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UniProtKB - Q15058 (KIF14_HUMAN)

Protein

Kinesin-like protein KIF14

Gene

KIF14

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

Functioni

Microtubule motor protein that binds to microtubules with high affinity through each tubulin heterodimer and has an ATPase activity (By similarity). Plays a role in many processes like cell division, cytokinesis and also in cell proliferation and apoptosis (PubMed:24784001, PubMed:16648480). During cytokinesis, targets to central spindle and midbody through its interaction with PRC1 and CIT respectively (PubMed:16431929). Regulates cell growth through regulation of cell cycle progression and cytokinesis (PubMed:24854087). During cell cycle progression acts through SCF-dependent proteasomal ubiquitin-dependent protein catabolic process which controls CDKN1B degradation, resulting in positive regulation of cyclins, including CCNE1, CCND1 and CCNB1 (PubMed:24854087). During late neurogenesis, regulates the cerebellar, cerebral cortex and olfactory bulb development through regulation of apoptosis, cell proliferation and cell division (By similarity). Also is required for chromosome congression and alignment during mitotic cell cycle process (PubMed:15843429). Regulates cell spreading, focal adhesion dynamics, and cell migration through its interaction with RADIL resulting in regulation of RAP1A-mediated inside-out integrin activation by tethering RADIL on microtubules (PubMed:23209302).By similarity6 Publications

Miscellaneous

It is resistant to docetaxel anhydrous.1 Publication

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi447 – 454ATPPROSITE-ProRule annotation8

GO - Molecular functioni

  • ATPase activity Source: UniProtKB
  • ATP binding Source: UniProtKB
  • ATP-dependent microtubule motor activity, plus-end-directed Source: UniProtKB
  • microtubule binding Source: UniProtKB
  • microtubule motor activity Source: GO_Central
  • PDZ domain binding Source: MGI
  • protein kinase binding Source: UniProtKB
  • tubulin binding Source: UniProtKB
View the complete GO annotation on QuickGO ...

GO - Biological processi

View the complete GO annotation on QuickGO ...

Keywordsi

Molecular functionMotor protein
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-HSA-5625900 RHO GTPases activate CIT

Names & Taxonomyi

Protein namesi
Recommended name:
Kinesin-like protein KIF14Curated
Gene namesi
Name:KIF14Imported
Synonyms:KIAA0042Imported
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

EuPathDBiHostDB:ENSG00000118193.11
HGNCiHGNC:19181 KIF14
MIMi611279 gene
neXtProtiNX_Q15058

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

Cytoplasm, Cytoskeleton, Microtubule, Nucleus

Pathology & Biotechi

Involvement in diseasei

Meckel syndrome 12 (MKS12)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA form of Meckel syndrome, a disorder characterized by a combination of renal cysts and variably associated features including developmental anomalies of the central nervous system (typically encephalocele), hepatic ductal dysplasia and cysts, and polydactyly.
See also OMIM:616258
Microcephaly 20, primary, autosomal recessive (MCPH20)2 Publications
The disease is caused by mutations affecting the gene represented in this entry. The disease-causing variant NM_014875.2:c.263T>A, which produces a premature truncation of the protein at Leu-88 (p.Leu88Ter), may also partly result in the deletion of 372 bp of exon 2 of KIF14 by activation of a cryptic splice site. This in-frame deletion predicts a protein that lacks 124 aa (p.Gly58-Leu181del). The disease-causing mutation NM_014875.2:c.3662G>T, resulting in the missence variant p.Gly1221Val, may also induce the skipping of exon 24, resulting in a protein that misses 76 aa (p.Gly1221_ Lys1296delinsVal).1 Publication
Disease descriptionA form of microcephaly, a disease defined as a head circumference more than 3 standard deviations below the age, sex and ethnically matched mean. Brain weight is markedly reduced and the cerebral cortex is disproportionately small. MCPH20 features include mild to moderate intellectual disability, autistic features, poor speech. Disease severity is highly variable.
See also OMIM:617914
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_08062388 – 1648Missing in MCPH20; drastically decreased expression at the mRNA level; loss of localization at the midbody during cytokinesis and consequently loss of CIT/CRIK recruitment to the midbody. 1 PublicationAdd BLAST1561
Natural variantiVAR_080624459G → R in MCPH20; unknown pathological significance. 1 Publication1
Natural variantiVAR_080625827Missing in MCPH20; unknown pathological significance. 1 Publication1
Natural variantiVAR_080626841S → F in MCPH20; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs139385693Ensembl.1
Natural variantiVAR_080627849H → D in MCPH20; Decreased expression at the mRNA level and loss of localization at the midbody during cytokinesis and consequently loss of CIT/CRIK recruitment to the midbody, when analyzed in primary fibroblasts from a patient who is a compound heterozygous with variant V-1221. 1 Publication1
Natural variantiVAR_0806281221G → V in MCPH20; Decreased expression at the mRNA level and loss of localization at the midbody during cytokinesis and consequently loss of CIT/CRIK recruitment to the midbody, when analyzed in primary fibroblasts from a patient who is a compound heterozygous with variant D-849. 1 Publication1

