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Q8TAS1 (UHMK1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 129. 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:
Serine/threonine-protein kinase Kist

EC=2.7.11.1
Alternative name(s):
Kinase interacting with stathmin
PAM COOH-terminal interactor protein 2
Short name=P-CIP2
U2AF homology motif kinase 1
Gene names
Name:UHMK1
Synonyms:KIS, KIST
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length419 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Upon serum stimulation, phosphorylates CDKN1B/p27Kip1, thus controlling CDKN1B subcellular location and cell cycle progression in G1 phase. May be involved in trafficking and/or processing of RNA By similarity.

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Subunit structure

Interacts with stathmin and CDKN1B/p27Kip1 By similarity. Interacts with PAM. Ref.6 Ref.7

Subcellular location

Nucleus Ref.8.

Tissue specificity

Widely expressed, with highest levels in skeletal muscle, kidney, placenta and peripheral blood leukocytes. Ref.7

Developmental stage

Regulated in a cell-cycle dependent manner, with lowest levels during S phase and highest at G1 phase (at protein level). Ref.8

Sequence similarities

Belongs to the protein kinase superfamily. Ser/Thr protein kinase family.

Contains 1 protein kinase domain.

Contains 1 RRM (RNA recognition motif) domain.

Ontologies

Keywords
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   LigandATP-binding
Nucleotide-binding
RNA-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcell cycle arrest

Inferred from mutant phenotype Ref.7. Source: HGNC

neuron projection development

Inferred from sequence or structural similarity. Source: BHF-UCL

peptidyl-serine phosphorylation

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of translational initiation

Inferred from sequence or structural similarity. Source: BHF-UCL

protein autophosphorylation

Inferred from direct assay Ref.7. Source: HGNC

regulation of protein export from nucleus

Inferred from direct assay Ref.7. Source: HGNC

   Cellular_componentaxon

Inferred from sequence or structural similarity. Source: BHF-UCL

dendrite cytoplasm

Inferred from sequence or structural similarity. Source: BHF-UCL

neuronal ribonucleoprotein granule

Inferred from sequence or structural similarity. Source: BHF-UCL

nucleus

Inferred from direct assay Ref.7. Source: HGNC

   Molecular_functionATP binding

Inferred by curator Ref.7. Source: HGNC

RNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction Ref.7. Source: HGNC

protein serine/threonine kinase activity

Inferred from direct assay Ref.7. Source: HGNC

ribonucleoprotein complex binding

Inferred from sequence or structural similarity. Source: BHF-UCL

transferase activity

Inferred by curator Ref.7. Source: HGNC

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8TAS1-1)

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: Q8TAS1-2)

The sequence of this isoform differs from the canonical sequence as follows:
     342-344: DVV → GLC
     345-419: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: Q8TAS1-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-89: MAGSGCAWGA...LEQLQGHRNI → MFLTRPKVCVDLNRR
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 419419Serine/threonine-protein kinase Kist
PRO_0000086777

Regions

Domain23 – 304282Protein kinase
Domain324 – 40683RRM
Nucleotide binding29 – 379ATP By similarity

Sites

Active site1581Proton acceptor By similarity
Binding site541ATP By similarity

Natural variations

Alternative sequence1 – 8989MAGSG…GHRNI → MFLTRPKVCVDLNRR in isoform 3.
VSP_046145
Alternative sequence342 – 3443DVV → GLC in isoform 2.
VSP_004908
Alternative sequence345 – 41975Missing in isoform 2.
VSP_004909
Natural variant1591L → V. Ref.9
Corresponds to variant rs34466082 [ dbSNP | Ensembl ].
VAR_041272
Natural variant1971Y → D. Ref.9
Corresponds to variant rs56201055 [ dbSNP | Ensembl ].
VAR_041273

Experimental info

Mutagenesis541K → A: Loss of kinase activity. Ref.7

Sequences

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

Last modified October 19, 2002. Version 2.
Checksum: 903E982EE12A8CF8

FASTA41946,546
        10         20         30         40         50         60 
MAGSGCAWGA EPPRFLEAFG RLWQVQSRLG SGSSASVYRV RCCGNPGSPP GALKQFLPPG 

        70         80         90        100        110        120 
TTGAAASAAE YGFRKERAAL EQLQGHRNIV TLYGVFTIHF SPNVPSRCLL LELLDVSVSE 

       130        140        150        160        170        180 
LLLYSSHQGC SMWMIQHCAR DVLEALAFLH HEGYVHADLK PRNILWSAEN ECFKLIDFGL 

       190        200        210        220        230        240 
SFKEGNQDVK YIQTDGYRAP EAELQNCLAQ AGLQSDTECT SAVDLWSLGI ILLEMFSGMK 

       250        260        270        280        290        300 
LKHTVRSQEW KANSSAIIDH IFASKAVVNA AIPAYHLRDL IKSMLHDDPS RRIPAEMALC 

       310        320        330        340        350        360 
SPFFSIPFAP HIEDLVMLPT PVLRLLNVLD DDYLENEEEY EDVVEDVKEE CQKYGPVVSL 

       370        380        390        400        410 
LVPKENPGRG QVFVEYANAG DSKAAQKLLT GRMFDGKFVV ATFYPLSAYK RGYLYQTLL 

« Hide

Isoform 2 [UniParc].

Checksum: F17050CA387CCA9B
Show »

FASTA34438,130
Isoform 3 [UniParc].

Checksum: 2D542DC30505CF01
Show »

FASTA34539,044

References

« Hide 'large scale' references
[1]"Quantitative RT-PCR reveals a ubiquitous but preferentially neural expression of the KIS gene in rat and human."
Bieche I., Manceau V., Curmi P.A., Laurendeau I., Lachkar S., Leroy K., Vidaud D., Sobel A., Maucuer A.
Brain Res. Mol. Brain Res. 114:55-64(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE (ISOFORM 1).
[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. 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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
Tissue: Testis.
[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].
[4]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].
[5]"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] (ISOFORMS 1 AND 2).
Tissue: Eye and Skin.
[6]"The novel kinase peptidylglycine alpha-amidating monooxygenase cytosolic interactor protein 2 interacts with the cytosolic routing determinants of the peptide processing enzyme peptidylglycine alpha-amidating monooxygenase."
Caldwell B.D., Darlington D.N., Penzes P., Johnson R.C., Eipper B.A., Mains R.E.
J. Biol. Chem. 274:34646-34656(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PAM.
[7]"A growth factor-dependent nuclear kinase phosphorylates p27(Kip1) and regulates cell cycle progression."
Boehm M., Yoshimoto T., Crook M.F., Nallamshetty S., True A., Nabel G.J., Nabel E.G.
EMBO J. 21:3390-3401(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CDKN1B, TISSUE SPECIFICITY, MUTAGENESIS OF LYS-54.
[8]"The CATS (FAM64A) protein is a substrate of the kinase interacting stathmin (KIS)."
Archangelo L.F., Greif P.A., Maucuer A., Manceau V., Koneru N., Bigarella C.L., Niemann F., Dos Santos M.T., Kobarg J., Bohlander S.K., Saad S.T.
Biochim. Biophys. Acta 1833:1269-1279(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE.
[9]"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] [Europe PMC] [Abstract]
Cited for: VARIANTS [LARGE SCALE ANALYSIS] VAL-159 AND ASP-197.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ536197 mRNA. Translation: CAD60192.1.
AK058195 mRNA. No translation available.
AK292369 mRNA. Translation: BAF85058.1.
AL359699 Genomic DNA. Translation: CAH70392.1.
CH471067 Genomic DNA. Translation: EAW90706.1.
CH471067 Genomic DNA. Translation: EAW90707.1.
BC014917 mRNA. Translation: AAH14917.1.
BC026046 mRNA. Translation: AAH26046.1.
CCDSCCDS1239.1. [Q8TAS1-1]
CCDS53423.1. [Q8TAS1-3]
CCDS53424.1. [Q8TAS1-2]
RefSeqNP_001171692.1. NM_001184763.1. [Q8TAS1-3]
NP_653225.2. NM_144624.2. [Q8TAS1-2]
NP_787062.1. NM_175866.4. [Q8TAS1-1]
UniGeneHs.127310.

3D structure databases

ProteinModelPortalQ8TAS1.
SMRQ8TAS1. Positions 23-411.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid126088. 2 interactions.
IntActQ8TAS1. 1 interaction.
MINTMINT-7241640.
STRING9606.ENSP00000420270.

PTM databases

PhosphoSiteQ8TAS1.

Polymorphism databases

DMDM24211880.

Proteomic databases

PaxDbQ8TAS1.
PRIDEQ8TAS1.

Protocols and materials databases

DNASU127933.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000489294; ENSP00000420270; ENSG00000152332. [Q8TAS1-1]
ENST00000538489; ENSP00000446416; ENSG00000152332. [Q8TAS1-2]
ENST00000545294; ENSP00000441226; ENSG00000152332. [Q8TAS1-3]
GeneID127933.
KEGGhsa:127933.
UCSCuc001gcc.2. human. [Q8TAS1-1]
uc001gcd.3. human.
uc009wuu.2. human. [Q8TAS1-2]

Organism-specific databases

CTD127933.
GeneCardsGC01P162467.
HGNCHGNC:19683. UHMK1.
MIM608849. gene.
neXtProtNX_Q8TAS1.
PharmGKBPA134974001.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000013166.
HOVERGENHBG056149.
InParanoidQ8TAS1.
KOK08877.
OMAYGVFTNH.
OrthoDBEOG7S4X5Z.
PhylomeDBQ8TAS1.
TreeFamTF331856.

Enzyme and pathway databases

SignaLinkQ8TAS1.

Gene expression databases

BgeeQ8TAS1.
CleanExHS_UHMK1.
GenevestigatorQ8TAS1.

Family and domain databases

Gene3D3.30.70.330. 1 hit.
InterProIPR011009. Kinase-like_dom.
IPR012677. Nucleotide-bd_a/b_plait.
IPR000719. Prot_kinase_dom.
IPR000504. RRM_dom.
[Graphical view]
PfamPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTSM00360. RRM. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS50011. PROTEIN_KINASE_DOM. 1 hit.
PS50102. RRM. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSUHMK1. human.
GeneWikiUHMK1.
GenomeRNAi127933.
NextBio82204.
PROQ8TAS1.
SOURCESearch...

Entry information

Entry nameUHMK1_HUMAN
AccessionPrimary (citable) accession number: Q8TAS1
Secondary accession number(s): A8K8K4, G3V1M1, Q96C22
Entry history
Integrated into UniProtKB/Swiss-Prot: October 19, 2002
Last sequence update: October 19, 2002
Last modified: July 9, 2014
This is version 129 of the entry and version 2 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