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P23258

- TBG1_HUMAN

UniProt

P23258 - TBG1_HUMAN

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Protein

Tubulin gamma-1 chain

Gene

TUBG1

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

Functioni

Tubulin is the major constituent of microtubules. The gamma chain is found at microtubule organizing centers (MTOC) such as the spindle poles or the centrosome. Pericentriolar matrix component that regulates alpha/beta chain minus-end nucleation, centrosome duplication and spindle formation.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi142 – 1487GTPSequence Analysis

GO - Molecular functioni

  1. GTPase activity Source: InterPro
  2. GTP binding Source: UniProtKB-KW
  3. structural constituent of cytoskeleton Source: ProtInc

GO - Biological processi

  1. cytoplasmic microtubule organization Source: InterPro
  2. G2/M transition of mitotic cell cycle Source: Reactome
  3. meiotic spindle organization Source: UniProtKB
  4. microtubule cytoskeleton organization Source: ProtInc
  5. microtubule nucleation Source: InterPro
  6. mitotic cell cycle Source: Reactome
Complete GO annotation...

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_15296. Recruitment of mitotic centrosome proteins and complexes.
REACT_15364. Loss of Nlp from mitotic centrosomes.
REACT_15451. Loss of proteins required for interphase microtubule organization from the centrosome.
REACT_15510. Recruitment of NuMA to mitotic centrosomes.
REACT_160315. Regulation of PLK1 Activity at G2/M Transition.

Names & Taxonomyi

Protein namesi
Recommended name:
Tubulin gamma-1 chain
Alternative name(s):
Gamma-1-tubulin
Gamma-tubulin complex component 1
Short name:
GCP-1
Gene namesi
Name:TUBG1
Synonyms:TUBG
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 17

Organism-specific databases

HGNCiHGNC:12417. TUBG1.

Subcellular locationi

Cytoplasmcytoskeletonmicrotubule organizing centercentrosome 1 Publication

GO - Cellular componenti

  1. apical part of cell Source: Ensembl
  2. cell leading edge Source: Ensembl
  3. centriole Source: Ensembl
  4. centrosome Source: UniProtKB
  5. ciliary basal body Source: Ensembl
  6. condensed nuclear chromosome Source: UniProtKB
  7. cytoplasm Source: UniProtKB
  8. cytoplasmic microtubule Source: Ensembl
  9. cytosol Source: Reactome
  10. gamma-tubulin complex Source: UniProtKB
  11. nonmotile primary cilium Source: Ensembl
  12. pericentriolar material Source: Ensembl
  13. polar microtubule Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Microtubule

Pathology & Biotechi

Involvement in diseasei

Cortical dysplasia, complex, with other brain malformations 4 (CDCBM4) [MIM:615412]: A disorder of aberrant neuronal migration and disturbed axonal guidance. Clinical features include early-onset seizures, microcephaly, spastic tetraplegia, and various malformations of cortical development, such as agyria, posterior or frontal pachygyria, thick cortex, and subcortical band heterotopia and thin corpus callosum in some patients.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti92 – 921Y → C in CDCBM4. 1 Publication
VAR_070577
Natural varianti331 – 3311T → P in CDCBM4. 1 Publication
VAR_070578
Natural varianti387 – 3871L → P in CDCBM4; the chaperonin-dependent folding and hence the yield of monomeric gamma-tubulin is compromised. 1 Publication
VAR_070579

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi615412. phenotype.
PharmGKBiPA37079.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 451451Tubulin gamma-1 chainPRO_0000048465Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei131 – 1311Phosphoserine; by BRSK1By similarity

Post-translational modificationi

Phosphorylation at Ser-131 by BRSK1 regulates centrosome duplication, possibly by mediating relocation of gamma-tubulin and its associated proteins from the cytoplasm to the centrosome.By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP23258.
PaxDbiP23258.
PRIDEiP23258.

2D gel databases

REPRODUCTION-2DPAGEIPI00295081.

PTM databases

PhosphoSiteiP23258.

Miscellaneous databases

PMAP-CutDBP23258.

Expressioni

Gene expression databases

BgeeiP23258.
CleanExiHS_TUBG1.
ExpressionAtlasiP23258. baseline and differential.
GenevestigatoriP23258.

Organism-specific databases

HPAiCAB004608.

Interactioni

Subunit structurei

Interacts with TUBGCP2 and TUBGCP3. Interacts with B9D2 (By similarity). Interacts with CDK5RAP2; the interaction is leading to centrosomal localization of TUBG1 and CDK5RAP2. Interacts with PIFO.By similarity2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
AXIN1O151694EBI-302589,EBI-710484
MARK4Q96L344EBI-302589,EBI-302319
MZT1Q08AG72EBI-302589,EBI-2637198
MZT2BQ6NZ672EBI-302589,EBI-1052566

Protein-protein interaction databases

BioGridi113134. 181 interactions.
DIPiDIP-29890N.
IntActiP23258. 33 interactions.
MINTiMINT-4051249.
STRINGi9606.ENSP00000251413.

Structurei

Secondary structure

1
451
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 106Combined sources
Helixi11 – 2818Combined sources
Beta strandi33 – 353Combined sources
Helixi48 – 503Combined sources
Beta strandi52 – 543Combined sources
Beta strandi60 – 623Combined sources
Beta strandi64 – 718Combined sources
Helixi72 – 798Combined sources
Turni81 – 855Combined sources
Helixi88 – 903Combined sources
Beta strandi91 – 933Combined sources
Helixi104 – 12724Combined sources
Beta strandi134 – 14411Combined sources
Helixi145 – 16016Combined sources
Beta strandi164 – 1729Combined sources
Helixi184 – 19714Combined sources
Beta strandi200 – 2067Combined sources
Helixi207 – 21610Combined sources
Helixi225 – 23915Combined sources
Turni240 – 2434Combined sources
Beta strandi244 – 2474Combined sources
Beta strandi248 – 2503Combined sources
Helixi253 – 2608Combined sources
Beta strandi262 – 2654Combined sources
Beta strandi268 – 2747Combined sources
Helixi290 – 2967Combined sources
Helixi300 – 3023Combined sources
Beta strandi303 – 3053Combined sources
Beta strandi317 – 32711Combined sources
Helixi330 – 34213Combined sources
Beta strandi350 – 3523Combined sources
Beta strandi356 – 3616Combined sources
Beta strandi374 – 3818Combined sources
Helixi382 – 3843Combined sources
Helixi385 – 40016Combined sources
Helixi406 – 4094Combined sources
Helixi412 – 4143Combined sources
Helixi419 – 43719Combined sources
Helixi441 – 4433Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1Z5VX-ray2.71A1-449[»]
1Z5WX-ray3.00A1-449[»]
3CB2X-ray2.30A/B1-451[»]
ProteinModelPortaliP23258.
SMRiP23258. Positions 2-446.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP23258.

Family & Domainsi

Sequence similaritiesi

Belongs to the tubulin family.Curated

Phylogenomic databases

eggNOGiCOG5023.
GeneTreeiENSGT00530000063251.
HOGENOMiHOG000165714.
HOVERGENiHBG098558.
InParanoidiP23258.
KOiK10389.
OMAiEGFMLMH.
OrthoDBiEOG70S755.
PhylomeDBiP23258.
TreeFamiTF300477.

Family and domain databases

Gene3Di1.10.287.600. 1 hit.
3.30.1330.20. 1 hit.
3.40.50.1440. 1 hit.
InterProiIPR002454. Gamma_tubulin.
IPR008280. Tub_FtsZ_C.
IPR000217. Tubulin.
IPR018316. Tubulin/FtsZ_2-layer-sand-dom.
IPR023123. Tubulin_C.
IPR017975. Tubulin_CS.
IPR003008. Tubulin_FtsZ_GTPase.
[Graphical view]
PANTHERiPTHR11588. PTHR11588. 1 hit.
PfamiPF00091. Tubulin. 1 hit.
PF03953. Tubulin_C. 1 hit.
[Graphical view]
PRINTSiPR01164. GAMMATUBULIN.
PR01161. TUBULIN.
SMARTiSM00864. Tubulin. 1 hit.
SM00865. Tubulin_C. 1 hit.
[Graphical view]
SUPFAMiSSF52490. SSF52490. 1 hit.
SSF55307. SSF55307. 1 hit.
PROSITEiPS00227. TUBULIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P23258-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MPREIITLQL GQCGNQIGFE FWKQLCAEHG ISPEGIVEEF ATEGTDRKDV
60 70 80 90 100
FFYQADDEHY IPRAVLLDLE PRVIHSILNS PYAKLYNPEN IYLSEHGGGA
110 120 130 140 150
GNNWASGFSQ GEKIHEDIFD IIDREADGSD SLEGFVLCHS IAGGTGSGLG
160 170 180 190 200
SYLLERLNDR YPKKLVQTYS VFPNQDEMSD VVVQPYNSLL TLKRLTQNAD
210 220 230 240 250
CVVVLDNTAL NRIATDRLHI QNPSFSQINQ LVSTIMSAST TTLRYPGYMN
260 270 280 290 300
NDLIGLIASL IPTPRLHFLM TGYTPLTTDQ SVASVRKTTV LDVMRRLLQP
310 320 330 340 350
KNVMVSTGRD RQTNHCYIAI LNIIQGEVDP TQVHKSLQRI RERKLANFIP
360 370 380 390 400
WGPASIQVAL SRKSPYLPSA HRVSGLMMAN HTSISSLFER TCRQYDKLRK
410 420 430 440 450
REAFLEQFRK EDMFKDNFDE MDTSREIVQQ LIDEYHAATR PDYISWGTQE

Q
Length:451
Mass (Da):51,170
Last modified:May 2, 2002 - v2
Checksum:iE2A4C0179ED0CFE8
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti35 – 351G → A in AAA52620. (PubMed:1904010)Curated
Sequence conflicti202 – 2021V → L in AAA52620. (PubMed:1904010)Curated

Mass spectrometryi

Molecular mass is 51197.98 Da from positions 1 - 451. Determined by MALDI. 1 Publication

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti92 – 921Y → C in CDCBM4. 1 Publication
VAR_070577
Natural varianti331 – 3311T → P in CDCBM4. 1 Publication
VAR_070578
Natural varianti387 – 3871L → P in CDCBM4; the chaperonin-dependent folding and hence the yield of monomeric gamma-tubulin is compromised. 1 Publication
VAR_070579
Natural varianti413 – 4131M → V.
Corresponds to variant rs13663 [ dbSNP | Ensembl ].
VAR_052674

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M61764 mRNA. Translation: AAA52620.1.
BT019931 mRNA. Translation: AAV38734.1.
CR407642 mRNA. Translation: CAG28570.1.
AK313339 mRNA. Translation: BAG36143.1.
BC000619 mRNA. Translation: AAH00619.1.
CCDSiCCDS11433.1.
PIRiA39527. UBHUG.
RefSeqiNP_001061.2. NM_001070.4.
UniGeneiHs.279669.

Genome annotation databases

EnsembliENST00000251413; ENSP00000251413; ENSG00000131462.
GeneIDi7283.
KEGGihsa:7283.
UCSCiuc002ian.3. human.

Polymorphism databases

DMDMi20455518.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M61764 mRNA. Translation: AAA52620.1 .
BT019931 mRNA. Translation: AAV38734.1 .
CR407642 mRNA. Translation: CAG28570.1 .
AK313339 mRNA. Translation: BAG36143.1 .
BC000619 mRNA. Translation: AAH00619.1 .
CCDSi CCDS11433.1.
PIRi A39527. UBHUG.
RefSeqi NP_001061.2. NM_001070.4.
UniGenei Hs.279669.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1Z5V X-ray 2.71 A 1-449 [» ]
1Z5W X-ray 3.00 A 1-449 [» ]
3CB2 X-ray 2.30 A/B 1-451 [» ]
ProteinModelPortali P23258.
SMRi P23258. Positions 2-446.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 113134. 181 interactions.
DIPi DIP-29890N.
IntActi P23258. 33 interactions.
MINTi MINT-4051249.
STRINGi 9606.ENSP00000251413.

Chemistry

DrugBanki DB00570. Vinblastine.

PTM databases

PhosphoSitei P23258.

Polymorphism databases

DMDMi 20455518.

2D gel databases

REPRODUCTION-2DPAGE IPI00295081.

Proteomic databases

MaxQBi P23258.
PaxDbi P23258.
PRIDEi P23258.

Protocols and materials databases

DNASUi 7283.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000251413 ; ENSP00000251413 ; ENSG00000131462 .
GeneIDi 7283.
KEGGi hsa:7283.
UCSCi uc002ian.3. human.

Organism-specific databases

CTDi 7283.
GeneCardsi GC17P040761.
HGNCi HGNC:12417. TUBG1.
HPAi CAB004608.
MIMi 191135. gene.
615412. phenotype.
neXtProti NX_P23258.
PharmGKBi PA37079.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5023.
GeneTreei ENSGT00530000063251.
HOGENOMi HOG000165714.
HOVERGENi HBG098558.
InParanoidi P23258.
KOi K10389.
OMAi EGFMLMH.
OrthoDBi EOG70S755.
PhylomeDBi P23258.
TreeFami TF300477.

Enzyme and pathway databases

Reactomei REACT_15296. Recruitment of mitotic centrosome proteins and complexes.
REACT_15364. Loss of Nlp from mitotic centrosomes.
REACT_15451. Loss of proteins required for interphase microtubule organization from the centrosome.
REACT_15510. Recruitment of NuMA to mitotic centrosomes.
REACT_160315. Regulation of PLK1 Activity at G2/M Transition.

Miscellaneous databases

ChiTaRSi TUBG1. human.
EvolutionaryTracei P23258.
GeneWikii TUBG1.
GenomeRNAii 7283.
NextBioi 28475.
PMAP-CutDB P23258.
PROi P23258.
SOURCEi Search...

Gene expression databases

Bgeei P23258.
CleanExi HS_TUBG1.
ExpressionAtlasi P23258. baseline and differential.
Genevestigatori P23258.

Family and domain databases

Gene3Di 1.10.287.600. 1 hit.
3.30.1330.20. 1 hit.
3.40.50.1440. 1 hit.
InterProi IPR002454. Gamma_tubulin.
IPR008280. Tub_FtsZ_C.
IPR000217. Tubulin.
IPR018316. Tubulin/FtsZ_2-layer-sand-dom.
IPR023123. Tubulin_C.
IPR017975. Tubulin_CS.
IPR003008. Tubulin_FtsZ_GTPase.
[Graphical view ]
PANTHERi PTHR11588. PTHR11588. 1 hit.
Pfami PF00091. Tubulin. 1 hit.
PF03953. Tubulin_C. 1 hit.
[Graphical view ]
PRINTSi PR01164. GAMMATUBULIN.
PR01161. TUBULIN.
SMARTi SM00864. Tubulin. 1 hit.
SM00865. Tubulin_C. 1 hit.
[Graphical view ]
SUPFAMi SSF52490. SSF52490. 1 hit.
SSF55307. SSF55307. 1 hit.
PROSITEi PS00227. TUBULIN. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Gamma-tubulin is present in Drosophila melanogaster and Homo sapiens and is associated with the centrosome."
    Zheng Y., Jung M.K., Oakley B.R.
    Cell 65:817-823(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "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 (OCT-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  3. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  4. "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].
    Tissue: Testis.
  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].
    Tissue: Skin.
  6. "Cluster analysis of an extensive human breast cancer cell line protein expression map database."
    Harris R.A., Yang A., Stein R.C., Lucy K., Brusten L., Herath A., Parekh R., Waterfield M.D., O'Hare M.J., Neville M.A., Page M.J., Zvelebil M.J.
    Proteomics 2:212-223(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: MASS SPECTROMETRY.
    Tissue: Mammary cancer.
  7. "Characterization of the human homologue of the yeast spc98p and its association with gamma-tubulin."
    Tassin A.-M., Celati C., Moudjou M., Bornens M.
    J. Cell Biol. 141:689-701(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  8. "CDK5RAP2 is a pericentriolar protein that functions in centrosomal attachment of the gamma-tubulin ring complex."
    Fong K.W., Choi Y.K., Rattner J.B., Qi R.Z.
    Mol. Biol. Cell 19:115-125(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CDK5RAP2.
  9. Cited for: INTERACTION WITH PIFO.
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. Cited for: VARIANTS CDCBM4 CYS-92; PRO-331 AND PRO-387, CHARACTERIZATION OF VARIANT CDCBM4 PRO-387.

Entry informationi

Entry nameiTBG1_HUMAN
AccessioniPrimary (citable) accession number: P23258
Secondary accession number(s): Q53X79, Q9BW59
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: May 2, 2002
Last modified: November 26, 2014
This is version 158 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

3D-structure, Complete proteome, 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3