Keywords - Diseasei

Ciliopathy, Disease mutation, Meckel syndrome, Primary microcephaly

Organism-specific databases

DisGeNETi9928
MalaCardsiKIF14
MIMi616258 phenotype
617914 phenotype
OpenTargetsiENSG00000118193
Orphaneti2512 Autosomal recessive primary microcephaly
439897 Lethal fetal cerebrorenogenitourinary agenesis/hypoplasia syndrome
PharmGKBiPA38820

Chemistry databases

ChEMBLiCHEMBL5576

Polymorphism and mutation databases

BioMutaiKIF14
DMDMi23396633

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001254491 – 1648Kinesin-like protein KIF14Add BLAST1648

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei12PhosphoserineCombined sources1
Modified residuei272PhosphoserineCombined sources1
Modified residuei277PhosphothreonineCombined sources1
Modified residuei346PhosphoserineCombined sources1
Modified residuei915PhosphothreonineCombined sources1
Modified residuei937PhosphoserineCombined sources1
Modified residuei1292PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ15058
MaxQBiQ15058
PaxDbiQ15058
PeptideAtlasiQ15058
PRIDEiQ15058
ProteomicsDBi60413

PTM databases

iPTMnetiQ15058
PhosphoSitePlusiQ15058

Expressioni

Inductioni

Up-regulated in cells progressing through G2/M phase.1 Publication

Gene expression databases

BgeeiENSG00000118193 Expressed in 107 organ(s), highest expression level in bone marrow
CleanExiHS_KIF14
GenevisibleiQ15058 HS

Organism-specific databases

HPAiHPA038061
HPA058220

Interactioni

Subunit structurei

Directly interacts with PRC1 within a complex also containing KIF4A, KIF20A and KIF23; targets to the central spindle. Directly interacts with CIT depending on the activation state of the kinase (stronger interaction with the kinase-dead form); targets to the midbody. Interacts with ARRB2; the interaction is detected in the nucleus upon OR1D2 stimulation. Interacts with AKT1; the interaction is detected in the plasma membrane upon INS stimulation and promotes AKT1 phosphorylation. Interacts with SVIL; at midbody during cytokinesis. Interacts with RADIL (via PDZ domain); recruits RADIL to the microtubule network restricting RADIL from interaction with activated RAP1A (PubMed:23209302).5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
SVILO463853EBI-1045252,EBI-6995105From Bos taurus.

GO - Molecular functioni

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridi115256, 92 interactors
IntActiQ15058, 40 interactors
MINTiQ15058
STRINGi9606.ENSP00000356319

Chemistry databases

BindingDBiQ15058

Structurei

3D structure databases

ProteinModelPortaliQ15058
SMRiQ15058
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini358 – 701Kinesin motorPROSITE-ProRule annotationAdd BLAST344
Domaini825 – 891FHAAdd BLAST67

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 356Required for PRC1-bindingAdd BLAST356
Regioni356 – 737Required for microtubule-binding with high affinityBy similarityAdd BLAST382
Regioni901 – 1648Required for CIT-bindingAdd BLAST748

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili705 – 791Sequence analysisAdd BLAST87
Coiled coili922 – 1079Sequence analysisAdd BLAST158
Coiled coili1332 – 1348Sequence analysisAdd BLAST17
Coiled coili1468 – 1500Sequence analysisAdd BLAST33

Domaini

The kinesin motor domain binds to microtubules with high affinity and has a robust ATPase activity but a very slow motility. The kinesin motor domain protects microtubules from cold depolymerization. Binds to each tubulin heterodimer resulting in a microtubule complexes. Binds at the tubulin intradimer interface, at the crest of the protofilament, and orients slightly toward the next protofilament.By similarity

Sequence similaritiesi

Belongs to the TRAFAC class myosin-kinesin ATPase superfamily. Kinesin family.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG0245 Eukaryota
COG5059 LUCA
GeneTreeiENSGT00930000150817
HOGENOMiHOG000113224
HOVERGENiHBG052249
InParanoidiQ15058
KOiK17915
OMAiQEVSYHL
OrthoDBiEOG091G0159
PhylomeDBiQ15058
TreeFamiTF105221

Family and domain databases

CDDicd00060 FHA, 1 hit
Gene3Di3.40.850.10, 1 hit
InterProiView protein in InterPro
IPR000253 FHA_dom
IPR027640 Kinesin-like_fam
IPR032405 Kinesin_assoc
IPR019821 Kinesin_motor_CS
IPR001752 Kinesin_motor_dom
IPR036961 Kinesin_motor_dom_sf
IPR027417 P-loop_NTPase
IPR008984 SMAD_FHA_dom_sf
PANTHERiPTHR24115 PTHR24115, 1 hit
PfamiView protein in Pfam
PF00498 FHA, 1 hit
PF00225 Kinesin, 1 hit
PF16183 Kinesin_assoc, 1 hit
PRINTSiPR00380 KINESINHEAVY
SMARTiView protein in SMART
SM00240 FHA, 1 hit
SM00129 KISc, 1 hit
SUPFAMiSSF49879 SSF49879, 1 hit
SSF52540 SSF52540, 1 hit
PROSITEiView protein in PROSITE
PS00411 KINESIN_MOTOR_1, 1 hit
PS50067 KINESIN_MOTOR_2, 1 hit

Sequencei

Sequence statusi: Complete.

Q15058-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSLHSTHNRN NSGDILDIPS SQNSSSLNAL THSSRLKLHL KSDMSECEND 
        60         70         80         90        100
DPLLRSAGKV RDINRTYVIS ASRKTADMPL TPNPVGRLAL QRRTTRNKES 
       110        120        130        140        150
SLLVSELEDT TEKTAETRLT LQRRAKTDSA EKWKTAEIDS VKMTLNVGGE 
       160        170        180        190        200
TENNGVSKES RTNVRIVNNA KNSFVASSVP LDEDPQVIEM MADKKYKETF 
       210        220        230        240        250
SAPSRANENV ALKYSSNRPP IASLSQTEVV RSGHLTTKPT QSKLDIKVLG 
       260        270        280        290        300
TGNLYHRSIG KEIAKTSNKF GSLEKRTPTK CTTEHKLTTK CSLPQLKSPA 
       310        320        330        340        350
PSILKNRMSN LQVKQRPKSS FLANKQERSA ENTILPEEET VVQNTSAGKD 
       360        370        380        390        400
PLKVENSQVT VAVRVRPFTK REKIEKASQV VFMSGKEITV EHPDTKQVYN 
       410        420        430        440        450
FIYDVSFWSF DECHPHYASQ TTVYEKLAAP LLERAFEGFN TCLFAYGQTG 
       460        470        480        490        500
SGKSYTMMGF SEEPGIIPRF CEDLFSQVAR KQTQEVSYHI EMSFFEVYNE 
       510        520        530        540        550
KIHDLLVCKD ENGQRKQPLR VREHPVYGPY VEALSMNIVS SYADIQSWLE 
       560        570        580        590        600
LGNKQRATAA TGMNDKSSRS HSVFTLVMTQ TKTEFVEGEE HDHRITSRIN 
       610        620        630        640        650
LIDLAGSERC STAHTNGDRL KEGVSINKSL LTLGKVISAL SEQANQRSVF 
       660        670        680        690        700
IPYRESVLTW LLKESLGGNS KTAMIATISP AASNIEETLS TLRYANQARL 
       710        720        730        740        750
IVNIAKVNED MNAKLIRELK AEIAKLKAAQ RNSRNIDPER YRLCRQEITS 
       760        770        780        790        800
LRMKLHQQER DMAEMQRVWK EKFEQAEKRK LQETKELQKA GIMFQMDNHL 
       810        820        830        840        850
PNLVNLNEDP QLSEMLLYMI KEGTTTVGKY KPNSSHDIQL SGVLIADDHC 
       860        870        880        890        900
TIKNFGGTVS IIPVGEAKTY VNGKHILEIT VLRHGDRVIL GGDHYFRFNH 
       910        920        930        940        950
PVEVQKGKRP SGRDTPISEG PKDFEFAKNE LLMAQRSQLE AEIKEAQLKA 
       960        970        980        990       1000
KEEMMQGIQI AKEMAQQELS SQKAAYESKI KALEAELREE SQRKKMQEIN 
      1010       1020       1030       1040       1050
NQKANHKIEE LEKAKQHLEQ EIYVNKKRLE METLATKQAL EDHSIRHARI 
      1060       1070       1080       1090       1100
LEALETEKQK IAKEVQILQQ NRNNRDKTFT VQTTWSSMKL SMMIQEANAI 
      1110       1120       1130       1140       1150
SSKLKTYYVF GRHDISDKSS SDTSIRVRNL KLGISTFWSL EKFESKLAAM 
      1160       1170       1180       1190       1200
KELYESNGSN RGEDAFCDPE DEWEPDITDA PVSSLSRRRS RSLMKNRRIS 
      1210       1220       1230       1240       1250
GCLHDIQVHP IKNLHSSHSS GLMDKSSTIY SNSAESFLPG ICKELIGSSL 
      1260       1270       1280       1290       1300
DFFGQSYDEE RTIADSLINS FLKIYNGLFA ISKAHEEQDE ESQDNLFSSD 
      1310       1320       1330       1340       1350
RAIQSLTIQT ACAFEQLVVL MKHWLSDLLP CTNIARLEDE LRQEVKKLGG 
      1360       1370       1380       1390       1400
YLQLFLQGCC LDISSMIKEA QKNAIQIVQQ AVKYVGQLAV LKGSKLHFLE 
      1410       1420       1430       1440       1450
NGNNKAASVQ EEFMDAVCDG VGLGMKILLD SGLEKAKELQ HELFRQCTKN 
      1460       1470       1480       1490       1500
EVTKEMKTNA MGLIRSLENI FAESKIKSFR RQVQEENFEY QDFKRMVNRA 
      1510       1520       1530       1540       1550
PEFLKLKHCL EKAIEIIISA LKGCHSDINL LQTCVESIRN LASDFYSDFS 
      1560       1570       1580       1590       1600
VPSTSVGSYE SRVTHIVHQE LESLAKSLLF CFESEESPDL LKPWETYNQN 
      1610       1620       1630       1640 
TKEEHQQSKS SGIDGSKNKG VPKRVYELHG SSPAVSSEEC TPSRIQWV
Length:1,648
Mass (Da):186,492
Last modified:November 1, 1996 - v1
Checksum:iFB1423668A7B79D7
GO

