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Protein

Tyrosine-protein kinase Fyn

Gene

FYN

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

Functioni

Non-receptor tyrosine-protein kinase that plays a role in many biological processes including regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. Inactive FYN is phosphorylated on its C-terminal tail within the catalytic domain. Following activation by PKA, the protein subsequently associates with PTK2/FAK1, allowing PTK2/FAK1 phosphorylation, activation and targeting to focal adhesions. Involved in the regulation of cell adhesion and motility through phosphorylation of CTNNB1 (beta-catenin) and CTNND1 (delta-catenin). Regulates cytoskeletal remodeling by phosphorylating several proteins including the actin regulator WAS and the microtubule-associated proteins MAP2 and MAPT. Promotes cell survival by phosphorylating AGAP2/PIKE-A and preventing its apoptotic cleavage. Participates in signal transduction pathways that regulate the integrity of the glomerular slit diaphragm (an essential part of the glomerular filter of the kidney) by phosphorylating several slit diaphragm components including NPHS1, KIRREL and TRPC6. Plays a role in neural processes by phosphorylating DPYSL2, a multifunctional adapter protein within the central nervous system, ARHGAP32, a regulator for Rho family GTPases implicated in various neural functions, and SNCA, a small pre-synaptic protein. Participates in the downstream signaling pathways that lead to T-cell differentiation and proliferation following T-cell receptor (TCR) stimulation. Also participates in negative feedback regulation of TCR signaling through phosphorylation of PAG1, thereby promoting interaction between PAG1 and CSK and recruitment of CSK to lipid rafts. CSK maintains LCK and FYN in an inactive form. Promotes CD28-induced phosphorylation of VAV1.19 Publications

Catalytic activityi

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.PROSITE-ProRule annotation

Cofactori

Enzyme regulationi

Inhibited by phosphorylation of Tyr-531 by leukocyte common antigen and activated by dephosphorylation of this site.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei299ATPPROSITE-ProRule annotation1
Active sitei390Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi277 – 285ATPPROSITE-ProRule annotation9

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionDevelopmental protein, Kinase, Transferase, Tyrosine-protein kinase
Biological processAdaptive immunity, Host-virus interaction, Immunity
LigandATP-binding, Manganese, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.10.2. 2681.
ReactomeiR-HSA-114604. GPVI-mediated activation cascade.
R-HSA-1227986. Signaling by ERBB2.
R-HSA-1257604. PIP3 activates AKT signaling.
R-HSA-1266695. Interleukin-7 signaling.
R-HSA-1433557. Signaling by SCF-KIT.
R-HSA-1433559. Regulation of KIT signaling.
R-HSA-164944. Nef and signal transduction.
R-HSA-202733. Cell surface interactions at the vascular wall.
R-HSA-2029481. FCGR activation.
R-HSA-210990. PECAM1 interactions.
R-HSA-2219530. Constitutive Signaling by Aberrant PI3K in Cancer.
R-HSA-2424491. DAP12 signaling.
R-HSA-2682334. EPH-Ephrin signaling.
R-HSA-2730905. Role of LAT2/NTAL/LAB on calcium mobilization.
R-HSA-373753. Nephrin family interactions.
R-HSA-375165. NCAM signaling for neurite out-growth.
R-HSA-389356. CD28 co-stimulation.
R-HSA-389357. CD28 dependent PI3K/Akt signaling.
R-HSA-389359. CD28 dependent Vav1 pathway.
R-HSA-389513. CTLA4 inhibitory signaling.
R-HSA-3928662. EPHB-mediated forward signaling.
R-HSA-3928663. EPHA-mediated growth cone collapse.
R-HSA-3928664. Ephrin signaling.
R-HSA-3928665. EPH-ephrin mediated repulsion of cells.
R-HSA-399954. Sema3A PAK dependent Axon repulsion.
R-HSA-399955. SEMA3A-Plexin repulsion signaling by inhibiting Integrin adhesion.
R-HSA-399956. CRMPs in Sema3A signaling.
R-HSA-418885. DCC mediated attractive signaling.
R-HSA-418886. Netrin mediated repulsion signals.
R-HSA-4420097. VEGFA-VEGFR2 Pathway.
R-HSA-5621480. Dectin-2 family.
R-HSA-5621575. CD209 (DC-SIGN) signaling.
R-HSA-5673001. RAF/MAP kinase cascade.
R-HSA-6811558. PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
R-HSA-75892. Platelet Adhesion to exposed collagen.
R-HSA-8866376. Reelin signalling pathway.
R-HSA-912631. Regulation of signaling by CBL.
R-HSA-983695. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
SignaLinkiP06241.
SIGNORiP06241.

