHs.313544.

Genome annotation databases

EnsembliENST00000394799; ENSP00000378278; ENSG00000163938. [Q9BVP2-2]
ENST00000418458; ENSP00000395772; ENSG00000163938. [Q9BVP2-1]
GeneIDi26354.
KEGGihsa:26354.
UCSCiuc003dfd.3. human. [Q9BVP2-1]

Polymorphism databases

DMDMi229462872.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF191018 mRNA. Translation: AAF09482.1 . Frameshift.
AY825265 mRNA. Translation: AAV74413.1 .
AK027514 mRNA. Translation: BAB55168.1 .
AK027516 mRNA. Translation: BAB55169.1 .
AK315484 mRNA. Translation: BAG37868.1 .
AC104446 Genomic DNA. No translation available.
BC001024 mRNA. Translation: AAH01024.1 .
CCDSi CCDS2861.1. [Q9BVP2-1 ]
CCDS43100.1. [Q9BVP2-2 ]
RefSeqi NP_055181.3. NM_014366.4. [Q9BVP2-1 ]
NP_996561.1. NM_206825.1. [Q9BVP2-2 ]
NP_996562.1. NM_206826.1. [Q9BVP2-2 ]
UniGenei Hs.313544.

3D structure databases

ProteinModelPortali Q9BVP2.
SMRi Q9BVP2. Positions 132-393.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 117690. 65 interactions.
IntActi Q9BVP2. 18 interactions.
MINTi MINT-1405256.
STRINGi 9606.ENSP00000395772.

PTM databases

PhosphoSitei Q9BVP2.

Polymorphism databases

DMDMi 229462872.

2D gel databases

SWISS-2DPAGE Q9BVP2.

Proteomic databases

MaxQBi Q9BVP2.
PaxDbi Q9BVP2.
PRIDEi Q9BVP2.

Protocols and materials databases

DNASUi 26354.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000394799 ; ENSP00000378278 ; ENSG00000163938 . [Q9BVP2-2 ]
ENST00000418458 ; ENSP00000395772 ; ENSG00000163938 . [Q9BVP2-1 ]
GeneIDi 26354.
KEGGi hsa:26354.
UCSCi uc003dfd.3. human. [Q9BVP2-1 ]

Organism-specific databases

CTDi 26354.
GeneCardsi GC03P052718.
H-InvDB HIX0003367.
HGNCi HGNC:29931. GNL3.
HPAi CAB020770.
MIMi 608011. gene.
neXtProti NX_Q9BVP2.
PharmGKBi PA134952132.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1161.
GeneTreei ENSGT00550000074731.
HOGENOMi HOG000207716.
HOVERGENi HBG051747.
InParanoidi Q9BVP2.
KOi K14538.
OMAi PKKLYCQ.
OrthoDBi EOG7J9VPR.
PhylomeDBi Q9BVP2.
TreeFami TF313085.

Miscellaneous databases

ChiTaRSi GNL3. human.
GeneWikii GNL3.
GenomeRNAii 26354.
NextBioi 48693.
PROi Q9BVP2.
SOURCEi Search...

Gene expression databases

Bgeei Q9BVP2.
CleanExi HS_GNL3.
ExpressionAtlasi Q9BVP2. baseline and differential.
Genevestigatori Q9BVP2.

Family and domain databases

Gene3Di 3.40.50.300. 1 hit.
InterProi IPR014813. Gnl3_N_dom.
IPR006073. GTP_binding_domain.
IPR027417. P-loop_NTPase.
[Graphical view ]
Pfami PF08701. GN3L_Grn1. 1 hit.
PF01926. MMR_HSR1. 1 hit.
[Graphical view ]
SUPFAMi SSF52540. SSF52540. 1 hit.
PROSITEi PS51721. G_CP. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Effects of estrogen on global gene expression: identification of novel targets of estrogen action."
    Charpentier A.H., Bednarek A.K., Daniel R.L., Hawkins K.A., Laflin K.J., Gaddis S., MacLeod M.C., Aldaz C.M.
    Cancer Res. 60:5977-5983(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS GLN-39 AND MET-367.
  2. "Cloning of the nucleostemin gene and its function in transforming human embryonic bone marrow mesenchymal stem cells into F6 tumor cells."
    Han C., Zhang X., Xu W., Wang W., Qian H., Chen Y.
    Int. J. Mol. Med. 16:205-213(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, VARIANTS GLN-39 AND MET-367.
  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.
    , 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 1 AND 2).
  4. "The DNA sequence, annotation and analysis of human chromosome 3."
    Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., 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., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
    Nature 440:1194-1198(2006) [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 1), VARIANTS GLN-39 AND MET-367.
    Tissue: Eye.
  6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION.
  7. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. "A nucleolar mechanism controlling cell proliferation in stem and cancer cells."
    Tsai R.Y.L., McKay R.D.G.
    Genes Dev. 16:2991-3003(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH TP53, SUBCELLULAR LOCATION.
  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-529, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  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-79, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. Cited for: VARIANT [LARGE SCALE ANALYSIS] MET-367, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiGNL3_HUMAN
AccessioniPrimary (citable) accession number: Q9BVP2
Secondary accession number(s): B2RDC1
, Q5PU80, Q96SV6, Q96SV7, Q9UJY0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 12, 2005
Last sequence update: May 5, 2009
Last modified: October 29, 2014
This is version 123 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 3
    Human chromosome 3: 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