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Q9UQ88 (CD11A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 137. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cyclin-dependent kinase 11A

EC=2.7.11.22
Alternative name(s):
Cell division cycle 2-like protein kinase 2
Cell division protein kinase 11A
Galactosyltransferase-associated protein kinase p58/GTA
PITSLRE serine/threonine-protein kinase CDC2L2
Gene names
Name:CDK11A
Synonyms:CDC2L2, CDC2L3, PITSLREB
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length783 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Appears to play multiple roles in cell cycle progression, cytokinesis and apoptosis. The p110 isoforms have been suggested to be involved in pre-mRNA splicing, potentially by phosphorylating the splicing protein SFRS7. The p58 isoform mayact as a negative regulator of normal cell cycle progression. Ref.5 Ref.7

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Cofactor

Magnesium.

Enzyme regulation

Phosphorylation at Thr-436 or Tyr-437 inactivates the enzyme, while phosphorylation at Thr-583 activates it By similarity.

Subunit structure

The cleaved p110 isoform, p110C, binds to the serine/threonine kinase PAK1. The p58 isoform butnot the p110 isoform orp110C interacts with CCND3. The p110 isoforms are found in large molecular weight complexes containing CCNL1 and SFRS7. Ref.5 Ref.7

Subcellular location

Cytoplasm. Nucleus Ref.1 Ref.5.

Tissue specificity

Expressed ubiquitously. Some evidence of isoform-specific tissue distribution. Ref.1 Ref.2

Induction

The p58 isoform isspecifically induced in G2/M phase of the cell cycle. Ref.6

Post-translational modification

During apoptosis, induced by Fas or tumor necrosis factor, specific CKD11 p110 isoforms are cleaved by caspases to produce a protein (p110C) that contains the C-terminal kinase domain of the CDK11 proteins.

Miscellaneous

Duplicated gene. CDK11A and CDK11B encode almost identical protein kinases of 110 kDa that contain at their C-termini the open reading frame of a smaller 58 kDa isoform whichis expressed following IRES-mediated alternative initiation of translation.

Sequence similarities

Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. CDC2/CDKX subfamily.

Contains 1 protein kinase domain.

Caution

Many references talk about 'p110 isoforms' but it is not yet known if this refers to CDK11A and/or CDK11B or one/some of the isoforms of each.

Sequence caution

The sequence AAC95297.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence AAC95298.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence AAC95299.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence AAC95300.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence AAC95302.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence AAC95303.1 differs from that shown. Reason: Erroneous gene model prediction.

Alternative products

This entry describes 8 isoforms produced by alternative splicing and alternative initiation. [Align] [Select]

Note: Additional isoforms seem to exist.
Isoform SV6 (identifier: Q9UQ88-1)

Also known as: p110;

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 SV1 (identifier: Q9UQ88-2)

Also known as: Pbeta21; Beta 2-1;

The sequence of this isoform differs from the canonical sequence as follows:
     109-109: W → CRHHSHSAEGG
     240-253: GEARPAPAQKPAQL → V
Isoform SV2 (identifier: Q9UQ88-3)

Also known as: Pbeta22;

The sequence of this isoform differs from the canonical sequence as follows:
     153-153: R → RGNDGFCLFR
     240-253: GEARPAPAQKPAQL → V
Isoform SV3 (identifier: Q9UQ88-4)

The sequence of this isoform differs from the canonical sequence as follows:
     240-253: GEARPAPAQKPAQL → V
Isoform SV7 (identifier: Q9UQ88-5)

Also known as: SV8;

The sequence of this isoform differs from the canonical sequence as follows:
     1-386: Missing.
     387-418: SALTEGDYVPDSPALLPIELKQELPKYLPALQ → MKNEKMKTTSWLFQSHGSTEIPGRVKKQRKKW
Isoform SV12 (identifier: Q9UQ88-8)

The sequence of this isoform differs from the canonical sequence as follows:
     1-616: Missing.
     617-658: GELLTQKPLF...IWPGYSELPV → MGKTEEKGNG...QDAGAAEGAA
Isoform SV13 (identifier: Q9UQ88-9)

