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Q9H0B6

- KLC2_HUMAN

UniProt

Q9H0B6 - KLC2_HUMAN

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Protein
Kinesin light chain 2
Gene
KLC2
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Kinesin is a microtubule-associated force-producing protein that may play a role in organelle transport. The light chain may function in coupling of cargo to the heavy chain or in the modulation of its ATPase activity By similarity.

GO - Molecular functioni

  1. kinesin binding Source: BHF-UCL
  2. microtubule motor activity Source: InterPro
  3. protein binding Source: HGNC

GO - Biological processi

  1. antigen processing and presentation of exogenous peptide antigen via MHC class II Source: Reactome
  2. axon cargo transport Source: Ensembl
  3. blood coagulation Source: Reactome
  4. microtubule-based movement Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Motor protein

Enzyme and pathway databases

ReactomeiREACT_121399. MHC class II antigen presentation.
REACT_25201. Kinesins.

Names & Taxonomyi

Protein namesi
Recommended name:
Kinesin light chain 2
Short name:
KLC 2
Gene namesi
Name:KLC2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 11

Organism-specific databases

HGNCiHGNC:20716. KLC2.

Subcellular locationi

Cytoplasmcytoskeleton Inferred

GO - Cellular componenti

  1. ciliary rootlet Source: Ensembl
  2. cytosol Source: HGNC
  3. kinesin I complex Source: BHF-UCL
  4. kinesin complex Source: HGNC
  5. microtubule Source: UniProtKB-KW
  6. neuron projection Source: Ensembl
  7. protein complex Source: LIFEdb
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Microtubule

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA142671587.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 622622Kinesin light chain 2
PRO_0000215095Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei151 – 1511Phosphoserine1 Publication
Modified residuei445 – 4451Phosphoserine3 Publications
Modified residuei581 – 5811Phosphoserine1 Publication
Modified residuei582 – 5821Phosphoserine3 Publications
Modified residuei589 – 5891Phosphoserine2 Publications
Modified residuei610 – 6101Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9H0B6.
PaxDbiQ9H0B6.
PRIDEiQ9H0B6.

PTM databases

PhosphoSiteiQ9H0B6.

Expressioni

Gene expression databases

ArrayExpressiQ9H0B6.
BgeeiQ9H0B6.
CleanExiHS_KLC2.
GenevestigatoriQ9H0B6.

Organism-specific databases

HPAiHPA040416.
HPA040434.

Interactioni

Subunit structurei

Oligomeric complex composed of two heavy chains and two light chains By similarity.

Protein-protein interaction databases

BioGridi122313. 28 interactions.
IntActiQ9H0B6. 10 interactions.
MINTiMINT-1401363.
STRINGi9606.ENSP00000314837.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi217 – 23216
Beta strandi234 – 2363
Helixi237 – 25216
Helixi256 – 27318
Helixi279 – 29315
Turni294 – 2963
Helixi298 – 31619
Helixi321 – 33515
Turni336 – 3383
Helixi340 – 35718
Helixi363 – 37917
Helixi382 – 40019
Beta strandi401 – 4033
Helixi411 – 42010
Helixi446 – 46116
Helixi465 – 47612

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3CEQX-ray2.75A/B217-480[»]
3EDTX-ray2.70B/D/F/H217-480[»]
ProteinModelPortaliQ9H0B6.
SMRiQ9H0B6. Positions 179-515.

Miscellaneous databases

EvolutionaryTraceiQ9H0B6.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati198 – 23134TPR 1
Add
BLAST
Repeati240 – 27334TPR 2
Add
BLAST
Repeati282 – 31534TPR 3
Add
BLAST
Repeati324 – 35734TPR 4
Add
BLAST
Repeati366 – 39934TPR 5
Add
BLAST
Repeati449 – 48234TPR 6
Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili78 – 14366 Reviewed prediction
Add
BLAST

Sequence similaritiesi

Contains 6 TPR repeats.

Keywords - Domaini

Coiled coil, Repeat, TPR repeat

Phylogenomic databases

eggNOGiCOG0457.
HOGENOMiHOG000261663.
HOVERGENiHBG006217.
InParanoidiQ9H0B6.
KOiK10407.
OMAiNNDNKPI.
OrthoDBiEOG7TXKGD.
PhylomeDBiQ9H0B6.
TreeFamiTF314010.

