Skip Header

Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot O96013 (PAK4_HUMAN)

Last modified February 9, 2010. Version 108. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Hide | Top

Names and origin

Protein namesRecommended name:
    Serine/threonine-protein kinase PAK 4
    EC=2.7.11.1
Alternative name(s):
    p21-activated kinase 4
      Short name=PAK-4
Gene names
Name: PAK4
Synonyms: KIAA1142
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Hide | Top

Protein attributes

Sequence length591 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level.

Hide | Top

General annotation (Comments)

Function

Activates the JNK pathway. Plays a role in the reorganization of the actin cytoskeleton and in the formation of filopodia. Phosphorylates and inactivates the protein phosphatase SSH1, leading to increased inhibitory phosphorylation of the actin binding/depolymerizing factor cofilin. Decreased cofilin activity may lead to stabilization of actin filaments. Phosphorylates ARHGEF2. Ref.8

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Subunit structure

Interacts with FGFR2 and GRB2 By similarity. Interacts tightly with GTP-bound but not GDP-bound CDC42/p21 and weakly with RAC1. Interacts with its substrate ARHGEF2. Ref.9

Tissue specificity

Highest expression in prostate, testis and colon.

Post-translational modification

Autophosphorylated on serine residues when activated by CDC42/p21. Ref.10 Ref.11 Ref.12 Ref.13 Ref.16

Phosphorylated on tyrosine residues upon stimulation of FGFR2 By similarity. Ref.10 Ref.11 Ref.12 Ref.13 Ref.16

Sequence similarities

Belongs to the protein kinase superfamily. STE Ser/Thr protein kinase family. STE20 subfamily.

Contains 1 CRIB domain.

Contains 1 protein kinase domain.

Hide | Top

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O96013-1)

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.
Isoform 2 (identifier: O96013-2)

The sequence of this isoform differs from the canonical sequence as follows:
     120-120: E → K
     121-285: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: O96013-3)

The sequence of this isoform differs from the canonical sequence as follows:
     69-221: Missing.
Isoform 4 (identifier: O96013-4)

The sequence of this isoform differs from the canonical sequence as follows:
     132-221: Missing.
Note: No experimental confirmation available.

Hide | Top

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 591591Serine/threonine-protein kinase PAK 4
PRO_0000086474

Regions

Domain11 – 2414CRIB
Domain321 – 572252Protein kinase
Nucleotide binding327 – 3359ATP By similarity
Region25 – 320296Linker
Region298 – 32326GEF-interaction domain (GID)

Sites

Active site4401Proton acceptor By similarity
Binding site3501ATP By similarity

Amino acid modifications

Modified residue411Phosphoserine Ref.12
Modified residue991Phosphoserine Ref.11
Modified residue1041Phosphoserine Ref.11 Ref.12
Modified residue1421Phosphoserine
Modified residue1481Phosphoserine Ref.11 Ref.12
Modified residue1671Phosphoserine Ref.11 Ref.12
Modified residue1811Phosphoserine Ref.11 Ref.12 Ref.13 Ref.16
Modified residue1871Phosphothreonine Ref.12
Modified residue1951Phosphoserine
Modified residue2071Phosphothreonine Ref.11 Ref.12
Modified residue2421Phosphoserine
Modified residue2581Phosphoserine Ref.12
Modified residue2671Phosphoserine Ref.11 Ref.12
Modified residue2771Phosphothreonine Ref.12
Modified residue2911Phosphoserine Ref.11 Ref.12
Modified residue4741Phosphoserine; by autocatalysis Ref.10 Ref.11 Ref.12 Ref.13 Ref.16

Natural variations

Alternative sequence69 – 221153Missing in isoform 3.
VSP_017572
Alternative sequence1201E → K in isoform 2.
VSP_004892
Alternative sequence121 – 285165Missing in isoform 2.
VSP_004893
Alternative sequence132 – 22190Missing in isoform 4.
VSP_017573
Natural variant1351R → Q: dbSNP rs56099436. Ref.18
VAR_040970
Natural variant1391A → T: dbSNP rs35655056. Ref.18
VAR_040971

Secondary structure

1 ............................................... 591
Helix Strand Turn

Details...