The sequence of this isoform differs from the canonical sequence as follows:
     1-57: Missing.
     153-153: R → RGNDGFCLFR
     240-253: GEARPAPAQKPAQL → V
     567-600: GDFGLAREYGSPLKAYTPVVVTQWYRAPELLLGA → SPPPSGPSQGDPPGPTHSRPSVVAGG
     601-783: Missing.
Isoform 4 (identifier: Q9UQ88-10)

Also known as: Beta 1; p58;

The sequence of this isoform differs from the canonical sequence as follows:
     1-344: Missing.
Note: Produced by alternative initiation at Met-345 of isoform SV6.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 783783Cyclin-dependent kinase 11A
PRO_0000024315

Regions

Domain427 – 647221Protein kinase
Nucleotide binding432 – 4409ATP By similarity
Compositional bias15 – 381367Glu-rich

Sites

Active site5501Proton acceptor By similarity
Binding site4551ATP By similarity

Amino acid modifications

Modified residue4701Phosphoserine; by CDK7 By similarity
Modified residue4761Phosphothreonine; by CDK7 By similarity
Modified residue5771Phosphoserine By similarity
Modified residue5821Phosphotyrosine By similarity
Modified residue5831Phosphothreonine By similarity

Natural variations

Alternative sequence1 – 616616Missing in isoform SV12.
VSP_008284
Alternative sequence1 – 386386Missing in isoform SV7.
VSP_008283
Alternative sequence1 – 344344Missing in isoform 4.
VSP_018836
Alternative sequence1 – 5757Missing in isoform SV13.
VSP_008281
Alternative sequence1091W → CRHHSHSAEGG in isoform SV1.
VSP_008286
Alternative sequence1531R → RGNDGFCLFR in isoform SV2 and isoform SV13.
VSP_008287
Alternative sequence240 – 25314GEARP…KPAQL → V in isoform SV1, isoform SV2, isoform SV3 and isoform SV13.
VSP_008288
Alternative sequence387 – 41832SALTE…LPALQ → MKNEKMKTTSWLFQSHGSTE IPGRVKKQRKKW in isoform SV7.
VSP_008289
Alternative sequence567 – 60034GDFGL…LLLGA → SPPPSGPSQGDPPGPTHSRP SVVAGG in isoform SV13.
VSP_008290
Alternative sequence601 – 783183Missing in isoform SV13.
VSP_008291
Alternative sequence617 – 65842GELLT…SELPV → MGKTEEKGNGKGAFQERKGP LGAVRKEAGAGAQDAGAAEG AA in isoform SV12.
VSP_008292
Natural variant571C → R.
Corresponds to variant rs17424353 [ dbSNP | Ensembl ].
VAR_060152
Natural variant921S → P.
Corresponds to variant rs7531938 [ dbSNP | Ensembl ].
VAR_062200
Natural variant931R → W. Ref.2 Ref.3
Corresponds to variant rs1059831 [ dbSNP | Ensembl ].
VAR_031716
Natural variant4021L → S. Ref.1
Corresponds to variant rs1059828 [ dbSNP | Ensembl ].
VAR_031717
Natural variant6581V → A.
Corresponds to variant rs1059811 [ dbSNP | Ensembl ].
VAR_060153

Experimental info

Sequence conflict1091Missing in AAA19594. Ref.1
Sequence conflict1091Missing in AAA19595. Ref.1
Sequence conflict2461P → R in AAC72087. Ref.2
Sequence conflict312 – 3143Missing in AAA19594. Ref.1
Sequence conflict312 – 3143Missing in AAA19595. Ref.1
Sequence conflict312 – 3143Missing in AAC72084. Ref.2
Sequence conflict312 – 3143Missing in AAC72085. Ref.2
Sequence conflict312 – 3143Missing in AAC72086. Ref.2
Sequence conflict312 – 3143Missing in AAC72087. Ref.2
Sequence conflict312 – 3143Missing in AAC72090. Ref.2
Sequence conflict4241E → D in AAA19585. Ref.1
Sequence conflict4241E → D in AAA19594. Ref.1
Sequence conflict4241E → D in AAA19595. Ref.1
Sequence conflict4631K → N in AAA19585. Ref.1
Sequence conflict4631K → N in AAA19594. Ref.1
Sequence conflict4631K → N in AAA19595. Ref.1
Sequence conflict6661E → R in AAA19585. Ref.1
Sequence conflict6661E → R in AAA19594. Ref.1
Sequence conflict6661E → R in AAA19595. Ref.1
Sequence conflict6821D → E in AAA19585. Ref.1
Sequence conflict6821D → E in AAA19594. Ref.1
Sequence conflict6821D → E in AAA19595. Ref.1
Isoform SV1:
Sequence conflict1091C → R in AAA19594. Ref.1
Sequence conflict1121H → R in AAA19594. Ref.1
Isoform SV2:
Sequence conflict1581F → V in AAA19595. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform SV6 (p110) [UniParc].

Last modified January 11, 2011. Version 4.
Checksum: 1BCF67EB180F37C6

FASTA78391,362
        10         20         30         40         50         60 
MGDEKDSWKV KTLDEILQEK KRRKEQEEKA EIKRLKNSDD RDSKRDSLEE GELRDHCMEI 

        70         80         90        100        110        120 
TIRNSPYRRE DSMEDRGEED DSLAIKPPQQ MSRKEKVHHR KDEKRKEKWK HARVKEREHE 

       130        140        150        160        170        180 
RRKRHREEQD KARREWERQK RREMAREHSR RERDRLEQLE RKRERERKMR EQQKEQREQK 

       190        200        210        220        230        240 
ERERRAEERR KEREARREVS AHHRTMREDY SDKVKASHWS RSPPRPPRER FELGDGRKPG 

       250        260        270        280        290        300 
EARPAPAQKP AQLKEEKMEE RDLLSDLQDI SDSERKTSSA ESSSAESGSG SEEEEEEEEE 

       310        320        330        340        350        360 
EEEEGSTSEE SEEEEEEEEE EEEETGSNSE EASEQSAEEV SEEEMSEDEE RENENHLLVV 

       370        380        390        400        410        420 
PESRFDRDSG ESEEAEEEVG EGTPQSSALT EGDYVPDSPA LLPIELKQEL PKYLPALQGC 

       430        440        450        460        470        480 
RSVEEFQCLN RIEEGTYGVV YRAKDKKTDE IVALKRLKME KEKEGFPITS LREINTILKA 

       490        500        510        520        530        540 
QHPNIVTVRE IVVGSNMDKI YIVMNYVEHD LKSLMETMKQ PFLPGEVKTL MIQLLRGVKH 

       550        560        570        580        590        600 
LHDNWILHRD LKTSNLLLSH AGILKVGDFG LAREYGSPLK AYTPVVVTQW YRAPELLLGA 

       610        620        630        640        650        660 
KEYSTAVDMW SVGCIFGELL TQKPLFPGNS EIDQINKVFK ELGTPSEKIW PGYSELPVVK 

       670        680        690        700        710        720 
KMTFSEHPYN NLRKRFGALL SDQGFDLMNK FLTYFPGRRI SAEDGLKHEY FRETPLPIDP 

       730        740        750        760        770        780 
SMFPTWPAKS EQQRVKRGTS PRPPEGGLGY SQLGDDDLKE TGFHLTTTNQ GASAAGPGFS 


LKF 

« Hide

Isoform SV1 (Pbeta21) (Beta 2-1) [UniParc].

Checksum: 5AA5206CBAFAA15B
Show »

FASTA78091,018
Isoform SV2 (Pbeta22) [UniParc].

Checksum: 519C680FC20A1250
Show »

FASTA77991,055
Isoform SV3 [UniParc].

Checksum: 44D5D04CACDB2519
Show »

FASTA77090,045
Isoform SV7 (SV8) [UniParc].

Checksum: 36B4BA8EE75D95C6
Show »

FASTA39745,229
Isoform SV12 [UniParc].

Checksum: F769BDEC242A9044
Show »

FASTA16718,110
Isoform SV13 [UniParc].

Checksum: 1BAA7CD839B07A06
Show »

FASTA53162,316
Isoform 4 (Beta 1) (p58) [UniParc].

Checksum: 3DCA65216905266A
Show »

FASTA43949,624

References

« Hide 'large scale' references
[1]"Molecular cloning and expression of alternatively spliced PITSLRE protein kinase isoforms."
Xiang J., Lahti J.M., Grenet J.A., Easton J.B., Kidd V.J.
J. Biol. Chem. 269:15786-15794(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS SV1; SV2 AND 4), TISSUE SPECIFICITY, SUBCELLULAR LOCATION, VARIANT SER-402.
Tissue: Cervix carcinoma.
[2]"Duplication of a genomic region containing the Cdc2L1-2 and MMP21-22 genes on human chromosome 1p36.3 and their linkage to D1Z2."
Gururajan R., Lahti J.M., Grenet J.A., Easton J., Gruber I., Ambros P.F., Kidd V.J.
Genome Res. 8:929-939(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS SV1; SV2; SV3; SV6; SV7; SV12 AND SV13), TISSUE SPECIFICITY, VARIANT TRP-93.
Tissue: Cervix carcinoma.
[3]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT TRP-93.
[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 SV7).
Tissue: Skin.
[5]"CDK11 complexes promote pre-mRNA splicing."
Hu D., Mayeda A., Trembley J.H., Lahti J.M., Kidd V.J.
J. Biol. Chem. 278:8623-8629(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CCNL1 AND SFRS7.
[6]"Identification and characterization of a novel cell cycle-regulated internal ribosome entry site."
Cornelis S., Bruynooghe Y., Denecker G., Van Huffel S., Tinton S., Beyaert R.
Mol. Cell 5:597-605(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: ALTERNATIVE INITIATION (ISOFORM 4), INDUCTION.
[7]"The C-terminal kinase domain of the p34cdc2-related PITSLRE protein kinase (p110C) associates with p21-activated kinase 1 and inhibits its activity during anoikis."
Chen S., Yin X., Zhu X., Yan J., Ji S., Chen C., Cai M., Zhang S., Zong H., Hu Y., Yuan Z., Shen Z., Gu J.
J. Biol. Chem. 278:20029-20036(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH PAK1.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U04819 mRNA. Translation: AAA19585.1.
U07704 mRNA. Translation: AAA19594.1.
U07705 mRNA. Translation: AAA19595.1.
AF067518 mRNA. Translation: AAC72083.1.
AF067519 mRNA. Translation: AAC72084.1.
AF067520 mRNA. Translation: AAC72085.1.
AF067521 mRNA. Translation: AAC72086.1.
AF067522 mRNA. Translation: AAC72087.1.
AF067523 mRNA. Translation: AAC72088.1.
AF067524 mRNA. Translation: AAC72089.1.
AF067525 mRNA. Translation: AAC72090.1.
AF067526 mRNA. Translation: AAC72091.1.
AF067527 mRNA. Translation: AAC72092.1.
AF067528 mRNA. Translation: AAC72093.1.
AF067529 mRNA. Translation: AAC72094.1.
AF080694 expand/collapse EMBL AC list , AF080695, AF105714, AF080696, AF080697, AF092427, AF092428, AF080689, AF080690, AF080691, AF080692, AF080693 Genomic DNA. Translation: AAC95297.1. Sequence problems.
AF080694 expand/collapse EMBL AC list , AF080695, AF105714, AF080696, AF080697, AF092427, AF092428, AF080689, AF080690, AF080691, AF080692, AF080693 Genomic DNA. Translation: AAC95298.1. Sequence problems.
AF080694 expand/collapse EMBL AC list , AF080695, AF105714, AF080696, AF080697, AF092427, AF092428, AF080689, AF080690, AF080691, AF080692, AF080693 Genomic DNA. Translation: AAC95299.1. Sequence problems.
AF080694 expand/collapse EMBL AC list , AF080695, AF105714, AF080696, AF080697, AF092427, AF092428, AF080689, AF080690, AF080691, AF080692, AF080693 Genomic DNA. Translation: AAC95300.1. Sequence problems.
AF080697 expand/collapse EMBL AC list , AF080695, AF105714, AF080696 Genomic DNA. Translation: AAC95302.1. Sequence problems.
AF080697 expand/collapse EMBL AC list , AF080695, AF105714, AF080696 Genomic DNA. Translation: AAC95303.1. Sequence problems.
AL031282 Genomic DNA. Translation: CAI20032.1.
AL031282 Genomic DNA. Translation: CAI20033.1.
AL031282 Genomic DNA. Translation: CAI20034.1.
BC110905 mRNA. Translation: AAI10906.1.
CCDSCCDS44042.1. [Q9UQ88-2]
CCDS44043.1. [Q9UQ88-4]
PIRB54024.
E54024.
F54024.
H54024.
RefSeqNP_076916.2. NM_024011.2. [Q9UQ88-2]
NP_277071.2. NM_033529.2. [Q9UQ88-4]
UniGeneHs.651228.
Hs.709182.