Names & Taxonomyi

Protein namesi
Recommended name:
Tyrosine-protein kinase Fyn (EC:2.7.10.2)
Alternative name(s):
Proto-oncogene Syn
Proto-oncogene c-Fyn
Src-like kinase
Short name:
SLK
p59-Fyn
Gene namesi
Name:FYN
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 6

Organism-specific databases

EuPathDBiHostDB:ENSG00000010810.17.
HGNCiHGNC:4037. FYN.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane, Nucleus

Pathology & Biotechi

Keywords - Diseasei

Proto-oncogene

Organism-specific databases

DisGeNETi2534.
OpenTargetsiENSG00000010810.
PharmGKBiPA28454.

Chemistry databases

ChEMBLiCHEMBL1841.
DrugBankiDB02078. 1-Methoxy-2-[2-(2-Methoxy-Ethoxy]-Ethane.
DB01254. Dasatinib.
GuidetoPHARMACOLOGYi2026.

Polymorphism and mutation databases

BioMutaiFYN.
DMDMi125370.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved
ChainiPRO_00000880992 – 537Tyrosine-protein kinase FynAdd BLAST536

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Lipidationi2N-myristoyl glycine1 Publication1
Lipidationi3S-palmitoyl cysteineBy similarity1
Lipidationi6S-palmitoyl cysteineBy similarity1
Modified residuei12Phosphothreonine; by PKC1 Publication1
Modified residuei21PhosphoserineCombined sources1
Modified residuei26PhosphoserineCombined sources1
Modified residuei124PhosphoserineBy similarity1
Modified residuei181PhosphothreonineBy similarity1
Modified residuei185PhosphotyrosineBy similarity1
Modified residuei214PhosphotyrosineBy similarity1
Modified residuei420Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei531Phosphotyrosine; by CSKCombined sources1 Publication1

Post-translational modificationi

Autophosphorylated at Tyr-420. Phosphorylation on the C-terminal tail at Tyr-531 by CSK maintains the enzyme in an inactive state (By similarity). PTPRC/CD45 dephosphorylates Tyr-531 leading to activation. Ultraviolet B (UVB) strongly increase phosphorylation at Thr-12 and kinase activity, and promotes translocation from the cytoplasm to the nucleus. Dephosphorylation at Tyr-420 by PTPN2 negatively regulates T-cell receptor signaling.By similarity4 Publications
Palmitoylation at Cys-3 and Cys-6 regulates subcellular location.By similarity

Keywords - PTMi

Lipoprotein, Myristate, Palmitate, Phosphoprotein

Proteomic databases

EPDiP06241.
MaxQBiP06241.
PaxDbiP06241.
PeptideAtlasiP06241.
PRIDEiP06241.

PTM databases

iPTMnetiP06241.
PhosphoSitePlusiP06241.
SwissPalmiP06241.

Miscellaneous databases

PMAP-CutDBiP06241.

Expressioni

Tissue specificityi

Isoform 1 is highly expressed in the brain. Isoform 2 is expressed in cells of hemopoietic lineages, especially T-lymphocytes.1 Publication

Gene expression databases

BgeeiENSG00000010810.
CleanExiHS_FYN.
ExpressionAtlasiP06241. baseline and differential.
GenevisibleiP06241. HS.

Organism-specific databases

HPAiCAB005034.
CAB018387.
HPA023887.
HPA063770.

Interactioni

Subunit structurei

Interacts (via its SH3 domain) with PIK3R1 and PRMT8. Interacts with FYB1, PAG1, and SH2D1A. Interacts with CD79A (tyrosine-phosphorylated form); the interaction increases FYN activity. Interacts (via SH2 domain) with CSF1R (tyrosine phosphorylated) (By similarity). Interacts with TOM1L1 (phosphorylated form). Interacts with KDR (tyrosine phosphorylated). Interacts (via SH3 domain) with KLHL2 (via N-terminus) (By similarity). Interacts with SH2D1A and SLAMF1. Interacts (via its SH3 domain) with HEV ORF3 protein. Interacts with ITCH; the interaction phosphorylates ITCH and negatively regulates its activity. Interacts with FASLG. Interacts with RUNX3. Interacts with KIT. Interacts with EPHA8; possible downstream effector of EPHA8 in regulation of cell adhesion. Interacts with PTK2/FAK1; this interaction leads to PTK2/FAK1 phosphorylation and activation. Interacts with CAV1; this interaction couples integrins to the Ras-ERK pathway. Interacts with UNC119. Interacts (via SH2 domain) with PTPRH (phosphorylated form) (By similarity). Interacts with PTPRO (phosphorylated form) (By similarity). Interacts with PTPRB (phosphorylated form) (By similarity). Interacts with FYB2 (PubMed:27335501).By similarity15 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

Protein-protein interaction databases

BioGridi108810. 187 interactors.
CORUMiP06241.
DIPiDIP-33876N.
ELMiP06241.
IntActiP06241. 250 interactors.
MINTiMINT-93594.
STRINGi9606.ENSP00000346671.

Chemistry databases

BindingDBiP06241.

Structurei

Secondary structure

1537
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi87 – 91Combined sources5
Beta strandi96 – 100Combined sources5
Beta strandi108 – 113Combined sources6
Beta strandi115 – 124Combined sources10
Turni125 – 127Combined sources3
Beta strandi130 – 134Combined sources5
Helixi135 – 137Combined sources3
Beta strandi138 – 141Combined sources4
Helixi144 – 146Combined sources3
Beta strandi147 – 150Combined sources4
Helixi156 – 163Combined sources8
Turni165 – 167Combined sources3
Beta strandi172 – 177Combined sources6
Beta strandi179 – 181Combined sources3
Beta strandi185 – 193Combined sources9
Turni194 – 196Combined sources3
Beta strandi197 – 207Combined sources11
Turni209 – 211Combined sources3
Beta strandi213 – 216Combined sources4
Beta strandi219 – 223Combined sources5
Helixi224 – 233Combined sources10
Beta strandi238 – 240Combined sources3
Beta strandi263 – 265Combined sources3
Helixi268 – 270Combined sources3
Beta strandi271 – 278Combined sources8
Beta strandi285 – 290Combined sources6
Turni291 – 293Combined sources3
Beta strandi294 – 299Combined sources6
Turni303 – 305Combined sources3
Helixi308 – 318Combined sources11
Beta strandi329 – 333Combined sources5
Beta strandi335 – 337Combined sources3
Beta strandi339 – 343Combined sources5
Helixi350 – 354Combined sources5
Beta strandi355 – 357Combined sources3
Turni358 – 360Combined sources3
Helixi364 – 383Combined sources20
Helixi393 – 395Combined sources3
Beta strandi396 – 399Combined sources4
Turni400 – 402Combined sources3
Beta strandi403 – 406Combined sources4
Beta strandi416 – 418Combined sources3
Turni430 – 432Combined sources3
Helixi435 – 438Combined sources4
Helixi445 – 460Combined sources16
Helixi472 – 481Combined sources10
Helixi496 – 502Combined sources7
Helixi507 – 509Combined sources3
Helixi513 – 521Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1A0NNMR-B80-148[»]
1AOTNMR-F143-248[»]
1AOUNMR-F143-248[»]
1AVZX-ray3.00C85-141[»]
1AZGNMR-B82-148[»]
1EFNX-ray2.50A/C86-143[»]
1FYNX-ray2.30A81-142[»]
1G83X-ray2.60A/B82-246[»]
1M27X-ray2.50C84-144[»]
1NYFNMR-A82-148[»]
1NYGNMR-A82-148[»]
1SHFX-ray1.90A/B84-142[»]
1ZBJNMR-A84-142[»]
2DQ7X-ray2.80X261-537[»]
2MQINMR-A148-248[»]
2MRJNMR-A148-248[»]
2MRKNMR-A149-248[»]
B528-537[»]
3H0FX-ray2.61A73-142[»]
3H0HX-ray1.76A73-142[»]
3H0IX-ray2.20A/B73-142[»]
3UA6X-ray1.85A/B81-143[»]
3UA7X-ray1.50A/B/C/D81-143[»]
4D8DX-ray2.52A/C84-141[»]
4EIKX-ray1.60A81-143[»]
4U17X-ray1.99A/B/C148-248[»]
4U1PX-ray1.40A148-248[»]
4ZNXX-ray2.10A/B/C/D84-141[»]
ProteinModelPortaliP06241.
SMRiP06241.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP06241.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini82 – 143SH3PROSITE-ProRule annotationAdd BLAST62
Domaini149 – 246SH2PROSITE-ProRule annotationAdd BLAST98
Domaini271 – 524Protein kinasePROSITE-ProRule annotationAdd BLAST254

Sequence similaritiesi

Belongs to the protein kinase superfamily. Tyr protein kinase family. SRC subfamily.PROSITE-ProRule annotation

Keywords - Domaini

SH2 domain, SH3 domain

Phylogenomic databases

eggNOGiKOG0197. Eukaryota.
COG0515. LUCA.
GeneTreeiENSGT00760000118938.
HOVERGENiHBG008761.
InParanoidiP06241.
KOiK05703.
OMAiSHNSGYR.
OrthoDBiEOG091G0D46.
PhylomeDBiP06241.
TreeFamiTF351634.

Family and domain databases

Gene3Di3.30.505.10. 1 hit.
InterProiView protein in InterPro
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR000980. SH2.
IPR001452. SH3_domain.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
PfamiView protein in Pfam
PF07714. Pkinase_Tyr. 1 hit.
PF00017. SH2. 1 hit.
PF00018. SH3_1. 1 hit.
PRINTSiPR00401. SH2DOMAIN.
PR00452. SH3DOMAIN.
PR00109. TYRKINASE.
SMARTiView protein in SMART
SM00252. SH2. 1 hit.
SM00326. SH3. 1 hit.
SM00219. TyrKc. 1 hit.
SUPFAMiSSF50044. SSF50044. 1 hit.
SSF55550. SSF55550. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiView protein in PROSITE
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
PS50001. SH2. 1 hit.
PS50002. SH3. 1 hit.

Sequences (3)i

Sequence statusi: Complete.

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

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P06241-1) [UniParc]FASTAAdd to basket
Also known as: B

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

        10         20         30         40         50
MGCVQCKDKE ATKLTEERDG SLNQSSGYRY GTDPTPQHYP SFGVTSIPNY
60 70 80 90 100
NNFHAAGGQG LTVFGGVNSS SHTGTLRTRG GTGVTLFVAL YDYEARTEDD
110 120 130 140 150
LSFHKGEKFQ ILNSSEGDWW EARSLTTGET GYIPSNYVAP VDSIQAEEWY
160 170 180 190 200
FGKLGRKDAE RQLLSFGNPR GTFLIRESET TKGAYSLSIR DWDDMKGDHV
210 220 230 240 250
KHYKIRKLDN GGYYITTRAQ FETLQQLVQH YSERAAGLCC RLVVPCHKGM
260 270 280 290 300
PRLTDLSVKT KDVWEIPRES LQLIKRLGNG QFGEVWMGTW NGNTKVAIKT
310 320 330 340 350
LKPGTMSPES FLEEAQIMKK LKHDKLVQLY AVVSEEPIYI VTEYMNKGSL
360 370 380 390 400
LDFLKDGEGR ALKLPNLVDM AAQVAAGMAY IERMNYIHRD LRSANILVGN
410 420 430 440 450
GLICKIADFG LARLIEDNEY TARQGAKFPI KWTAPEAALY GRFTIKSDVW
460 470 480 490 500
SFGILLTELV TKGRVPYPGM NNREVLEQVE RGYRMPCPQD CPISLHELMI
510 520 530
HCWKKDPEER PTFEYLQSFL EDYFTATEPQ YQPGENL
Length:537
Mass (Da):60,762
Last modified:January 23, 2007 - v3
Checksum:i4A1E443A4B5A0977
GO
Isoform 2 (identifier: P06241-2) [UniParc]FASTAAdd to basket
Also known as: T

The sequence of this isoform differs from the canonical sequence as follows:
     234-287: RAAGLCCRLV...GNGQFGEVWM → KADGLCFNLT...GQGCFAEVWL

Show »
Length:534
Mass (Da):60,141
Checksum:iFA082D40A24C2802
GO
Isoform 3 (identifier: P06241-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     233-287: Missing.

Note: No experimental confirmation available.
Show »
Length:482
Mass (Da):54,513
Checksum:i055C3965AC5A9135
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti184A → S in AAA36615 (PubMed:3099169).Curated1
Sequence conflicti437A → R in AAA36615 (PubMed:3099169).Curated1
Sequence conflicti437A → R in AAB33113 (PubMed:7822789).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_041704243V → L in a lung squamous cell carcinoma sample; somatic mutation. 1 Publication1
Natural variantiVAR_041705410G → R in a metastatic melanoma sample; somatic mutation. 1 Publication1
Natural variantiVAR_014661445I → F. Corresponds to variant dbSNP:rs1801121Ensembl.1
Natural variantiVAR_041706506D → E1 PublicationCorresponds to variant dbSNP:rs28763975Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_024108233 – 287Missing in isoform 3. 1 PublicationAdd BLAST55
Alternative sequenceiVSP_024110234 – 287RAAGL…GEVWM → KADGLCFNLTVIASSCTPQT SGLAKDAWEVARRSLCLEKK LGQGCFAEVWL in isoform 2. 1 PublicationAdd BLAST54

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M14676 mRNA. Translation: AAA36615.1.
M14333 mRNA. Translation: AAC08285.1.
S74774 mRNA. Translation: AAB33113.2.
AB451293 mRNA. Translation: BAG70107.1.
AB451426 mRNA. Translation: BAG70240.1.
Z97989 Genomic DNA. Translation: CAI22300.1.
Z97989 Genomic DNA. Translation: CAI22301.1.
CH471051 Genomic DNA. Translation: EAW48278.1.
CH471051 Genomic DNA. Translation: EAW48279.1.
CH471051 Genomic DNA. Translation: EAW48281.1.
CH471051 Genomic DNA. Translation: EAW48282.1.
CH471051 Genomic DNA. Translation: EAW48283.1.
BC032496 mRNA. Translation: AAH32496.1.
CCDSiCCDS5094.1. [P06241-1]
CCDS5095.1. [P06241-2]
CCDS5096.1. [P06241-3]
PIRiA24314. TVHUSY.
RefSeqiNP_002028.1. NM_002037.5. [P06241-1]
NP_694592.1. NM_153047.3. [P06241-2]
NP_694593.1. NM_153048.3. [P06241-3]
XP_005266947.1. XM_005266890.3. [P06241-2]
XP_005266949.1. XM_005266892.3. [P06241-3]
XP_016866139.1. XM_017010650.1. [P06241-1]
XP_016866140.1. XM_017010651.1. [P06241-1]
XP_016866141.1. XM_017010652.1. [P06241-1]
XP_016866142.1. XM_017010653.1. [P06241-1]
XP_016866143.1. XM_017010654.1. [P06241-1]
UniGeneiHs.390567.
Hs.664520.

Genome annotation databases

EnsembliENST00000229471; ENSP00000229471; ENSG00000010810. [P06241-3]
ENST00000354650; ENSP00000346671; ENSG00000010810. [P06241-1]
ENST00000368667; ENSP00000357656; ENSG00000010810. [P06241-1]
ENST00000368678; ENSP00000357667; ENSG00000010810. [P06241-2]
ENST00000368682; ENSP00000357671; ENSG00000010810. [P06241-2]
ENST00000538466; ENSP00000440646; ENSG00000010810. [P06241-2]
GeneIDi2534.
KEGGihsa:2534.
UCSCiuc003pvh.3. human. [P06241-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Similar proteinsi

Entry informationi

Entry nameiFYN_HUMAN
AccessioniPrimary (citable) accession number: P06241
Secondary accession number(s): B5BU57
, E1P557, H0UI48, Q16248, Q5R3A6, Q5R3A7, Q8N5D7
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 23, 2007
Last modified: September 27, 2017
This is version 226 of the entry and version 3 of the sequence. See 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 6
    Human chromosome 6: 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. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  7. SIMILARITY comments
    Index of protein domains and families