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Q9NRK6

- ABCBA_HUMAN

UniProt

Q9NRK6 - ABCBA_HUMAN

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Protein

ATP-binding cassette sub-family B member 10, mitochondrial

Gene

ABCB10

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

Functioni

May mediate critical mitochondrial transport functions related to heme biosynthesis.By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi527 – 5348ATP

GO - Molecular functioni

  1. ATPase activity, coupled to transmembrane movement of substances Source: RefGenome
  2. ATP binding Source: UniProtKB-KW
  3. transporter activity Source: UniProtKB

GO - Biological processi

  1. transmembrane transport Source: RefGenome
  2. transport Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Transport

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi3.6.3.43. 2681.
ReactomeiREACT_111108. Mitochondrial ABC transporters.

Protein family/group databases

TCDBi3.A.1.201.17. the atp-binding cassette (abc) superfamily.

Names & Taxonomyi

Protein namesi
Recommended name:
ATP-binding cassette sub-family B member 10, mitochondrial
Alternative name(s):
ATP-binding cassette transporter 10
Short name:
ABC transporter 10 protein
Mitochondrial ATP-binding cassette 2
Short name:
M-ABC2
Gene namesi
Name:ABCB10
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:41. ABCB10.

Subcellular locationi

GO - Cellular componenti

  1. integral component of mitochondrial membrane Source: UniProtKB
  2. mitochondrial inner membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion inner membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA24385.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 105105Mitochondrion1 PublicationAdd
BLAST
Chaini106 – 738633ATP-binding cassette sub-family B member 10, mitochondrialPRO_0000000255Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei265 – 2651N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ9NRK6.
PaxDbiQ9NRK6.
PRIDEiQ9NRK6.

PTM databases

PhosphoSiteiQ9NRK6.

Expressioni

Tissue specificityi

Ubiquitous. Highly expressed in bone marrow, expressed at intermediate to high levels in skeletal muscle, small intestine, thyroid, heart, brain, placenta, liver, pancreas, prostate, testis, ovary, leukocyte, stomach, spinal cord, lymph node, trachea and adrenal gland, and low levels are found in lung, kidney, spleen, thymus and colon.

Gene expression databases

BgeeiQ9NRK6.
CleanExiHS_ABCB10.
ExpressionAtlasiQ9NRK6. baseline and differential.
GenevestigatoriQ9NRK6.

Organism-specific databases

HPAiCAB044063.
CAB044065.

Interactioni

Subunit structurei

Homodimer or homooligomer.2 Publications

Protein-protein interaction databases

BioGridi117020. 14 interactions.
IntActiQ9NRK6. 1 interaction.
STRINGi9606.ENSP00000355637.

Structurei

Secondary structure

1
738
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi154 – 16411
Helixi165 – 1673
Helixi168 – 18518
Helixi188 – 20114
Helixi208 – 25548
Helixi260 – 2656
Helixi268 – 28518
Helixi288 – 31023
Helixi312 – 35948
Helixi361 – 3666
Helixi370 – 42253
Helixi428 – 46942
Turni485 – 4873
Beta strandi492 – 4998
Beta strandi502 – 5043
Beta strandi509 – 5179
Beta strandi522 – 5265
Helixi530 – 54011
Beta strandi547 – 5537
Helixi558 – 5603
Helixi563 – 5686
Beta strandi569 – 5735
Beta strandi581 – 5833
Helixi584 – 5896
Beta strandi592 – 5943
Turni595 – 5973
Helixi600 – 60910
Helixi613 – 6175
Beta strandi619 – 6213
Helixi622 – 6243
Beta strandi628 – 6314
Helixi636 – 65015
Beta strandi653 – 6586
Helixi666 – 68015
Beta strandi683 – 6886
Helixi692 – 6976
Beta strandi698 – 7047
Beta strandi706 – 7138
Helixi715 – 7195

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3ZDQX-ray2.85A152-738[»]
4AYTX-ray2.85A152-738[»]
4AYWX-ray3.30A1-738[»]
4AYXX-ray2.90A152-738[»]
ProteinModelPortaliQ9NRK6.
SMRiQ9NRK6. Positions 153-722.
ModBaseiSearch...
MobiDBiSearch...

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini106 – 17065Mitochondrial intermembraneSequence AnalysisAdd
BLAST
Topological domaini192 – 21524Mitochondrial matrixSequence AnalysisAdd
BLAST
Topological domaini237 – 31276Mitochondrial intermembraneSequence AnalysisAdd
BLAST
Topological domaini334 – 40774Mitochondrial matrixSequence AnalysisAdd
BLAST
Topological domaini429 – 4302Mitochondrial intermembraneSequence Analysis
Topological domaini452 – 738287Mitochondrial matrixSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei171 – 19121HelicalPROSITE-ProRule annotationAdd
BLAST
Transmembranei216 – 23621HelicalPROSITE-ProRule annotationAdd
BLAST
Transmembranei313 – 33321HelicalPROSITE-ProRule annotationAdd
BLAST
Transmembranei408 – 42821HelicalPROSITE-ProRule annotationAdd
BLAST
Transmembranei431 – 45121HelicalPROSITE-ProRule annotationAdd
BLAST

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini171 – 457287ABC transmembrane type-1PROSITE-ProRule annotationAdd
BLAST
Domaini492 – 731240ABC transporterPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 ABC transmembrane type-1 domain.PROSITE-ProRule annotation
Contains 1 ABC transporter domain.PROSITE-ProRule annotation

Keywords - Domaini

Transit peptide, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG1132.
GeneTreeiENSGT00550000074497.
HOVERGENiHBG008358.
InParanoidiQ9NRK6.
KOiK05657.
OMAiIEVNRYN.
OrthoDBiEOG7Z3F4H.
PhylomeDBiQ9NRK6.
TreeFamiTF105198.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR003593. AAA+_ATPase.
IPR011527. ABC1_TM_dom.
IPR003439. ABC_transporter-like.
IPR017871. ABC_transporter_CS.
IPR001140. ABC_transptr_TM_dom.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF00664. ABC_membrane. 1 hit.
PF00005. ABC_tran. 1 hit.
[Graphical view]
SMARTiSM00382. AAA. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
SSF90123. SSF90123. 1 hit.
PROSITEiPS50929. ABC_TM1F. 1 hit.
PS00211. ABC_TRANSPORTER_1. 1 hit.
PS50893. ABC_TRANSPORTER_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q9NRK6-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MRGPPAWPLR LLEPPSPAEP GRLLPVACVW AAASRVPGSL SPFTGLRPAR
60 70 80 90 100
LWGAGPALLW GVGAARRWRS GCRGGGPGAS RGVLGLARLL GLWARGPGSC
110 120 130 140 150
RCGAFAGPGA PRLPRARFPG GPAAAAWAGD EAWRRGPAAP PGDKGRLRPA
160 170 180 190 200
AAGLPEARKL LGLAYPERRR LAAAVGFLTM SSVISMSAPF FLGKIIDVIY
210 220 230 240 250
TNPTVDYSDN LTRLCLGLSA VFLCGAAANA IRVYLMQTSG QRIVNRLRTS
260 270 280 290 300
LFSSILRQEV AFFDKTRTGE LINRLSSDTA LLGRSVTENL SDGLRAGAQA
310 320 330 340 350
SVGISMMFFV SPNLATFVLS VVPPVSIIAV IYGRYLRKLT KVTQDSLAQA
360 370 380 390 400
TQLAEERIGN VRTVRAFGKE MTEIEKYASK VDHVMQLARK EAFARAGFFG
410 420 430 440 450
ATGLSGNLIV LSVLYKGGLL MGSAHMTVGE LSSFLMYAFW VGISIGGLSS
460 470 480 490 500
FYSELMKGLG AGGRLWELLE REPKLPFNEG VILNEKSFQG ALEFKNVHFA
510 520 530 540 550
YPARPEVPIF QDFSLSIPSG SVTALVGPSG SGKSTVLSLL LRLYDPASGT
560 570 580 590 600
ISLDGHDIRQ LNPVWLRSKI GTVSQEPILF SCSIAENIAY GADDPSSVTA
610 620 630 640 650
EEIQRVAEVA NAVAFIRNFP QGFNTVVGEK GVLLSGGQKQ RIAIARALLK
660 670 680 690 700
NPKILLLDEA TSALDAENEY LVQEALDRLM DGRTVLVIAH RLSTIKNANM
710 720 730
VAVLDQGKIT EYGKHEELLS KPNGIYRKLM NKQSFISA
Length:738
Mass (Da):79,148
Last modified:April 3, 2007 - v2
Checksum:iC68B4FAC0F8B7E43
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti393 – 3931F → V in AAF78198. (PubMed:10922475)Curated
Sequence conflicti511 – 5111Q → K in AAA84438. (PubMed:7766993)Curated
Sequence conflicti558 – 5636IRQLNP → NPSAKPS in AAA84438. (PubMed:7766993)Curated
Sequence conflicti606 – 6116VAEVAN → GLKGQ in BAB20265. 1 PublicationCurated
Sequence conflicti615 – 6228FIRNFPQG → SPEFPPR in AAA84438. (PubMed:7766993)Curated
Sequence conflicti691 – 6911R → S in AAA84438. (PubMed:7766993)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti150 – 1501A → S.1 Publication
Corresponds to variant rs4148756 [ dbSNP | Ensembl ].
VAR_013702
Natural varianti242 – 2421R → G.
Corresponds to variant rs17584642 [ dbSNP | Ensembl ].
VAR_048133
Natural varianti471 – 4711R → T in a breast cancer sample; somatic mutation. 1 Publication
VAR_035735
Natural varianti545 – 5451D → N.1 Publication
Corresponds to variant rs35698797 [ dbSNP | Ensembl ].
VAR_031435

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF216833 mRNA. Translation: AAF78198.1.
AB013380 mRNA. Translation: BAB20265.1.
AL121990 Genomic DNA. Translation: CAI22012.1.
CH471098 Genomic DNA. Translation: EAW69901.1.
BC064930 mRNA. Translation: AAH64930.1.
U18237 mRNA. Translation: AAA84438.1.
CCDSiCCDS1580.1.
RefSeqiNP_036221.2. NM_012089.2.
UniGeneiHs.17614.

Genome annotation databases

EnsembliENST00000344517; ENSP00000355637; ENSG00000135776.
GeneIDi23456.
KEGGihsa:23456.
UCSCiuc001htp.4. human.

Polymorphism databases

DMDMi143811359.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

ABCMdb

Database for mutations in ABC proteins

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF216833 mRNA. Translation: AAF78198.1 .
AB013380 mRNA. Translation: BAB20265.1 .
AL121990 Genomic DNA. Translation: CAI22012.1 .
CH471098 Genomic DNA. Translation: EAW69901.1 .
BC064930 mRNA. Translation: AAH64930.1 .
U18237 mRNA. Translation: AAA84438.1 .
CCDSi CCDS1580.1.
RefSeqi NP_036221.2. NM_012089.2.
UniGenei Hs.17614.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3ZDQ X-ray 2.85 A 152-738 [» ]
4AYT X-ray 2.85 A 152-738 [» ]
4AYW X-ray 3.30 A 1-738 [» ]
4AYX X-ray 2.90 A 152-738 [» ]
ProteinModelPortali Q9NRK6.
SMRi Q9NRK6. Positions 153-722.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 117020. 14 interactions.
IntActi Q9NRK6. 1 interaction.
STRINGi 9606.ENSP00000355637.

Protein family/group databases

TCDBi 3.A.1.201.17. the atp-binding cassette (abc) superfamily.

PTM databases

PhosphoSitei Q9NRK6.

Polymorphism databases

DMDMi 143811359.

Proteomic databases

MaxQBi Q9NRK6.
PaxDbi Q9NRK6.
PRIDEi Q9NRK6.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000344517 ; ENSP00000355637 ; ENSG00000135776 .
GeneIDi 23456.
KEGGi hsa:23456.
UCSCi uc001htp.4. human.

Organism-specific databases

CTDi 23456.
GeneCardsi GC01M229652.
H-InvDB HIX0028493.
HGNCi HGNC:41. ABCB10.
HPAi CAB044063.
CAB044065.
MIMi 605454. gene.
neXtProti NX_Q9NRK6.
PharmGKBi PA24385.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1132.
GeneTreei ENSGT00550000074497.
HOVERGENi HBG008358.
InParanoidi Q9NRK6.
KOi K05657.
OMAi IEVNRYN.
OrthoDBi EOG7Z3F4H.
PhylomeDBi Q9NRK6.
TreeFami TF105198.

Enzyme and pathway databases

BRENDAi 3.6.3.43. 2681.
Reactomei REACT_111108. Mitochondrial ABC transporters.

Miscellaneous databases

GenomeRNAii 23456.
NextBioi 45747.
PROi Q9NRK6.
SOURCEi Search...

Gene expression databases

Bgeei Q9NRK6.
CleanExi HS_ABCB10.
ExpressionAtlasi Q9NRK6. baseline and differential.
Genevestigatori Q9NRK6.

Family and domain databases

Gene3Di 3.40.50.300. 1 hit.
InterProi IPR003593. AAA+_ATPase.
IPR011527. ABC1_TM_dom.
IPR003439. ABC_transporter-like.
IPR017871. ABC_transporter_CS.
IPR001140. ABC_transptr_TM_dom.
IPR027417. P-loop_NTPase.
[Graphical view ]
Pfami PF00664. ABC_membrane. 1 hit.
PF00005. ABC_tran. 1 hit.
[Graphical view ]
SMARTi SM00382. AAA. 1 hit.
[Graphical view ]
SUPFAMi SSF52540. SSF52540. 1 hit.
SSF90123. SSF90123. 1 hit.
PROSITEi PS50929. ABC_TM1F. 1 hit.
PS00211. ABC_TRANSPORTER_1. 1 hit.
PS50893. ABC_TRANSPORTER_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "M-ABC2, a new human mitochondrial ATP-binding cassette membrane protein."
    Zhang F., Hogue D.L., Liu L., Fisher C.L., Hui D., Childs S., Ling V.
    FEBS Lett. 478:89-94(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ASN-545.
    Tissue: Lymphoblast.
  2. "Human mono ATP-binding cassette protein."
    Ito K., Suzuki H., Sugiyama Y.
    Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. 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].
    Tissue: Eye.
  6. "Characterization and mapping of three new mammalian ATP-binding transporter genes from an EST database."
    Allikmets R., Gerrard B., Glavac D., Ravnik-Glavac M., Jenkins N.A., Gilbert D.J., Copeland N.G., Modi W., Dean M.
    Mamm. Genome 6:114-117(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 510-738.
  7. "Targeting, import, and dimerization of a mammalian mitochondrial ATP binding cassette (ABC) transporter, ABCB10 (ABC-me)."
    Graf S.A., Haigh S.E., Corson E.D., Shirihai O.S.
    J. Biol. Chem. 279:42954-42963(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: TRANSIT PEPTIDE CLEAVAGE SITE, SUBUNIT.
  8. "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-265, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. Cited for: X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS) OF 152-738 ALONE AND IN COMPLEX WITH ATP ANALOGS, ATP-BINDING REGION, SUBUNIT.
  11. "Three hundred twenty-six genetic variations in genes encoding nine members of ATP-binding cassette, subfamily B (ABCB/MDR/TAP), in the Japanese population."
    Saito S., Iida A., Sekine A., Miura Y., Ogawa C., Kawauchi S., Higuchi S., Nakamura Y.
    J. Hum. Genet. 47:38-50(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT SER-150.
  12. Cited for: VARIANT [LARGE SCALE ANALYSIS] THR-471.

Entry informationi

Entry nameiABCBA_HUMAN
AccessioniPrimary (citable) accession number: Q9NRK6
Secondary accession number(s): Q13040, Q6P1Q8, Q9H3V0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 2, 2002
Last sequence update: April 3, 2007
Last modified: October 29, 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: 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