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Protein

Tyrosine-protein kinase Fes/Fps

Gene

FES

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

Functioni

Tyrosine-protein kinase that acts downstream of cell surface receptors and plays a role in the regulation of the actin cytoskeleton, microtubule assembly, cell attachment and cell spreading. Plays a role in FCER1 (high affinity immunoglobulin epsilon receptor)-mediated signaling in mast cells. Acts down-stream of the activated FCER1 receptor and the mast/stem cell growth factor receptor KIT. Plays a role in the regulation of mast cell degranulation. Plays a role in the regulation of cell differentiation and promotes neurite outgrowth in response to NGF signaling. Plays a role in cell scattering and cell migration in response to HGF-induced activation of EZR. Phosphorylates BCR and down-regulates BCR kinase activity. Phosphorylates HCLS1/HS1, PECAM1, STAT3 and TRIM28.11 Publications

Miscellaneous

Cellular homolog of retroviral oncogenes. In contrast to the viral oncoproteins, the kinase activity of cellular FSP/FES is tightly regulated, and the kinase is inactive in normal cells in the absence of activating stimuli (PubMed:15485904).1 Publication

Catalytic activityi

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.PROSITE-ProRule annotation6 Publications

Enzyme regulationi

Kinase activity is tightly regulated. Activated in response to signaling from a cell surface receptor. Activation probably requires binding of a substrate via the SH2 domain, plus autophosphorylation at Tyr-713. Present in an inactive form in the absence of activating stimuli.2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei590ATPPROSITE-ProRule annotation1
Active sitei683Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi567 – 575ATPPROSITE-ProRule annotation9

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • immunoglobulin receptor binding Source: UniProtKB
  • microtubule binding Source: Ensembl
  • non-membrane spanning protein tyrosine kinase activity Source: UniProtKB
  • phosphatidylinositol binding Source: UniProtKB
  • protein tyrosine kinase activity Source: UniProtKB

GO - Biological processi

  • cell migration Source: GO_Central
  • cell proliferation Source: ProtInc
  • centrosome cycle Source: Ensembl
  • chemotaxis Source: GO_Central
  • epidermal growth factor receptor signaling pathway Source: GO_Central
  • innate immune response Source: GO_Central
  • microtubule bundle formation Source: Ensembl
  • multicellular organism development Source: ProtInc
  • peptidyl-tyrosine autophosphorylation Source: GO_Central
  • peptidyl-tyrosine phosphorylation Source: UniProtKB
  • positive regulation of actin cytoskeleton reorganization Source: UniProtKB
  • positive regulation of microtubule polymerization Source: UniProtKB
  • positive regulation of myeloid cell differentiation Source: UniProtKB
  • positive regulation of neuron projection development Source: UniProtKB
  • protein autophosphorylation Source: UniProtKB
  • protein phosphorylation Source: ProtInc
  • regulation of cell adhesion Source: UniProtKB
  • regulation of cell differentiation Source: UniProtKB
  • regulation of cell motility Source: UniProtKB
  • regulation of cell proliferation Source: UniProtKB
  • regulation of cell shape Source: UniProtKB
  • regulation of mast cell degranulation Source: UniProtKB
  • regulation of vesicle-mediated transport Source: UniProtKB

Keywordsi

Molecular functionKinase, Transferase, Tyrosine-protein kinase
LigandATP-binding, Lipid-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.10.2 2681
ReactomeiR-HSA-1433557 Signaling by SCF-KIT
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
SignaLinkiP07332
SIGNORiP07332

Names & Taxonomyi

Protein namesi
Recommended name:
Tyrosine-protein kinase Fes/Fps (EC:2.7.10.2)
Alternative name(s):
Feline sarcoma/Fujinami avian sarcoma oncogene homolog
Proto-oncogene c-Fes
Proto-oncogene c-Fps
p93c-fes
Gene namesi
Name:FES
Synonyms:FPS
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi

Organism-specific databases

EuPathDBiHostDB:ENSG00000182511.11
HGNCiHGNC:3657 FES
MIMi190030 gene
neXtProtiNX_P07332

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 junction, Cell membrane, Cytoplasm, Cytoplasmic vesicle, Cytoskeleton, Golgi apparatus, Membrane

Pathology & Biotechi

Involvement in diseasei

Has been shown to act as proto-oncogene in some types of cancer, possibly due to abnormal activation of the kinase. Has been shown to act as tumor suppressor in other types of cancer. Expressed and present as activated kinase in a subset of acute myeloid leukemia patients; promotes survival of leukemia cells (PubMed:20111072). Expression is absent in K562 leukemia cells; ectopic expression of FSP/FES restores myeloid differentiation (PubMed:2656706). May function as tumor suppressor in colorectal cancer; expression is reduced or absent in samples from some colon cancer patients (PubMed:16455651). Ectopic expression of FSP/FES suppresses anchorage-independent growth in colon cancer cell lines (PubMed:16455651). Up-regulated in prostate cancer, and might be a predictor of recurrence after radical surgery (PubMed:21563194). May promote growth of renal carcinoma cells (PubMed:19082481).5 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi113 – 114RK → EE: Reduced binding to membranes containing phosphoinositides. 1 Publication2
Mutagenesisi113 – 114RK → QQ: Reduced binding to membranes containing phosphoinositides. 1 Publication2
Mutagenesisi145L → P: Constitutively activated kinase that can act as oncogene. Promotes myeloid cell survival and proliferation. 2 Publications1
Mutagenesisi334L → P: Abolishes autophosphorylation. 1 Publication1
Mutagenesisi463G → V: Abolishes kinase activity. 1 Publication1
Mutagenesisi483R → M: Abolishes pTyr binding. Abolishes association with microtubules. Abolishes autophosphorylation. Reduced kinase activity. 2 Publications1
Mutagenesisi590K → E: Abolishes kinase activity. 1 Publication1
Mutagenesisi704M → V: Reduced autophosphorylation and strongly reduced kinase activity. 2 Publications1
Mutagenesisi706R → Q: Negligible effect on autophosphorylation and kinase activity. 2 Publications1
Mutagenesisi713Y → F: Reduces kinase activity by over 90%. 1 Publication1
Mutagenesisi743V → M: Strongly reduced autophosphorylation and kinase activity. 2 Publications1
Mutagenesisi759S → F: Reduced autophosphorylation and strongly reduced kinase activity. 2 Publications1

Keywords - Diseasei

Proto-oncogene, Tumor suppressor

Organism-specific databases

DisGeNETi2242
OpenTargetsiENSG00000182511
PharmGKBiPA28098

Chemistry databases

ChEMBLiCHEMBL5455
GuidetoPHARMACOLOGYi2023

Polymorphism and mutation databases

BioMutaiFES
DMDMi115502390

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000880881 – 822Tyrosine-protein kinase Fes/FpsAdd BLAST822

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei64PhosphoserineCombined sources1
Modified residuei67PhosphoserineCombined sources1
Modified residuei261PhosphotyrosineCombined sources1
Modified residuei408PhosphoserineCombined sources1
Modified residuei411PhosphoserineCombined sources1
Modified residuei421Phosphothreonine1 Publication1
Modified residuei713Phosphotyrosine; by autocatalysisCombined sources5 Publications1
Modified residuei716PhosphoserineCombined sources1

Post-translational modificationi

Autophosphorylated on Tyr-713. Phosphorylated by LYN in response to FCER1 activation. Phosphorylated by HCK.7 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiP07332
MaxQBiP07332
PaxDbiP07332
PeptideAtlasiP07332
PRIDEiP07332

PTM databases

iPTMnetiP07332
PhosphoSitePlusiP07332

Expressioni

Tissue specificityi

Widely expressed. Detected in adult colon epithelium.2 Publications

Gene expression databases

BgeeiENSG00000182511
CleanExiHS_FES
ExpressionAtlasiP07332 baseline and differential
GenevisibleiP07332 HS

Organism-specific databases

HPAiHPA001376

Interactioni

Subunit structurei

Homooligomer. Interacts with BCR. Interacts (when activated, via coiled coil domain) with TRIM28. Interacts (via SH2 domain) with phosphorylated EZR, MS4A2/FCER1B and HCLS1/HS1. Interacts with phosphorylated KIT. Interacts with FLT3. Interacts (via F-BAR domain) with soluble tubulin. Interacts (via SH2 domain) with microtubules.9 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

  • immunoglobulin receptor binding Source: UniProtKB
  • microtubule binding Source: Ensembl

Protein-protein interaction databases

BioGridi108533, 25 interactors
IntActiP07332, 22 interactors
MINTiP07332
STRINGi9606.ENSP00000331504

Chemistry databases

BindingDBiP07332

Structurei

Secondary structure

1822
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi3 – 6Combined sources4
Helixi10 – 51Combined sources42
Helixi68 – 96Combined sources29
Helixi98 – 131Combined sources34
Helixi133 – 154Combined sources22
Helixi167 – 202Combined sources36
Helixi204 – 234Combined sources31
Beta strandi236 – 238Combined sources3
Helixi239 – 254Combined sources16
Helixi257 – 259Combined sources3
Helixi262 – 268Combined sources7
Turni300 – 302Combined sources3
Helixi303 – 344Combined sources42
Helixi350 – 353Combined sources4
Helixi354 – 389Combined sources36
Turni390 – 393Combined sources4
Helixi450 – 452Combined sources3
Helixi455 – 457Combined sources3
Beta strandi461 – 464Combined sources4
Helixi467 – 473Combined sources7
Beta strandi479 – 484Combined sources6
Turni486 – 489Combined sources4
Beta strandi491 – 494Combined sources4
Beta strandi503 – 506Combined sources4
Beta strandi507 – 509Combined sources3
Beta strandi512 – 517Combined sources6
Beta strandi520 – 522Combined sources3
Helixi523 – 533Combined sources11
Turni539 – 541Combined sources3
Helixi558 – 560Combined sources3
Beta strandi561 – 570Combined sources10
Beta strandi573 – 580Combined sources8
Turni581 – 583Combined sources3
Beta strandi586 – 591Combined sources6
Helixi598 – 601Combined sources4
Helixi602 – 605Combined sources4
Helixi606 – 611Combined sources6
Beta strandi622 – 626Combined sources5
Beta strandi628 – 631Combined sources4
Beta strandi633 – 637Combined sources5
Helixi644 – 651Combined sources8
Helixi652 – 654Combined sources3
Helixi657 – 676Combined sources20
Helixi686 – 688Combined sources3
Beta strandi689 – 691Combined sources3
Beta strandi697 – 699Combined sources3
Helixi702 – 704Combined sources3
Beta strandi711 – 714Combined sources4
Beta strandi720 – 723Combined sources4
Helixi724 – 726Combined sources3
Helixi729 – 734Combined sources6
Beta strandi736 – 738Combined sources3
Helixi739 – 754Combined sources16
Turni755 – 757Combined sources3
Helixi766 – 774Combined sources9
Helixi787 – 796Combined sources10
Helixi801 – 803Combined sources3
Helixi807 – 820Combined sources14

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1WQUNMR-A450-550[»]
2DCRNMR-A450-550[»]
3BKBX-ray1.78A448-822[»]
3CBLX-ray1.75A448-822[»]
3CD3X-ray1.98A448-822[»]
4DYLX-ray2.18A1-405[»]
4E93X-ray1.84A448-822[»]
ProteinModelPortaliP07332
SMRiP07332
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP07332

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1 – 260F-BARPROSITE-ProRule annotationAdd BLAST260
Domaini460 – 549SH2PROSITE-ProRule annotationAdd BLAST90
Domaini561 – 822Protein kinasePROSITE-ProRule annotationAdd BLAST262

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 300Important for interaction with membranes containing phosphoinositidesAdd BLAST300

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili125 – 169Sequence analysisAdd BLAST45
Coiled coili324 – 368Sequence analysisAdd BLAST45

Domaini

The coiled coil domains are important for regulating the kinase activity. They mediate homooligomerization and probably also interaction with other proteins.
The N-terminal region including the first coiled coil domain mediates interaction with phosphoinositide-containing membranes.

Sequence similaritiesi

Belongs to the protein kinase superfamily. Tyr protein kinase family. Fes/fps subfamily.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, SH2 domain

Phylogenomic databases

eggNOGiKOG0194 Eukaryota
ENOG410Y6RP LUCA
GeneTreeiENSGT00760000119011
HOVERGENiHBG005655
InParanoidiP07332
KOiK07527
OMAiPKDKWAL
OrthoDBiEOG091G01S4
PhylomeDBiP07332
TreeFamiTF315363

Family and domain databases

CDDicd10361 SH2_Fps_family, 1 hit
Gene3Di1.20.1270.60, 1 hit
3.30.505.10, 1 hit
InterProiView protein in InterPro
IPR027267 AH/BAR_dom_sf
IPR031160 F_BAR
IPR001060 FCH_dom
IPR035849 Fes/Fps/Fer_SH2
IPR011009 Kinase-like_dom_sf
IPR000719 Prot_kinase_dom
IPR017441 Protein_kinase_ATP_BS
IPR001245 Ser-Thr/Tyr_kinase_cat_dom
IPR000980 SH2
IPR036860 SH2_dom_sf
IPR016250 Tyr-prot_kinase_Fes/Fps
IPR008266 Tyr_kinase_AS
IPR020635 Tyr_kinase_cat_dom
PfamiView protein in Pfam
PF07714 Pkinase_Tyr, 1 hit
PF00017 SH2, 1 hit
PIRSFiPIRSF000632 TyrPK_fps, 1 hit
PRINTSiPR00401 SH2DOMAIN
PR00109 TYRKINASE
SMARTiView protein in SMART
SM00055 FCH, 1 hit
SM00252 SH2, 1 hit
SM00219 TyrKc, 1 hit
SUPFAMiSSF103657 SSF103657, 1 hit
SSF55550 SSF55550, 1 hit
SSF56112 SSF56112, 1 hit
PROSITEiView protein in PROSITE
PS51741 F_BAR, 1 hit
PS00107 PROTEIN_KINASE_ATP, 1 hit
PS50011 PROTEIN_KINASE_DOM, 1 hit
PS00109 PROTEIN_KINASE_TYR, 1 hit
PS50001 SH2, 1 hit

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P07332-1) [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

        10         20         30         40         50
MGFSSELCSP QGHGVLQQMQ EAELRLLEGM RKWMAQRVKS DREYAGLLHH
60 70 80 90 100
MSLQDSGGQS RAISPDSPIS QSWAEITSQT EGLSRLLRQH AEDLNSGPLS
110 120 130 140 150
KLSLLIRERQ QLRKTYSEQW QQLQQELTKT HSQDIEKLKS QYRALARDSA
160 170 180 190 200
QAKRKYQEAS KDKDRDKAKD KYVRSLWKLF AHHNRYVLGV RAAQLHHQHH
210 220 230 240 250
HQLLLPGLLR SLQDLHEEMA CILKEILQEY LEISSLVQDE VVAIHREMAA
260 270 280 290 300
AAARIQPEAE YQGFLRQYGS APDVPPCVTF DESLLEEGEP LEPGELQLNE
310 320 330 340 350
LTVESVQHTL TSVTDELAVA TEMVFRRQEM VTQLQQELRN EEENTHPRER
360 370 380 390 400
VQLLGKRQVL QEALQGLQVA LCSQAKLQAQ QELLQTKLEH LGPGEPPPVL
410 420 430 440 450
LLQDDRHSTS SSEQEREGGR TPTLEILKSH ISGIFRPKFS LPPPLQLIPE
460 470 480 490 500
VQKPLHEQLW YHGAIPRAEV AELLVHSGDF LVRESQGKQE YVLSVLWDGL
510 520 530 540 550
PRHFIIQSLD NLYRLEGEGF PSIPLLIDHL LSTQQPLTKK SGVVLHRAVP
560 570 580 590 600
KDKWVLNHED LVLGEQIGRG NFGEVFSGRL RADNTLVAVK SCRETLPPDL
610 620 630 640 650
KAKFLQEARI LKQYSHPNIV RLIGVCTQKQ PIYIVMELVQ GGDFLTFLRT
660 670 680 690 700
EGARLRVKTL LQMVGDAAAG MEYLESKCCI HRDLAARNCL VTEKNVLKIS
710 720 730 740 750
DFGMSREEAD GVYAASGGLR QVPVKWTAPE ALNYGRYSSE SDVWSFGILL
760 770 780 790 800
WETFSLGASP YPNLSNQQTR EFVEKGGRLP CPELCPDAVF RLMEQCWAYE
810 820
PGQRPSFSTI YQELQSIRKR HR
Length:822
Mass (Da):93,497
Last modified:October 3, 2006 - v3
Checksum:i4C2A90555857F045
GO
Isoform 2 (identifier: P07332-2) [UniParc]FASTAAdd to basket
Also known as: Variant 1

The sequence of this isoform differs from the canonical sequence as follows:
     72-129: Missing.
     441-510: Missing.

Show »
Length:694
Mass (Da):78,633
Checksum:i9BFFA652C8C3B8EB
GO
Isoform 3 (identifier: P07332-3) [UniParc]FASTAAdd to basket
Also known as: Variant 3

The sequence of this isoform differs from the canonical sequence as follows:
     72-129: Missing.

Show »
Length:764
Mass (Da):86,663
Checksum:i3F3713631F1D08A2
GO
Isoform 4 (identifier: P07332-4) [UniParc]FASTAAdd to basket
Also known as: Variant 4

The sequence of this isoform differs from the canonical sequence as follows:
     441-510: Missing.

Show »
Length:752
Mass (Da):85,466
Checksum:i0580B667FEF3FDD1
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti719L → S in CAA36438 (PubMed:2179816).Curated1
Sequence conflicti719L → S in AAS82866 (Ref. 3) Curated1
Sequence conflicti719L → S in AAS82869 (Ref. 3) Curated1
Sequence conflicti719L → S in AAS82868 (Ref. 3) Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_04169785R → C1 PublicationCorresponds to variant dbSNP:rs56041861Ensembl.1
Natural variantiVAR_041698246R → Q1 PublicationCorresponds to variant dbSNP:rs34573430Ensembl.1
Natural variantiVAR_041699323M → V1 PublicationCorresponds to variant dbSNP:rs56296062Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_04174872 – 129Missing in isoform 2 and isoform 3. 2 PublicationsAdd BLAST58
Alternative sequenceiVSP_041749441 – 510Missing in isoform 2 and isoform 4. 2 PublicationsAdd BLAST70

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X52192 mRNA Translation: CAA36438.1
X06292 Genomic DNA Translation: CAA29619.1
AY513654 mRNA Translation: AAS82866.1
AY513656 mRNA Translation: AAS82868.1
AY513657 mRNA Translation: AAS82869.1
AK300595 mRNA Translation: BAG62292.1
AK312545 mRNA Translation: BAG35443.1
AC124248 Genomic DNA No translation available.
CH471101 Genomic DNA Translation: EAX02114.1
BC035357 mRNA Translation: AAH35357.1
CCDSiCCDS10365.1 [P07332-1]
CCDS45349.1 [P07332-4]
CCDS45350.1 [P07332-3]
CCDS45351.1 [P07332-2]
PIRiA24673 TVHUFF
RefSeqiNP_001137255.1, NM_001143783.1 [P07332-3]
NP_001137256.1, NM_001143784.1 [P07332-4]
NP_001137257.1, NM_001143785.1 [P07332-2]
NP_001996.1, NM_002005.3 [P07332-1]
XP_005254937.1, XM_005254880.1 [P07332-3]
XP_005254939.1, XM_005254882.1 [P07332-4]
XP_016877494.1, XM_017022005.1 [P07332-1]
XP_016877495.1, XM_017022006.1 [P07332-3]
XP_016877496.1, XM_017022007.1 [P07332-4]
XP_016877497.1, XM_017022008.1 [P07332-2]
XP_016877498.1, XM_017022009.1 [P07332-1]
XP_016877499.1, XM_017022010.1 [P07332-3]
UniGeneiHs.7636

Genome annotation databases

EnsembliENST00000328850; ENSP00000331504; ENSG00000182511 [P07332-1]
ENST00000394300; ENSP00000377837; ENSG00000182511 [P07332-3]
ENST00000414248; ENSP00000414629; ENSG00000182511 [P07332-2]
ENST00000444422; ENSP00000400868; ENSG00000182511 [P07332-4]
GeneIDi2242
KEGGihsa:2242
UCSCiuc002bpv.4 human [P07332-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Entry informationi

Entry nameiFES_HUMAN
AccessioniPrimary (citable) accession number: P07332
Secondary accession number(s): B2R6E6
, B4DUD0, E9PC94, E9PC95, Q2VXS7, Q2VXS8, Q2VXT0, Q6GTU5
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: October 3, 2006
Last modified: May 23, 2018
This is version 202 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 15
    Human chromosome 15: 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

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