Family and domain databases

Gene3Di1.25.40.10. 2 hits.
InterProiIPR002151. Kinesin_light.
IPR015792. Kinesin_light_repeat.
IPR015390. Rabaptin_Rab5-bd_dom.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical.
IPR013105. TPR_2.
IPR019734. TPR_repeat.
[Graphical view]
PfamiPF09311. Rab5-bind. 1 hit.
PF07719. TPR_2. 1 hit.
[Graphical view]
PRINTSiPR00381. KINESINLIGHT.
SMARTiSM00028. TPR. 4 hits.
[Graphical view]
PROSITEiPS01160. KINESIN_LIGHT. 2 hits.
PS50005. TPR. 5 hits.
PS50293. TPR_REGION. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9H0B6-1) [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

MAMMVFPREE KLSQDEIVLG TKAVIQGLET LRGEHRALLA PLVAPEAGEA    50
EPGSQERCIL LRRSLEAIEL GLGEAQVILA LSSHLGAVES EKQKLRAQVR 100
RLVQENQWLR EELAGTQQKL QRSEQAVAQL EEEKQHLLFM SQIRKLDEDA 150
SPNEEKGDVP KDTLDDLFPN EDEQSPAPSP GGGDVSGQHG GYEIPARLRT 200
LHNLVIQYAS QGRYEVAVPL CKQALEDLEK TSGHDHPDVA TMLNILALVY 250
RDQNKYKEAA HLLNDALAIR EKTLGKDHPA VAATLNNLAV LYGKRGKYKE 300
AEPLCKRALE IREKVLGKFH PDVAKQLSNL ALLCQNQGKA EEVEYYYRRA 350
LEIYATRLGP DDPNVAKTKN NLASCYLKQG KYQDAETLYK EILTRAHEKE 400
FGSVNGDNKP IWMHAEEREE SKDKRRDSAP YGEYGSWYKA CKVDSPTVNT 450
TLRSLGALYR RQGKLEAAHT LEDCASRNRK QGLDPASQTK VVELLKDGSG 500
RRGDRRSSRD MAGGAGPRSE SDLEDVGPTA EWNGDGSGSL RRSGSFGKLR 550
DALRRSSEML VKKLQGGTPQ EPPNPRMKRA SSLNFLNKSV EEPTQPGGTG 600
LSDSRTLSSS SMDLSRRSSL VG 622
Length:622
Mass (Da):68,935
Last modified:March 1, 2001 - v1
Checksum:i5B57ABE4DF6E396E
GO
Isoform 2 (identifier: Q9H0B6-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     77-153: Missing.

Note: No experimental confirmation available.

Show »
Length:545
Mass (Da):60,047
Checksum:iB30B27FA163B5D47
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti517 – 5171P → S.
Corresponds to variant rs2276036 [ dbSNP | Ensembl ].
VAR_020379

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei77 – 15377Missing in isoform 2.
VSP_043486Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti6 – 61F → Y in BAB14302. 1 Publication
Sequence conflicti306 – 3061K → R in BAB14039. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AL136864 mRNA. Translation: CAB66798.1.
AK022449 mRNA. Translation: BAB14039.1.
AK022907 mRNA. Translation: BAB14302.1.
AK094593 mRNA. Translation: BAG52895.1.
AK315725 mRNA. Translation: BAG38081.1.
AP000759 Genomic DNA. No translation available.
AP001107 Genomic DNA. No translation available.
BC034373 mRNA. Translation: AAH34373.1.
CCDSiCCDS44653.1. [Q9H0B6-2]
CCDS8130.1. [Q9H0B6-1]
RefSeqiNP_001128246.1. NM_001134774.1. [Q9H0B6-2]
NP_001128247.1. NM_001134775.1. [Q9H0B6-1]
NP_001128248.1. NM_001134776.1. [Q9H0B6-1]
NP_073733.1. NM_022822.2. [Q9H0B6-1]
XP_005274239.1. XM_005274182.1. [Q9H0B6-1]
XP_005274240.1. XM_005274183.1. [Q9H0B6-1]
UniGeneiHs.280792.

Genome annotation databases

EnsembliENST00000316924; ENSP00000314837; ENSG00000174996. [Q9H0B6-1]
ENST00000394066; ENSP00000377630; ENSG00000174996. [Q9H0B6-2]
ENST00000394067; ENSP00000377631; ENSG00000174996. [Q9H0B6-1]
ENST00000417856; ENSP00000399403; ENSG00000174996. [Q9H0B6-1]
ENST00000421552; ENSP00000408484; ENSG00000174996. [Q9H0B6-2]
GeneIDi64837.
KEGGihsa:64837.
UCSCiuc001ohb.2. human. [Q9H0B6-1]
uc001ohd.2. human. [Q9H0B6-2]

Polymorphism databases

DMDMi13878553.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AL136864 mRNA. Translation: CAB66798.1 .
AK022449 mRNA. Translation: BAB14039.1 .
AK022907 mRNA. Translation: BAB14302.1 .
AK094593 mRNA. Translation: BAG52895.1 .
AK315725 mRNA. Translation: BAG38081.1 .
AP000759 Genomic DNA. No translation available.
AP001107 Genomic DNA. No translation available.
BC034373 mRNA. Translation: AAH34373.1 .
CCDSi CCDS44653.1. [Q9H0B6-2 ]
CCDS8130.1. [Q9H0B6-1 ]
RefSeqi NP_001128246.1. NM_001134774.1. [Q9H0B6-2 ]
NP_001128247.1. NM_001134775.1. [Q9H0B6-1 ]
NP_001128248.1. NM_001134776.1. [Q9H0B6-1 ]
NP_073733.1. NM_022822.2. [Q9H0B6-1 ]
XP_005274239.1. XM_005274182.1. [Q9H0B6-1 ]
XP_005274240.1. XM_005274183.1. [Q9H0B6-1 ]
UniGenei Hs.280792.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3CEQ X-ray 2.75 A/B 217-480 [» ]
3EDT X-ray 2.70 B/D/F/H 217-480 [» ]
ProteinModelPortali Q9H0B6.
SMRi Q9H0B6. Positions 179-515.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 122313. 28 interactions.
IntActi Q9H0B6. 10 interactions.
MINTi MINT-1401363.
STRINGi 9606.ENSP00000314837.

PTM databases

PhosphoSitei Q9H0B6.

Polymorphism databases

DMDMi 13878553.

Proteomic databases

MaxQBi Q9H0B6.
PaxDbi Q9H0B6.
PRIDEi Q9H0B6.

Protocols and materials databases

DNASUi 64837.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000316924 ; ENSP00000314837 ; ENSG00000174996 . [Q9H0B6-1 ]
ENST00000394066 ; ENSP00000377630 ; ENSG00000174996 . [Q9H0B6-2 ]
ENST00000394067 ; ENSP00000377631 ; ENSG00000174996 . [Q9H0B6-1 ]
ENST00000417856 ; ENSP00000399403 ; ENSG00000174996 . [Q9H0B6-1 ]
ENST00000421552 ; ENSP00000408484 ; ENSG00000174996 . [Q9H0B6-2 ]
GeneIDi 64837.
KEGGi hsa:64837.
UCSCi uc001ohb.2. human. [Q9H0B6-1 ]
uc001ohd.2. human. [Q9H0B6-2 ]

Organism-specific databases

CTDi 64837.
GeneCardsi GC11P066026.
HGNCi HGNC:20716. KLC2.
HPAi HPA040416.
HPA040434.
MIMi 611729. gene.
neXtProti NX_Q9H0B6.
PharmGKBi PA142671587.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0457.
HOGENOMi HOG000261663.
HOVERGENi HBG006217.
InParanoidi Q9H0B6.
KOi K10407.
OMAi NNDNKPI.
OrthoDBi EOG7TXKGD.
PhylomeDBi Q9H0B6.
TreeFami TF314010.

Enzyme and pathway databases

Reactomei REACT_121399. MHC class II antigen presentation.
REACT_25201. Kinesins.

Miscellaneous databases

EvolutionaryTracei Q9H0B6.
GeneWikii KLC2.
GenomeRNAii 64837.
NextBioi 66920.
PROi Q9H0B6.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9H0B6.
Bgeei Q9H0B6.
CleanExi HS_KLC2.
Genevestigatori Q9H0B6.

Family and domain databases

Gene3Di 1.25.40.10. 2 hits.
InterProi IPR002151. Kinesin_light.
IPR015792. Kinesin_light_repeat.
IPR015390. Rabaptin_Rab5-bd_dom.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical.
IPR013105. TPR_2.
IPR019734. TPR_repeat.
[Graphical view ]
Pfami PF09311. Rab5-bind. 1 hit.
PF07719. TPR_2. 1 hit.
[Graphical view ]
PRINTSi PR00381. KINESINLIGHT.
SMARTi SM00028. TPR. 4 hits.
[Graphical view ]
PROSITEi PS01160. KINESIN_LIGHT. 2 hits.
PS50005. TPR. 5 hits.
PS50293. TPR_REGION. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Testis.
  2. "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).
    Tissue: Mammary gland and Testis.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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).
    Tissue: Lymph.
  5. "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.
  6. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
    Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
    Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-445, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-445; SER-582 AND SER-589, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  9. "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-151; SER-445; SER-581; SER-582 AND SER-589, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-582 AND SER-610, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiKLC2_HUMAN
AccessioniPrimary (citable) accession number: Q9H0B6
Secondary accession number(s): A8MXL7
, B2RDY4, Q9H9C8, Q9HA20
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: March 1, 2001
Last modified: September 3, 2014
This is version 136 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 11
    Human chromosome 11: 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

Similar proteinsi