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Protein

SRSF protein kinase 2

Gene

SRPK2

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

Functioni

Serine/arginine-rich protein-specific kinase which specifically phosphorylates its substrates at serine residues located in regions rich in arginine/serine dipeptides, known as RS domains and is involved in the phosphorylation of SR splicing factors and the regulation of splicing. Promotes neuronal apoptosis by up-regulating cyclin-D1 (CCND1) expression. This is done by the phosphorylation of SRSF2, leading to the suppression of p53/TP53 phosphorylation thereby relieving the repressive effect of p53/TP53 on cyclin-D1 (CCND1) expression. Phosphorylates ACIN1, and redistributes it from the nuclear speckles to the nucleoplasm, resulting in cyclin A1 but not cyclin A2 up-regulation. Plays an essential role in spliceosomal B complex formation via the phosphorylation of DDX23/PRP28. Can mediate hepatitis B virus (HBV) core protein phosphorylation. Plays a negative role in the regulation of HBV replication through a mechanism not involving the phosphorylation of the core protein but by reducing the packaging efficiency of the pregenomic RNA (pgRNA) without affecting the formation of the viral core particles.8 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.2 Publications

Cofactori

Mg2+2 Publications

Enzyme regulationi

Activated by phosphorylation on Ser-52 and Ser-588.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei110ATPPROSITE-ProRule annotationBy similarity1
Active sitei214Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi87 – 95ATPPROSITE-ProRule annotationBy similarity9

GO - Molecular functioni

  • 14-3-3 protein binding Source: BHF-UCL
  • ATP binding Source: UniProtKB
  • magnesium ion binding Source: UniProtKB
  • poly(A) RNA binding Source: UniProtKB
  • protein serine/threonine kinase activity Source: UniProtKB

GO - Biological processi

  • angiogenesis Source: BHF-UCL
  • cell differentiation Source: UniProtKB-KW
  • innate immune response Source: BHF-UCL
  • intracellular signal transduction Source: UniProtKB
  • negative regulation of viral genome replication Source: BHF-UCL
  • nuclear speck organization Source: BHF-UCL
  • positive regulation of cell cycle Source: BHF-UCL
  • positive regulation of cell proliferation Source: BHF-UCL
  • positive regulation of gene expression Source: BHF-UCL
  • positive regulation of neuron apoptotic process Source: BHF-UCL
  • positive regulation of viral genome replication Source: BHF-UCL
  • protein phosphorylation Source: UniProtKB
  • regulation of mRNA splicing, via spliceosome Source: UniProtKB
  • RNA splicing Source: UniProtKB
  • spliceosomal complex assembly Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Differentiation, mRNA processing, mRNA splicing

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciZFISH:HS05974-MONOMER.
SignaLinkiP78362.
SIGNORiP78362.

Names & Taxonomyi

Protein namesi
Recommended name:
SRSF protein kinase 2 (EC:2.7.11.1)
Alternative name(s):
SFRS protein kinase 2
Serine/arginine-rich protein-specific kinase 2
Short name:
SR-protein-specific kinase 2
Cleaved into the following 2 chains:
Gene namesi
Name:SRPK2Imported
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 7

Organism-specific databases

HGNCiHGNC:11306. SRPK2.

Subcellular locationi

  • Cytoplasm
  • Nucleus

  • Note: Shuttles between the nucleus and the cytoplasm. KAT5/TIP60 inhibits its nuclear translocation. Phosphorylation at Thr-492 by PKB/AKT1 promotes nuclear translocation.

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • nucleolus Source: HPA
  • nucleoplasm Source: HPA
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

DisGeNETi6733.
OpenTargetsiENSG00000135250.
PharmGKBiPA36130.

Chemistry databases

ChEMBLiCHEMBL5668.
DrugBankiDB00173. Adenine.
GuidetoPHARMACOLOGYi2209.

Polymorphism and mutation databases

DMDMi300669676.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000866771 – 688SRSF protein kinase 2Add BLAST688
ChainiPRO_00004147511 – 139SRSF protein kinase 2 N-terminalAdd BLAST139
ChainiPRO_0000414752140 – 688SRSF protein kinase 2 C-terminalAdd BLAST549

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei52PhosphoserineCombined sources1
Modified residuei380PhosphoserineCombined sources1
Modified residuei475PhosphoserineBy similarity1
Modified residuei478PhosphothreonineBy similarity1
Modified residuei484PhosphoserineBy similarity1
Modified residuei486PhosphoserineBy similarity1
Modified residuei490PhosphoserineBy similarity1
Modified residuei492Phosphothreonine; by PKB/AKT11 Publication1
Modified residuei494PhosphoserineCombined sources1
Modified residuei497PhosphoserineCombined sources1
Modified residuei588Phosphoserine; by CK2By similarity1

Post-translational modificationi

Phosphorylation at Thr-492 by PKB/AKT1 enhances its stimulatory activity in triggering cyclin-D1 (CCND1) expression and promoting apoptosis in neurons, which can be blocked by YWHAB. It also enhances its protein kinase activity toward ACIN1 and SRSF2, promotes its nuclear translocation and prevents its proteolytic cleavage.1 Publication
Proteolytically cleaved at Asp-139 and Asp-403 by caspase-3 during apoptotic cell death. Cleavage at Asp-139 which is the major site of cleavage, produces a small N-terminal fragment that translocates into nucleus and promotes VP16-induced apoptosis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei139 – 140Cleavage; by caspase-32
Sitei403 – 404Cleavage; by caspase-32

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiP78362.
MaxQBiP78362.
PaxDbiP78362.
PeptideAtlasiP78362.
PRIDEiP78362.

PTM databases

iPTMnetiP78362.
PhosphoSitePlusiP78362.

Expressioni

Tissue specificityi

Highly expressed in brain, moderately expressed in heart and skeletal muscle and at low levels in lung, liver, and kidney.1 Publication

Gene expression databases

BgeeiENSG00000135250.
CleanExiHS_SRPK2.
ExpressionAtlasiP78362. baseline and differential.
GenevisibleiP78362. HS.

Organism-specific databases

HPAiHPA015522.
HPA020876.

Interactioni

Subunit structurei

Interacts with PKB/AKT1 in a phosphorylation-dependent manner. The phosphorylated form (by PKB/AKT1) interacts with YWHAB and YWHAE. Interaction with YWHAB suppresses its cleavage by caspases and inhibits the release of its N-terminal pro-apoptotic fragment. Interacts with SFN. Associates with U4/U6-U5 tri-small nuclear ribonucleoproteins (U4/U6-U5 tri-snRNPs).2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
AESQ081173EBI-593303,EBI-717810
ARGLU1Q9NWB62EBI-593303,EBI-2808785
CLK2P497603EBI-593303,EBI-750020
CLK3P497614EBI-593303,EBI-745579
FXR2P511163EBI-593303,EBI-740459
HNRNPCP079102EBI-593303,EBI-357966
LUC7LQ9NQ292EBI-593303,EBI-473747
LUC7L2Q9Y3832EBI-593303,EBI-352851
LUZP4Q9P1273EBI-593303,EBI-10198848
MMTAG2Q9BU762EBI-593303,EBI-742459
PRPF38AQ8NAV15EBI-593303,EBI-715374
RBM23Q86U062EBI-593303,EBI-780319
RBM39Q144989EBI-593303,EBI-395290
RBM8AQ9Y5S92EBI-593303,EBI-447231
RNPS1D3DU923EBI-593303,EBI-10176640
RNPS1Q152873EBI-593303,EBI-395959
SNRNP27Q8WVK25EBI-593303,EBI-2512550
SNRNP70P086213EBI-593303,EBI-1049228
SRSF7Q166292EBI-593303,EBI-398885
SRSF8Q9BRL62EBI-593303,EBI-6380719
TRA2BP629953EBI-593303,EBI-725485
U2AF1Q010817EBI-593303,EBI-632461
U2AF1Q01081-23EBI-593303,EBI-10176676
U2AF2P263684EBI-593303,EBI-742339
YTHDC1Q96MU73EBI-593303,EBI-2849854
YWHABP319462EBI-593303,EBI-359815
ZRSR2Q156966EBI-593303,EBI-6657923
ZSCAN9O155355EBI-593303,EBI-751531

GO - Molecular functioni

Protein-protein interaction databases

BioGridi112611. 449 interactors.
IntActiP78362. 240 interactors.
MINTiMINT-1468300.
STRINGi9606.ENSP00000377262.

Chemistry databases

BindingDBiP78362.

Structurei

Secondary structure

1688
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni78 – 80Combined sources3
Beta strandi81 – 89Combined sources9
Beta strandi91 – 100Combined sources10
Turni101 – 104Combined sources4
Beta strandi105 – 112Combined sources8
Helixi116 – 134Combined sources19
Helixi140 – 144Combined sources5
Beta strandi150 – 156Combined sources7
Beta strandi159 – 166Combined sources8
Helixi173 – 179Combined sources7
Turni180 – 182Combined sources3
Helixi187 – 206Combined sources20
Helixi217 – 219Combined sources3
Beta strandi220 – 222Combined sources3
Helixi226 – 233Combined sources8
Helixi518 – 520Combined sources3
Turni521 – 523Combined sources3
Beta strandi526 – 528Combined sources3
Helixi531 – 533Combined sources3
Helixi548 – 550Combined sources3
Helixi553 – 557Combined sources5
Helixi564 – 579Combined sources16
Helixi594 – 606Combined sources13
Helixi611 – 614Combined sources4
Helixi620 – 623Combined sources4
Beta strandi630 – 632Combined sources3
Helixi641 – 649Combined sources9
Helixi653 – 666Combined sources14
Helixi671 – 673Combined sources3
Helixi677 – 681Combined sources5
Helixi684 – 686Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2X7GX-ray2.50A51-688[»]
ProteinModelPortaliP78362.
SMRiP78362.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP78362.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini81 – 684Protein kinasePROSITE-ProRule annotationAdd BLAST604

Sequence similaritiesi

Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG1290. Eukaryota.
ENOG410XRBH. LUCA.
GeneTreeiENSGT00530000063566.
HOVERGENiHBG108512.
InParanoidiP78362.
KOiK08831.
OMAiNDQDGEY.
OrthoDBiEOG091G05H9.
PhylomeDBiP78362.
TreeFamiTF105334.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 2 hits.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 2 hits.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P78362-1) [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
MSVNSEKSSS SERPEPQQKA PLVPPPPPPP PPPPPPLPDP TPPEPEEEIL
60 70 80 90 100
GSDDEEQEDP ADYCKGGYHP VKIGDLFNGR YHVIRKLGWG HFSTVWLCWD
110 120 130 140 150
MQGKRFVAMK VVKSAQHYTE TALDEIKLLK CVRESDPSDP NKDMVVQLID
160 170 180 190 200
DFKISGMNGI HVCMVFEVLG HHLLKWIIKS NYQGLPVRCV KSIIRQVLQG
210 220 230 240 250
LDYLHSKCKI IHTDIKPENI LMCVDDAYVR RMAAEATEWQ KAGAPPPSGS
260 270 280 290 300
AVSTAPQQKP IGKISKNKKK KLKKKQKRQA ELLEKRLQEI EELEREAERK
310 320 330 340 350
IIEENITSAA PSNDQDGEYC PEVKLKTTGL EEAAEAETAK DNGEAEDQEE
360 370 380 390 400
KEDAEKENIE KDEDDVDQEL ANIDPTWIES PKTNGHIENG PFSLEQQLDD
410 420 430 440 450
EDDDEEDCPN PEEYNLDEPN AESDYTYSSS YEQFNGELPN GRHKIPESQF
460 470 480 490 500
PEFSTSLFSG SLEPVACGSV LSEGSPLTEQ EESSPSHDRS RTVSASSTGD
510 520 530 540 550
LPKAKTRAAD LLVNPLDPRN ADKIRVKIAD LGNACWVHKH FTEDIQTRQY
560 570 580 590 600
RSIEVLIGAG YSTPADIWST ACMAFELATG DYLFEPHSGE DYSRDEDHIA
610 620 630 640 650
HIIELLGSIP RHFALSGKYS REFFNRRGEL RHITKLKPWS LFDVLVEKYG
660 670 680
WPHEDAAQFT DFLIPMLEMV PEKRASAGEC LRHPWLNS
Length:688
Mass (Da):77,527
Last modified:July 13, 2010 - v3
Checksum:iACCAF2A887444EC2
GO
Isoform 2 (identifier: P78362-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-13: MSVNSEKSSSSER → MSSRKVLAIQARKRRPKREKHPKK

Show »
Length:699
Mass (Da):79,029
Checksum:i70B084ABA32CC3DB
GO

Sequence cautioni

The sequence AAQ63886 differs from that shown. The cDNA appears to contain a duplicated region.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti137P → R in AAH68547 (PubMed:15489334).Curated1
Sequence conflicti236 – 237AT → P in AAC05299 (PubMed:9472028).Curated2
Sequence conflicti521A → R in AAC05299 (PubMed:9472028).Curated1
Sequence conflicti601H → L in AAC29141 (PubMed:12853948).Curated1
Sequence conflicti608 – 609SI → KV in AAC29141 (PubMed:12853948).Curated2
Sequence conflicti612 – 616HFALS → KYAML in AAC29141 (PubMed:12853948).Curated5
Sequence conflicti621R → K in AAC29141 (PubMed:12853948).Curated1
Sequence conflicti625 – 627NRR → TRK in AAC29141 (PubMed:12853948).Curated3
Sequence conflicti640S → G in AAH68547 (PubMed:15489334).Curated1
Sequence conflicti681Missing in AAC05299 (PubMed:9472028).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_04111443P → L.1 PublicationCorresponds to variant rs34699980dbSNPEnsembl.1
Natural variantiVAR_041115243G → D in a glioblastoma multiforme sample; somatic mutation. 1 Publication1
Natural variantiVAR_041116426T → P.1 PublicationCorresponds to variant rs55743527dbSNPEnsembl.1
Natural variantiVAR_041117486S → F.1 PublicationCorresponds to variant rs56112661dbSNPEnsembl.1
Natural variantiVAR_041118515P → T.1 PublicationCorresponds to variant rs56017595dbSNPEnsembl.1
Natural variantiVAR_060390608S → N.Corresponds to variant rs1050413dbSNPEnsembl.1
Natural variantiVAR_057111615L → I.Corresponds to variant rs1050418dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0393861 – 13MSVNS…SSSER → MSSRKVLAIQARKRRPKREK HPKK in isoform 2. 1 PublicationAdd BLAST13

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U88666 mRNA. Translation: AAC05299.1.
AC005070 Genomic DNA. Translation: AAC29140.1.
AC005070 Genomic DNA. Translation: AAC29141.1.
AC004884 Genomic DNA. No translation available.
AC073138 Genomic DNA. No translation available.
CH471070 Genomic DNA. Translation: EAW83359.1.
BC035214 mRNA. Translation: AAH35214.1.
BC068547 mRNA. Translation: AAH68547.1.
BE781215 mRNA. No translation available.
AY354201 mRNA. Translation: AAQ63886.1. Sequence problems.
CCDSiCCDS34724.1. [P78362-2]
CCDS5735.1. [P78362-1]
RefSeqiNP_001265202.1. NM_001278273.1. [P78362-1]
NP_872633.1. NM_182691.2. [P78362-1]
NP_872634.1. NM_182692.2. [P78362-2]
XP_016868055.1. XM_017012566.1. [P78362-1]
UniGeneiHs.285197.

Genome annotation databases

EnsembliENST00000357311; ENSP00000349863; ENSG00000135250. [P78362-1]
ENST00000393651; ENSP00000377262; ENSG00000135250. [P78362-2]
ENST00000489828; ENSP00000419791; ENSG00000135250. [P78362-1]
GeneIDi6733.
KEGGihsa:6733.
UCSCiuc003vct.5. human. [P78362-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U88666 mRNA. Translation: AAC05299.1.
AC005070 Genomic DNA. Translation: AAC29140.1.
AC005070 Genomic DNA. Translation: AAC29141.1.
AC004884 Genomic DNA. No translation available.
AC073138 Genomic DNA. No translation available.
CH471070 Genomic DNA. Translation: EAW83359.1.
BC035214 mRNA. Translation: AAH35214.1.
BC068547 mRNA. Translation: AAH68547.1.
BE781215 mRNA. No translation available.
AY354201 mRNA. Translation: AAQ63886.1. Sequence problems.
CCDSiCCDS34724.1. [P78362-2]
CCDS5735.1. [P78362-1]
RefSeqiNP_001265202.1. NM_001278273.1. [P78362-1]
NP_872633.1. NM_182691.2. [P78362-1]
NP_872634.1. NM_182692.2. [P78362-2]
XP_016868055.1. XM_017012566.1. [P78362-1]
UniGeneiHs.285197.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2X7GX-ray2.50A51-688[»]
ProteinModelPortaliP78362.
SMRiP78362.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112611. 449 interactors.
IntActiP78362. 240 interactors.
MINTiMINT-1468300.
STRINGi9606.ENSP00000377262.

Chemistry databases

BindingDBiP78362.
ChEMBLiCHEMBL5668.
DrugBankiDB00173. Adenine.
GuidetoPHARMACOLOGYi2209.

PTM databases

iPTMnetiP78362.
PhosphoSitePlusiP78362.

Polymorphism and mutation databases

DMDMi300669676.

Proteomic databases

EPDiP78362.
MaxQBiP78362.
PaxDbiP78362.
PeptideAtlasiP78362.
PRIDEiP78362.

Protocols and materials databases

DNASUi6733.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000357311; ENSP00000349863; ENSG00000135250. [P78362-1]
ENST00000393651; ENSP00000377262; ENSG00000135250. [P78362-2]
ENST00000489828; ENSP00000419791; ENSG00000135250. [P78362-1]
GeneIDi6733.
KEGGihsa:6733.
UCSCiuc003vct.5. human. [P78362-1]

Organism-specific databases

CTDi6733.
DisGeNETi6733.
GeneCardsiSRPK2.
H-InvDBHIX0006976.
HGNCiHGNC:11306. SRPK2.
HPAiHPA015522.
HPA020876.
MIMi602980. gene.
neXtProtiNX_P78362.
OpenTargetsiENSG00000135250.
PharmGKBiPA36130.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1290. Eukaryota.
ENOG410XRBH. LUCA.
GeneTreeiENSGT00530000063566.
HOVERGENiHBG108512.
InParanoidiP78362.
KOiK08831.
OMAiNDQDGEY.
OrthoDBiEOG091G05H9.
PhylomeDBiP78362.
TreeFamiTF105334.

Enzyme and pathway databases

BioCyciZFISH:HS05974-MONOMER.
SignaLinkiP78362.
SIGNORiP78362.

Miscellaneous databases

ChiTaRSiSRPK2. human.
EvolutionaryTraceiP78362.
GeneWikiiSRPK2.
GenomeRNAii6733.
PROiP78362.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000135250.
CleanExiHS_SRPK2.
ExpressionAtlasiP78362. baseline and differential.
GenevisibleiP78362. HS.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 2 hits.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 2 hits.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiSRPK2_HUMAN
AccessioniPrimary (citable) accession number: P78362
Secondary accession number(s): A8MVX2
, O75220, O75221, Q6NUL0, Q6V1X2, Q8IYQ3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 5, 2005
Last sequence update: July 13, 2010
Last modified: November 30, 2016
This is version 161 of the entry and version 3 of the sequence. [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 7
    Human chromosome 7: 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.