Hide | Top

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: 04C2A5C0B06427D5

FASTA59164,072
        10         20         30         40         50         60 
MFGKRKKRVE ISAPSNFEHR VHTGFDQHEQ KFTGLPRQWQ SLIEESARRP KPLVDPACIT 

        70         80         90        100        110        120 
SIQPGAPKTI VRGSKGAKDG ALTLLLDEFE NMSVTRSNSL RRDSPPPPAR ARQENGMPEE 

       130        140        150        160        170        180 
PATTARGGPG KAGSRGRFAG HSEAGGGSGD RRRAGPEKRP KSSREGSGGP QESSRDKRPL 

       190        200        210        220        230        240 
SGPDVGTPQP AGLASGAKLA AGRPFNTYPR ADTDHPSRGA QGEPHDVAPN GPSAGGLAIP 

       250        260        270        280        290        300 
QSSSSSSRPP TRARGAPSPG VLGPHASEPQ LAPPACTPAA PAVPGPPGPR SPQREPQRVS 

       310        320        330        340        350        360 
HEQFRAALQL VVDPGDPRSY LDNFIKIGEG STGIVCIATV RSSGKLVAVK KMDLRKQQRR 

       370        380        390        400        410        420 
ELLFNEVVIM RDYQHENVVE MYNSYLVGDE LWVVMEFLEG GALTDIVTHT RMNEEQIAAV 

       430        440        450        460        470        480 
CLAVLQALSV LHAQGVIHRD IKSDSILLTH DGRVKLSDFG FCAQVSKEVP RRKSLVGTPY 

       490        500        510        520        530        540 
WMAPELISRL PYGPEVDIWS LGIMVIEMVD GEPPYFNEPP LKAMKMIRDN LPPRLKNLHK 

       550        560        570        580        590 
VSPSLKGFLD RLLVRDPAQR ATAAELLKHP FLAKAGPPAS IVPLMRQNRT R

« Hide

Isoform 2.

Checksum: 505879690593E93A
Show »

FASTA42647,924
Isoform 3.

Checksum: 4A596EBBCECE9883
Show »

FASTA43848,268
Isoform 4.

Checksum: 6EE6240ECE65E79D
Show »

FASTA50154,940

Hide | Top

References

« Hide 'large scale' references
[1]"PAK4, a novel effector for Cdc42Hs, is implicated in the reorganization of the actin cytoskeleton and in the formation of filopodia."
Abo A., Qu J., Cammarano M.S., Dan C., Fritsch A., Baud V., Belisle B., Minden A.
EMBO J. 17:6527-6540(1998) [PubMed: 9822598] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Lymphoma.
[2]Melnick M.B.
Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Neuroblastoma.
[3]"Characterization of cDNA clones selected by the GeneMark analysis from size-fractionated cDNA libraries from human brain."
Hirosawa M., Nagase T., Ishikawa K., Kikuno R., Nomura N., Ohara O.
DNA Res. 6:329-336(1999) [PubMed: 10574461] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
Tissue: Brain.
[4]"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. expand/collapse author list , 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: 14702039] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 264-591 (ISOFORM 1).
Tissue: Brain and Teratocarcinoma.
[5]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed: 17974005] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
Tissue: Brain.
[6]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 4).
Tissue: Eye, Pancreas and Placenta.
[8]"Interplay between components of a novel LIM kinase-slingshot phosphatase complex regulates cofilin."
Soosairajah J., Maiti S., Wiggan O., Sarmiere P., Moussi N., Sarcevic B., Sampath R., Bamburg J.R., Bernard O.
EMBO J. 24:473-486(2005) [PubMed: 15660133] [Abstract]
Cited for: FUNCTION.
[9]"PAK4 mediates morphological changes through the regulation of GEF-H1."
Callow M.G., Zozulya S., Gishizky M.L., Jallal B., Smeal T.
J. Cell Sci. 118:1861-1872(2005) [PubMed: 15827085] [Abstract]
Cited for: INTERACTION WITH ARHGEF2.
[10]"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: 17081983] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-474, MASS SPECTROMETRY.
Tissue: Epithelium.
[11]"Proteomics analysis of protein kinases by target class-selective prefractionation and tandem mass spectrometry."
Wissing J., Jaensch L., Nimtz M., Dieterich G., Hornberger R., Keri G., Wehland J., Daub H.
Mol. Cell. Proteomics 6:537-547(2007) [PubMed: 17192257] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-99; SER-104; SER-148; SER-167; SER-181; THR-207; SER-267; SER-291 AND SER-474, MASS SPECTROMETRY.
[12]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed: 18691976] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-41; SER-104; SER-148; SER-167; SER-181; THR-187; THR-207; SER-258; SER-267; THR-277; SER-291 AND SER-474, MASS SPECTROMETRY.
[13]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181 AND SER-474, MASS SPECTROMETRY.
[14]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[15]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed: 19369195] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-41; SER-104; SER-142; SER-148; SER-167; SER-181; THR-187; SER-195; THR-207; SER-242; SER-258; SER-267; SER-291 AND SER-474, MASS SPECTROMETRY.
[16]"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: 19690332] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181 AND SER-474, MASS SPECTROMETRY.
Tissue: T-cell.
[17]"Crystal structure of the human p21-activated kinase 4."
Eswaran J., Debreczeni J.E., Bunkoczi G., Filippakopoulos P., Das S., Fedorov O., Sundstrom M., Arrowsmith C., Edwards A., von Delft F., Knapp S.
Submitted (JUL-2005) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 300-591, PHOSPHORYLATION AT SER-474.
[18]"Patterns of somatic mutation in human cancer genomes."
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G. expand/collapse author list , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
Nature 446:153-158(2007) [PubMed: 17344846] [Abstract]
Cited for: VARIANTS [LARGE SCALE ANALYSIS] GLN-135 AND THR-139.
+Additional computationally mapped references.

Hide | Top

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AJ011855 mRNA. Translation: CAA09820.1.
AF005046 mRNA. Translation: AAD01210.1.
AB032968 mRNA. Translation: BAA86456.1. Different initiation.
AK074728 mRNA. Translation: BAC11166.1. Different initiation.
AK294586 mRNA. Translation: BAG57777.1.
AL834236 mRNA. Translation: CAD38914.2.
CH471126 Genomic DNA. Translation: EAW56861.1.
BC002921 mRNA. Translation: AAH02921.1.
BC011368 mRNA. Translation: AAH11368.1.
BC025282 mRNA. Translation: AAH25282.1.
BC034511 mRNA. Translation: AAH34511.1.
IPIIPI00014068.
IPI00178714.
IPI00384231.
IPI00556065.
RefSeqNP_001014831.1.
NP_001014832.1.
NP_001014834.1.
NP_001014835.1.
NP_005875.1.
UniGeneHs.20447

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2BVAX-ray2.30A/B300-591[»]
2CDZX-ray2.30A291-591[»]
2J0IX-ray1.60A291-591[»]
2OV2X-ray2.10I/J/K/L/M/N/O/P10-44[»]
2Q0NX-ray1.75A291-591[»]
ModBaseSearch...

Protein-protein interaction databases

IntActO96013. 13 interactions.
STRINGO96013.

PTM databases

PhosphoSiteO96013.

Proteomic databases

PRIDEO96013.

Genome annotation databases

EnsemblENST00000358301; ENSP00000351049; ENSG00000130669; Homo sapiens. [Genome view]
ENST00000360442; ENSP00000353625; ENSG00000130669; Homo sapiens. [Genome view]
ENST00000435673; ENSP00000392753; ENSG00000130669; Homo sapiens. [Genome view]
GeneID10298.
KEGGhsa:10298.
UCSCuc002okj.1. human.
uc002okm.1. human.
uc002okp.1. human.

Organism-specific databases

CTD10298.
GeneCardsGC19P044274.
H-InvDBHIX0015110.
HGNCHGNC:16059. PAK4.
HPACAB025747.
MIM605451. gene.
PharmGKBPA32920.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG17248.
HOGENOMHBG755340.
HOVERGENO96013.
InParanoidO96013.
OMAARQENGM.
OrthoDBEOG9VX4QH.
PhylomeDBO96013.

Enzyme and pathway databases

BRENDA2.7.11.1. 247.
Pathway_Interaction_DBfgf_pathway. FGF signaling pathway.
ReactomeREACT_18266. Axon guidance.

Gene expression databases

ArrayExpressO96013.
BgeeO96013.
CleanExHS_PAK4.
GenevestigatorO96013.
GermOnlineENSG00000130669. Homo sapiens.

Family and domain databases

InterProIPR011009. Kinase-like_dom.
IPR000095. PAK_box_Rho_bd.
IPR000719. Prot_kinase_cat_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR017442. Se/Thr_prot_kinase-like_dom.
IPR015750. Ser/Thr_kinase_Pak-rel.
IPR002290. Ser/Thr_prot_kinase_dom.
[Graphical view]
PANTHERPTHR22986:SF84. Pak_like. 1 hit.
PfamPF00786. PBD. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]
SMARTSM00285. PBD. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
PROSITEPS50108. CRIB. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. False negative.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio39028.
SOURCESearch...

Hide | Top

Entry information

Entry namePAK4_HUMAN
AccessionPrimary (citable) accession number: O96013
Secondary accession number(s): B4DGG6 expand/collapse secondary AC list , Q8N4E1, Q8NCH5, Q8NDE3, Q9BU33, Q9ULS8
Entry history
Integrated into UniProtKB/Swiss-Prot: January 24, 2001
Last sequence update: May 1, 1999
Last modified: February 9, 2010
This is version 108 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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.

Hide | Top

Relevant documents

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents