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Q9H9A7

- RMI1_HUMAN

UniProt

Q9H9A7 - RMI1_HUMAN

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Protein

RecQ-mediated genome instability protein 1

Gene

RMI1

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

Functioni

Essential component of the RMI complex, a complex that plays an important role in the processing of homologous recombination intermediates to limit DNA crossover formation in cells. Promotes TOP3A binding to double Holliday junctions (DHJ) and hence stimulates TOP3A-mediated dissolution. Required for BLM phosphorylation during mitosis. Within the BLM complex, required for BLM and TOP3A stability.3 Publications

GO - Biological processi

  1. DNA replication Source: UniProtKB-KW
  2. glucose homeostasis Source: Ensembl
  3. multicellular organism growth Source: Ensembl
  4. reduction of food intake in response to dietary excess Source: Ensembl
  5. response to glucose Source: Ensembl
Complete GO annotation...

Keywords - Biological processi

DNA replication

Names & Taxonomyi

Protein namesi
Recommended name:
RecQ-mediated genome instability protein 1
Alternative name(s):
BLM-associated protein of 75 kDa
Short name:
BLAP75
FAAP75
Gene namesi
Name:RMI1
Synonyms:C9orf76
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 9

Organism-specific databases

HGNCiHGNC:25764. RMI1.

Subcellular locationi

Nucleus 1 Publication
Note: Forms foci in response to DNA damage.

GO - Cellular componenti

  1. nucleus Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134939007.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 625625RecQ-mediated genome instability protein 1PRO_0000227546Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication
Modified residuei225 – 2251Phosphoserine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9H9A7.
PaxDbiQ9H9A7.
PRIDEiQ9H9A7.

PTM databases

PhosphoSiteiQ9H9A7.

Expressioni

Gene expression databases

BgeeiQ9H9A7.
CleanExiHS_RMI1.
GenevestigatoriQ9H9A7.

Organism-specific databases

HPAiCAB012247.
HPA021661.
HPA051592.

Interactioni

Subunit structurei

Component of the RMI complex, containing at least TOP3A, RMI1 and RMI2. The RMI complex interacts with BLM. Directly interacts with RMI2 and TOP3A. May bind DHJ. Interacts (via N-terminal region) with BLM; the interaction is direct.6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
BLMP5413210EBI-621339,EBI-621372

Protein-protein interaction databases

BioGridi123066. 21 interactions.
DIPiDIP-33324N.
IntActiQ9H9A7. 13 interactions.
MINTiMINT-8048917.
STRINGi9606.ENSP00000317039.

Structurei

Secondary structure

1
625
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 1816Combined sources
Helixi24 – 3815Combined sources
Helixi45 – 5713Combined sources
Helixi61 – 644Combined sources
Turni71 – 755Combined sources
Beta strandi77 – 9519Combined sources
Helixi96 – 10813Combined sources
Helixi113 – 1153Combined sources
Helixi126 – 1294Combined sources
Beta strandi135 – 1439Combined sources
Beta strandi145 – 1506Combined sources
Beta strandi166 – 17611Combined sources
Beta strandi179 – 1824Combined sources
Helixi184 – 1863Combined sources
Beta strandi187 – 1915Combined sources
Helixi195 – 2017Combined sources
Helixi203 – 2108Combined sources
Helixi480 – 4823Combined sources
Helixi483 – 4875Combined sources
Helixi494 – 4996Combined sources
Beta strandi506 – 51712Combined sources
Helixi524 – 5263Combined sources
Beta strandi531 – 5355Combined sources
Beta strandi540 – 5456Combined sources
Helixi547 – 5548Combined sources
Helixi558 – 5647Combined sources
Helixi568 – 58720Combined sources
Beta strandi589 – 5979Combined sources
Turni598 – 6014Combined sources
Beta strandi602 – 6098Combined sources
Helixi613 – 62210Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3MXNX-ray1.55A473-625[»]
3NBHX-ray2.00A475-625[»]
3NBIX-ray2.00A2-213[»]
4CGYX-ray2.85B1-219[»]
4CHTX-ray3.25B1-219[»]
4DAYX-ray3.30A473-625[»]
ProteinModelPortaliQ9H9A7.
SMRiQ9H9A7. Positions 2-216, 475-625.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the RMI1 family.Curated

Phylogenomic databases

eggNOGiNOG261197.
GeneTreeiENSGT00740000115530.
HOVERGENiHBG061190.
InParanoidiQ9H9A7.
KOiK10990.
OMAiAMDLYSP.
OrthoDBiEOG7F7W8R.
PhylomeDBiQ9H9A7.
TreeFamiTF316491.

Family and domain databases

InterProiIPR013894. DUF1767.
[Graphical view]
PfamiPF08585. DUF1767. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9H9A7-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MNVTSIALRA ETWLLAAWHV KVPPMWLEAC INWIQEENNN VNLSQAQMNK
60 70 80 90 100
QVFEQWLLTD LRDLEHPLLP DGILEIPKGE LNGFYALQIN SLVDVSQPAY
110 120 130 140 150
SQIQKLRGKN TTNDLVTAEA QVTPKPWEAK PSRMLMLQLT DGIVQIQGME
160 170 180 190 200
YQPIPILHSD LPPGTKILIY GNISFRLGVL LLKPENVKVL GGEVDALLEE
210 220 230 240 250
YAQEKVLARL IGEPDLVVSV IPNNSNENIP RVTDVLDPAL GPSDEELLAS
260 270 280 290 300
LDENDELTAN NDTSSERCFT TGSSSNTIPT RQSSFEPEFV ISPRPKEEPS
310 320 330 340 350
NLSIHVMDGE LDDFSLEEAL LLEETVQKEQ METKELQPLT FNRNADRSIE
360 370 380 390 400
RFSHNPNTTN NFSLTCKNGN NNWSEKNVSE QMTNEDKSFG CPSVRDQNRS
410 420 430 440 450
IFSVHCNVPL AHDFTNKEKN LETDNKIKQT SSSDSHSLNN KILNREVVNY
460 470 480 490 500
VQKRNSQISN ENDCNLQSCS LRSSENSINL SIAMDLYSPP FVYLSVLMAS
510 520 530 540 550
KPKEVTTVKV KAFIVTLTGN LSSSGGIWSI TAKVSDGTAY LDVDFVDEIL
560 570 580 590 600
TSLIGFSVPE MKQSKKDPLQ YQKFLEGLQK CQRDLIDLCC LMTISFNPSL
610 620
SKAMVLALQD VNMEHLENLK KRLNK
Length:625
Mass (Da):70,144
Last modified:February 8, 2011 - v3
Checksum:i2BB449363DBF76B7
GO

Sequence cautioni

The sequence AAH20606.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.Curated
The sequence AAH32494.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.Curated
The sequence AAH39999.1 differs from that shown. Reason: Frameshift at position 375. Curated
The sequence AAH39999.1 differs from that shown. Reason: Frameshift at positions 377 and 444. Curated
The sequence AAH53549.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.Curated
The sequence AAH64937.1 differs from that shown. Reason: Frameshift at positions 444 and 615. Curated
The sequence AAH64937.1 differs from that shown. Reason: Frameshift at positions 377 and 444. Curated
The sequence CAI13575.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti11 – 111E → G in BAB14325. (PubMed:14702039)Curated
Sequence conflicti259 – 2591A → T in BAB14325. (PubMed:14702039)Curated
Sequence conflicti318 – 3181E → D in AAH20606. (PubMed:15489334)Curated
Sequence conflicti443 – 4431L → F in AAH39999. (PubMed:15489334)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti100 – 1001Y → H.1 Publication
Corresponds to variant rs17855932 [ dbSNP | Ensembl ].
VAR_025556
Natural varianti455 – 4551N → S.2 Publications
Corresponds to variant rs1982151 [ dbSNP | Ensembl ].
VAR_025557

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK022950 mRNA. Translation: BAB14325.1.
AL732446 Genomic DNA. Translation: CAI13576.1.
AL732446 Genomic DNA. Translation: CAI13575.1. Sequence problems.
BC020606 mRNA. Translation: AAH20606.1. Sequence problems.
BC032494 mRNA. Translation: AAH32494.1. Sequence problems.
BC039999 mRNA. Translation: AAH39999.1. Frameshift.
BC053549 mRNA. Translation: AAH53549.1. Sequence problems.
BC064937 mRNA. Translation: AAH64937.1. Frameshift.
CCDSiCCDS6669.1.
RefSeqiNP_079221.2. NM_024945.2.
XP_005252268.1. XM_005252211.1.
XP_005252270.1. XM_005252213.1.
UniGeneiHs.726327.

Genome annotation databases

EnsembliENST00000325875; ENSP00000317039; ENSG00000178966.
GeneIDi80010.
KEGGihsa:80010.
UCSCiuc004anp.4. human.

Polymorphism databases

DMDMi322510109.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK022950 mRNA. Translation: BAB14325.1 .
AL732446 Genomic DNA. Translation: CAI13576.1 .
AL732446 Genomic DNA. Translation: CAI13575.1 . Sequence problems.
BC020606 mRNA. Translation: AAH20606.1 . Sequence problems.
BC032494 mRNA. Translation: AAH32494.1 . Sequence problems.
BC039999 mRNA. Translation: AAH39999.1 . Frameshift.
BC053549 mRNA. Translation: AAH53549.1 . Sequence problems.
BC064937 mRNA. Translation: AAH64937.1 . Frameshift.
CCDSi CCDS6669.1.
RefSeqi NP_079221.2. NM_024945.2.
XP_005252268.1. XM_005252211.1.
XP_005252270.1. XM_005252213.1.
UniGenei Hs.726327.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3MXN X-ray 1.55 A 473-625 [» ]
3NBH X-ray 2.00 A 475-625 [» ]
3NBI X-ray 2.00 A 2-213 [» ]
4CGY X-ray 2.85 B 1-219 [» ]
4CHT X-ray 3.25 B 1-219 [» ]
4DAY X-ray 3.30 A 473-625 [» ]
ProteinModelPortali Q9H9A7.
SMRi Q9H9A7. Positions 2-216, 475-625.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 123066. 21 interactions.
DIPi DIP-33324N.
IntActi Q9H9A7. 13 interactions.
MINTi MINT-8048917.
STRINGi 9606.ENSP00000317039.

PTM databases

PhosphoSitei Q9H9A7.

Polymorphism databases

DMDMi 322510109.

Proteomic databases

MaxQBi Q9H9A7.
PaxDbi Q9H9A7.
PRIDEi Q9H9A7.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000325875 ; ENSP00000317039 ; ENSG00000178966 .
GeneIDi 80010.
KEGGi hsa:80010.
UCSCi uc004anp.4. human.

Organism-specific databases

CTDi 80010.
GeneCardsi GC09P086595.
H-InvDB HIX0008132.
HGNCi HGNC:25764. RMI1.
HPAi CAB012247.
HPA021661.
HPA051592.
MIMi 610404. gene.
neXtProti NX_Q9H9A7.
PharmGKBi PA134939007.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG261197.
GeneTreei ENSGT00740000115530.
HOVERGENi HBG061190.
InParanoidi Q9H9A7.
KOi K10990.
OMAi AMDLYSP.
OrthoDBi EOG7F7W8R.
PhylomeDBi Q9H9A7.
TreeFami TF316491.

Miscellaneous databases

GeneWikii RMI1.
GenomeRNAii 80010.
NextBioi 70103.
PROi Q9H9A7.
SOURCEi Search...

Gene expression databases

Bgeei Q9H9A7.
CleanExi HS_RMI1.
Genevestigatori Q9H9A7.

Family and domain databases

InterProi IPR013894. DUF1767.
[Graphical view ]
Pfami PF08585. DUF1767. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "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], VARIANT SER-455.
  2. "DNA sequence and analysis of human chromosome 9."
    Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
    , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
    Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "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], VARIANTS HIS-100 AND SER-455.
    Tissue: Brain, Skin, Testis and Uterus.
  4. "BLAP75, an essential component of Bloom's syndrome protein complexes that maintain genome integrity."
    Yin J., Sobeck A., Xu C., Meetei A.R., Hoatlin M., Li L., Wang W.
    EMBO J. 24:1465-1476(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION IN COMPLEX WITH BLM AND TOP3A, SUBCELLULAR LOCATION.
  5. "A double Holliday junction dissolvasome comprising BLM, topoisomerase III alpha, and BLAP75."
    Raynard S., Bussen W., Sung P.
    J. Biol. Chem. 281:13861-13864(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH BLM AND TOP3A.
  6. "BLAP75/RMI1 promotes the BLM-dependent dissolution of homologous recombination intermediates."
    Wu L., Bachrati C.Z., Ou J., Xu C., Yin J., Chang M., Wang W., Li L., Brown G.W., Hickson I.D.
    Proc. Natl. Acad. Sci. U.S.A. 103:4068-4073(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, BINDING TO DOUBLE HOLLIDAY JUNCTION, INTERACTION WITH TOP3A.
  7. "RMI, a new OB-fold complex essential for Bloom syndrome protein to maintain genome stability."
    Xu D., Guo R., Sobeck A., Bachrati C.Z., Yang J., Enomoto T., Brown G.W., Hoatlin M.E., Hickson I.D., Wang W.
    Genes Dev. 22:2843-2855(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE RMI COMPLEX, INTERACTION WITH RMI2.
  8. "BLAP18/RMI2, a novel OB-fold-containing protein, is an essential component of the Bloom helicase-double Holliday junction dissolvasome."
    Singh T.R., Ali A.M., Busygina V., Raynard S., Fan Q., Du C.-H., Andreassen P.R., Sung P., Meetei A.R.
    Genes Dev. 22:2856-2868(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE RMI COMPLEX, INTERACTION WITH RMI2.
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-225, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "Scaffolding protein SPIDR/KIAA0146 connects the Bloom syndrome helicase with homologous recombination repair."
    Wan L., Han J., Liu T., Dong S., Xie F., Chen H., Huang J.
    Proc. Natl. Acad. Sci. U.S.A. 110:10646-10651(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH BLM.

Entry informationi

Entry nameiRMI1_HUMAN
AccessioniPrimary (citable) accession number: Q9H9A7
Secondary accession number(s): Q05BX1
, Q05CW3, Q5SQG8, Q5SQG9, Q6P1Q4, Q6PI89, Q7Z6L6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 21, 2006
Last sequence update: February 8, 2011
Last modified: November 26, 2014
This is version 105 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 9
    Human chromosome 9: 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