3D structure databases

ProteinModelPortalQ9UQ88.
SMRQ9UQ88. Positions 362-753.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid609064. 34 interactions.
IntActQ9UQ88. 25 interactions.

Chemistry

BindingDBQ9UQ88.
ChEMBLCHEMBL5416.
GuidetoPHARMACOLOGY1963.

PTM databases

PhosphoSiteQ9UQ88.

Polymorphism databases

DMDM317373559.

Proteomic databases

MaxQBQ9UQ88.
PaxDbQ9UQ88.
PRIDEQ9UQ88.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000358779; ENSP00000351629; ENSG00000008128. [Q9UQ88-4]
ENST00000378633; ENSP00000367900; ENSG00000008128. [Q9UQ88-1]
ENST00000404249; ENSP00000384442; ENSG00000008128. [Q9UQ88-2]
GeneID728642.
KEGGhsa:728642.
UCSCuc001ahj.4. human. [Q9UQ88-5]
uc009vkr.3. human. [Q9UQ88-4]
uc009vks.3. human. [Q9UQ88-2]

Organism-specific databases

CTD728642.
GeneCardsGC01M001634.
HGNCHGNC:1730. CDK11A.
HPACAB010467.
HPA025061.
MIM116951. gene.
neXtProtNX_Q9UQ88.
PharmGKBPA26263.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOVERGENHBG014652.
InParanoidQ9UQ88.
KOK08818.
OMAWKHARVK.
OrthoDBEOG74BJS4.
TreeFamTF101035.

Enzyme and pathway databases

ReactomeREACT_115566. Cell Cycle.
SignaLinkQ9UQ88.

Gene expression databases

BgeeQ9UQ88.
GenevestigatorQ9UQ88.

Family and domain databases

InterProIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiCDC2L2.
GenomeRNAi728642.
NextBio127852.
PROQ9UQ88.
SOURCESearch...

Entry information

Entry nameCD11A_HUMAN
AccessionPrimary (citable) accession number: Q9UQ88
Secondary accession number(s): O95227 expand/collapse secondary AC list , O95228, O96012, Q12821, Q12853, Q12854, Q2TAJ0, Q5QPR0, Q5QPR1, Q5QPR2, Q9UBC4, Q9UBI3, Q9UEI1, Q9UEI2, Q9UP53, Q9UP54, Q9UP55, Q9UP56, Q9UQ86, Q9UQ87, Q9UQ89
Entry history
Integrated into UniProtKB/Swiss-Prot: September 19, 2003
Last sequence update: January 11, 2011
Last modified: July 9, 2014
This is version 137 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM