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P33176

- KINH_HUMAN

UniProt

P33176 - KINH_HUMAN

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Protein

Kinesin-1 heavy chain

Gene
KIF5B, KNS, KNS1
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Microtubule-dependent motor required for normal distribution of mitochondria and lysosomes By similarity.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi85 – 928ATP

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. microtubule binding Source: HGNC
  3. microtubule motor activity Source: HGNC
  4. protein binding Source: UniProtKB

GO - Biological processi

  1. cellular protein metabolic process Source: Reactome
  2. cytoplasm organization Source: Ensembl
  3. microtubule-based movement Source: ProtInc
  4. positive regulation of establishment of protein localization to plasma membrane Source: BHF-UCL
  5. positive regulation of potassium ion transport Source: BHF-UCL
  6. regulation of membrane potential Source: BHF-UCL
  7. stress granule disassembly Source: BHF-UCL
  8. vesicle transport along microtubule Source: HGNC
Complete GO annotation...

Keywords - Molecular functioni

Motor protein

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_121399. MHC class II antigen presentation.
REACT_15550. Insulin processing.
REACT_25201. Kinesins.

Names & Taxonomyi

Protein namesi
Recommended name:
Kinesin-1 heavy chain
Alternative name(s):
Conventional kinesin heavy chain
Ubiquitous kinesin heavy chain
Short name:
UKHC
Gene namesi
Name:KIF5B
Synonyms:KNS, KNS1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 10

Organism-specific databases

HGNCiHGNC:6324. KIF5B.

Subcellular locationi

Cytoplasmcytoskeleton By similarity
Note: Uniformly distributed between soma and neurites in hippocampal neurons By similarity.

GO - Cellular componenti

  1. ciliary rootlet Source: Ensembl
  2. cytoplasm Source: HPA
  3. kinesin complex Source: ProtInc
  4. microtubule Source: UniProtKB-KW
  5. microtubule organizing center Source: HPA
  6. neuron projection Source: Ensembl
  7. perinuclear region of cytoplasm Source: HGNC
  8. vesicle Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Microtubule

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA30108.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 963962Kinesin-1 heavy chainPRO_0000125351Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine3 Publications
Modified residuei933 – 9331Phosphoserine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP33176.
PaxDbiP33176.
PRIDEiP33176.

PTM databases

PhosphoSiteiP33176.

Expressioni

Gene expression databases

ArrayExpressiP33176.
BgeeiP33176.
CleanExiHS_KIF5B.
GenevestigatoriP33176.

Organism-specific databases

HPAiCAB009846.
HPA037589.
HPA037590.

Interactioni

Subunit structurei

Oligomer composed of two heavy chains and two light chains. Interacts with GRIP1 and PPP1R42 By similarity. Interacts with SYBU. Interacts with JAKMIP1. Interacts with PLEKHM2. Interacts with ECM29.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
VACWR159P686193EBI-355878,EBI-7133540From a different organism.

Protein-protein interaction databases

BioGridi110000. 64 interactions.
DIPiDIP-29244N.
IntActiP33176. 22 interactions.
MINTiMINT-4999704.
STRINGi9606.ENSP00000307078.

Structurei

Secondary structure

1
963
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi8 – 158
Helixi20 – 256
Beta strandi32 – 343
Turni35 – 373
Beta strandi38 – 414
Beta strandi44 – 474
Beta strandi49 – 524
Helixi58 – 658
Helixi67 – 748
Beta strandi79 – 846
Helixi91 – 955
Turni102 – 1043
Helixi107 – 12216
Beta strandi124 – 13815
Beta strandi141 – 1466
Beta strandi155 – 1573
Beta strandi163 – 1653
Beta strandi171 – 1733
Helixi176 – 18914
Turni190 – 1934
Helixi197 – 2037
Beta strandi204 – 21613
Turni217 – 2193
Beta strandi222 – 23110
Helixi238 – 2414
Beta strandi242 – 2443
Helixi256 – 26914
Helixi277 – 2793
Helixi281 – 2855
Helixi286 – 2883
Beta strandi290 – 2934
Beta strandi295 – 3028
Helixi306 – 3083
Helixi309 – 32012
Beta strandi326 – 3294
Helixi337 – 34812

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BG2X-ray1.80A1-325[»]
1MKJX-ray2.70A1-349[»]
2P4Nelectron microscopy9.00K1-325[»]
4HNAX-ray3.19K1-349[»]
ProteinModelPortaliP33176.
SMRiP33176. Positions 3-325.

Miscellaneous databases

EvolutionaryTraceiP33176.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini8 – 325318Kinesin motorAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni915 – 96349GlobularAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili329 – 914586Add
BLAST

Domaini

Composed of three structural domains: a large globular N-terminal domain which is responsible for the motor activity of kinesin (it hydrolyzes ATP and binds microtubule), a central alpha-helical coiled coil domain that mediates the heavy chain dimerization; and a small globular C-terminal domain which interacts with other proteins (such as the kinesin light chains), vesicles and membranous organelles.

Sequence similaritiesi

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiCOG5059.
HOVERGENiHBG006210.
InParanoidiP33176.
KOiK10396.
OMAiLAECNIK.
OrthoDBiEOG7T4MJD.
PhylomeDBiP33176.
TreeFamiTF105225.

Family and domain databases

Gene3Di3.40.850.10. 1 hit.
InterProiIPR027640. Kinesin-like_fam.
IPR019821. Kinesin_motor_CS.
IPR001752. Kinesin_motor_dom.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR24115. PTHR24115. 1 hit.
PfamiPF00225. Kinesin. 1 hit.
[Graphical view]
PRINTSiPR00380. KINESINHEAVY.
SMARTiSM00129. KISc. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
PROSITEiPS00411. KINESIN_MOTOR_1. 1 hit.
PS50067. KINESIN_MOTOR_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P33176-1 [UniParc]FASTAAdd to Basket

« Hide

MADLAECNIK VMCRFRPLNE SEVNRGDKYI AKFQGEDTVV IASKPYAFDR    50
VFQSSTSQEQ VYNDCAKKIV KDVLEGYNGT IFAYGQTSSG KTHTMEGKLH 100
DPEGMGIIPR IVQDIFNYIY SMDENLEFHI KVSYFEIYLD KIRDLLDVSK 150
TNLSVHEDKN RVPYVKGCTE RFVCSPDEVM DTIDEGKSNR HVAVTNMNEH 200
SSRSHSIFLI NVKQENTQTE QKLSGKLYLV DLAGSEKVSK TGAEGAVLDE 250
AKNINKSLSA LGNVISALAE GSTYVPYRDS KMTRILQDSL GGNCRTTIVI 300
CCSPSSYNES ETKSTLLFGQ RAKTIKNTVC VNVELTAEQW KKKYEKEKEK 350
NKILRNTIQW LENELNRWRN GETVPIDEQF DKEKANLEAF TVDKDITLTN 400
DKPATAIGVI GNFTDAERRK CEEEIAKLYK QLDDKDEEIN QQSQLVEKLK 450
TQMLDQEELL ASTRRDQDNM QAELNRLQAE NDASKEEVKE VLQALEELAV 500
NYDQKSQEVE DKTKEYELLS DELNQKSATL ASIDAELQKL KEMTNHQKKR 550
AAEMMASLLK DLAEIGIAVG NNDVKQPEGT GMIDEEFTVA RLYISKMKSE 600
VKTMVKRCKQ LESTQTESNK KMEENEKELA ACQLRISQHE AKIKSLTEYL 650
QNVEQKKRQL EESVDALSEE LVQLRAQEKV HEMEKEHLNK VQTANEVKQA 700
VEQQIQSHRE THQKQISSLR DEVEAKAKLI TDLQDQNQKM MLEQERLRVE 750
HEKLKATDQE KSRKLHELTV MQDRREQARQ DLKGLEETVA KELQTLHNLR 800
KLFVQDLATR VKKSAEIDSD DTGGSAAQKQ KISFLENNLE QLTKVHKQLV 850
RDNADLRCEL PKLEKRLRAT AERVKALESA LKEAKENASR DRKRYQQEVD 900
RIKEAVRSKN MARRGHSAQI AKPIRPGQHP AASPTHPSAI RGGGAFVQNS 950
QPVAVRGGGG KQV 963
Length:963
Mass (Da):109,685
Last modified:October 1, 1993 - v1
Checksum:iA1FE5760C3250C8B
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X65873 mRNA. Translation: CAA46703.1.
AL161932 Genomic DNA. Translation: CAH71618.1.
BC126279 mRNA. Translation: AAI26280.1.
BC126281 mRNA. Translation: AAI26282.1.
CCDSiCCDS7171.1.
PIRiA41919.
RefSeqiNP_004512.1. NM_004521.2.
UniGeneiHs.327736.

Genome annotation databases

EnsembliENST00000302418; ENSP00000307078; ENSG00000170759.
GeneIDi3799.
KEGGihsa:3799.
UCSCiuc001iwe.4. human.

Polymorphism databases

DMDMi417216.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X65873 mRNA. Translation: CAA46703.1 .
AL161932 Genomic DNA. Translation: CAH71618.1 .
BC126279 mRNA. Translation: AAI26280.1 .
BC126281 mRNA. Translation: AAI26282.1 .
CCDSi CCDS7171.1.
PIRi A41919.
RefSeqi NP_004512.1. NM_004521.2.
UniGenei Hs.327736.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1BG2 X-ray 1.80 A 1-325 [» ]
1MKJ X-ray 2.70 A 1-349 [» ]
2P4N electron microscopy 9.00 K 1-325 [» ]
4HNA X-ray 3.19 K 1-349 [» ]
ProteinModelPortali P33176.
SMRi P33176. Positions 3-325.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 110000. 64 interactions.
DIPi DIP-29244N.
IntActi P33176. 22 interactions.
MINTi MINT-4999704.
STRINGi 9606.ENSP00000307078.

Chemistry

BindingDBi P33176.
ChEMBLi CHEMBL5864.

PTM databases

PhosphoSitei P33176.

Polymorphism databases

DMDMi 417216.

Proteomic databases

MaxQBi P33176.
PaxDbi P33176.
PRIDEi P33176.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000302418 ; ENSP00000307078 ; ENSG00000170759 .
GeneIDi 3799.
KEGGi hsa:3799.
UCSCi uc001iwe.4. human.

Organism-specific databases

CTDi 3799.
GeneCardsi GC10M032340.
HGNCi HGNC:6324. KIF5B.
HPAi CAB009846.
HPA037589.
HPA037590.
MIMi 602809. gene.
neXtProti NX_P33176.
PharmGKBi PA30108.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5059.
HOVERGENi HBG006210.
InParanoidi P33176.
KOi K10396.
OMAi LAECNIK.
OrthoDBi EOG7T4MJD.
PhylomeDBi P33176.
TreeFami TF105225.

Enzyme and pathway databases

Reactomei REACT_121399. MHC class II antigen presentation.
REACT_15550. Insulin processing.
REACT_25201. Kinesins.

Miscellaneous databases

ChiTaRSi KIF5B. human.
EvolutionaryTracei P33176.
GeneWikii KIF5B.
GenomeRNAii 3799.
NextBioi 14917.
PROi P33176.
SOURCEi Search...

Gene expression databases

ArrayExpressi P33176.
Bgeei P33176.
CleanExi HS_KIF5B.
Genevestigatori P33176.

Family and domain databases

Gene3Di 3.40.850.10. 1 hit.
InterProi IPR027640. Kinesin-like_fam.
IPR019821. Kinesin_motor_CS.
IPR001752. Kinesin_motor_dom.
IPR027417. P-loop_NTPase.
[Graphical view ]
PANTHERi PTHR24115. PTHR24115. 1 hit.
Pfami PF00225. Kinesin. 1 hit.
[Graphical view ]
PRINTSi PR00380. KINESINHEAVY.
SMARTi SM00129. KISc. 1 hit.
[Graphical view ]
SUPFAMi SSF52540. SSF52540. 1 hit.
PROSITEi PS00411. KINESIN_MOTOR_1. 1 hit.
PS50067. KINESIN_MOTOR_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and expression of a human kinesin heavy chain gene: interaction of the COOH-terminal domain with cytoplasmic microtubules in transfected CV-1 cells."
    Navone F., Niclas J., Hom-Booher N., Sparks L., Bernstein H.D., McCaffrey G., Vale R.D.
    J. Cell Biol. 117:1263-1275(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Placenta.
  2. "The DNA sequence and comparative analysis of human chromosome 10."
    Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
    , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
    Nature 429:375-381(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].
  4. "Syntabulin is a microtubule-associated protein implicated in syntaxin transport in neurons."
    Su Q., Cai Q., Gerwin C., Smith C.L., Sheng Z.-H.
    Nat. Cell Biol. 6:941-953(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SYBU.
  5. "The intracellular fate of Salmonella depends on the recruitment of kinesin."
    Boucrot E., Henry T., Borg J.-P., Gorvel J.-P., Meresse S.
    Science 308:1174-1178(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PLEKHM2.
  6. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. "Marlin-1 and conventional kinesin link GABAB receptors to the cytoskeleton and regulate receptor transport."
    Vidal R.L., Ramirez O.A., Sandoval L., Koenig-Robert R., Haertel S., Couve A.
    Mol. Cell. Neurosci. 35:501-512(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH JAKMIP1.
  8. "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].
  9. "A protein interaction network for Ecm29 links the 26 S proteasome to molecular motors and endosomal components."
    Gorbea C., Pratt G., Ustrell V., Bell R., Sahasrabudhe S., Hughes R.E., Rechsteiner M.
    J. Biol. Chem. 285:31616-31633(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ECM29.
  10. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-933, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "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].
  13. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "Crystal structure of the kinesin motor domain reveals a structural similarity to myosin."
    Kull F.J., Sablin E.P., Lau R., Fletterick R.J., Vale R.D.
    Nature 380:550-555(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 1-349 IN COMPLEX WITH ADP.
  15. "Two conformations in the human kinesin power stroke defined by X-ray crystallography and EPR spectroscopy."
    Sindelar C.V., Budny M.J., Rice S., Naber N., Fletterick R., Cooke R.
    Nat. Struct. Biol. 9:844-848(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 1-349 IN COMPLEX WITH ADP.
  16. "The beginning of kinesin's force-generating cycle visualized at 9-A resolution."
    Sindelar C.V., Downing K.H.
    J. Cell Biol. 177:377-385(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY ELECTRON MICROSCOPY (9.0 ANGSTROMS) OF 1-325.

Entry informationi

Entry nameiKINH_HUMAN
AccessioniPrimary (citable) accession number: P33176
Secondary accession number(s): A0AVB2, Q5VZ85
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: September 3, 2014
This is version 145 of the entry and version 1 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 10
    Human chromosome 10: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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