Sequence cautioni

The sequence BAA05392 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti660W → C in AAH98582 (PubMed:15489334).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_08062388 – 1648Missing in MCPH20; drastically decreased expression at the mRNA level; loss of localization at the midbody during cytokinesis and consequently loss of CIT/CRIK recruitment to the midbody. 1 PublicationAdd BLAST1561
Natural variantiVAR_080624459G → R in MCPH20; unknown pathological significance. 1 Publication1
Natural variantiVAR_080625827Missing in MCPH20; unknown pathological significance. 1 Publication1
Natural variantiVAR_080626841S → F in MCPH20; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs139385693Ensembl.1
Natural variantiVAR_080627849H → D in MCPH20; Decreased expression at the mRNA level and loss of localization at the midbody during cytokinesis and consequently loss of CIT/CRIK recruitment to the midbody, when analyzed in primary fibroblasts from a patient who is a compound heterozygous with variant V-1221. 1 Publication1
Natural variantiVAR_0806281221G → V in MCPH20; Decreased expression at the mRNA level and loss of localization at the midbody during cytokinesis and consequently loss of CIT/CRIK recruitment to the midbody, when analyzed in primary fibroblasts from a patient who is a compound heterozygous with variant D-849. 1 Publication1
Natural variantiVAR_0377771633P → A1 PublicationCorresponds to variant dbSNP:rs12120084Ensembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D26361 mRNA Translation: BAA05392.2 Different initiation.
AL445483 Genomic DNA No translation available.
CH471067 Genomic DNA Translation: EAW91316.1
BC098582 mRNA Translation: AAH98582.1
BC113742 mRNA Translation: AAI13743.1
CCDSiCCDS30963.1
RefSeqiNP_001292721.1, NM_001305792.1
NP_055690.1, NM_014875.2
XP_011508533.1, XM_011510231.2
XP_011508534.1, XM_011510232.2
XP_016858494.1, XM_017003005.1
UniGeneiHs.3104

Genome annotation databases

EnsembliENST00000367350; ENSP00000356319; ENSG00000118193
ENST00000614960; ENSP00000483069; ENSG00000118193
GeneIDi9928
KEGGihsa:9928
UCSCiuc010ppk.2 human

Keywords - Coding sequence diversityi

Polymorphism

Similar proteinsi

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D26361 mRNA Translation: BAA05392.2 Different initiation.
AL445483 Genomic DNA No translation available.
CH471067 Genomic DNA Translation: EAW91316.1
BC098582 mRNA Translation: AAH98582.1
BC113742 mRNA Translation: AAI13743.1
CCDSiCCDS30963.1
RefSeqiNP_001292721.1, NM_001305792.1
NP_055690.1, NM_014875.2
XP_011508533.1, XM_011510231.2
XP_011508534.1, XM_011510232.2
XP_016858494.1, XM_017003005.1
UniGeneiHs.3104

3D structure databases

ProteinModelPortaliQ15058
SMRiQ15058
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115256, 92 interactors
IntActiQ15058, 40 interactors
MINTiQ15058
STRINGi9606.ENSP00000356319

Chemistry databases

BindingDBiQ15058
ChEMBLiCHEMBL5576

PTM databases

iPTMnetiQ15058
PhosphoSitePlusiQ15058

Polymorphism and mutation databases

BioMutaiKIF14
DMDMi23396633

Proteomic databases

EPDiQ15058
MaxQBiQ15058
PaxDbiQ15058
PeptideAtlasiQ15058
PRIDEiQ15058
ProteomicsDBi60413

Protocols and materials databases

DNASUi9928
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000367350; ENSP00000356319; ENSG00000118193
ENST00000614960; ENSP00000483069; ENSG00000118193
GeneIDi9928
KEGGihsa:9928
UCSCiuc010ppk.2 human

Organism-specific databases

CTDi9928
DisGeNETi9928
EuPathDBiHostDB:ENSG00000118193.11
GeneCardsiKIF14
HGNCiHGNC:19181 KIF14
HPAiHPA038061
HPA058220
MalaCardsiKIF14
MIMi611279 gene
616258 phenotype
617914 phenotype
neXtProtiNX_Q15058
OpenTargetsiENSG00000118193
Orphaneti2512 Autosomal recessive primary microcephaly
439897 Lethal fetal cerebrorenogenitourinary agenesis/hypoplasia syndrome
PharmGKBiPA38820
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0245 Eukaryota
COG5059 LUCA
GeneTreeiENSGT00930000150817
HOGENOMiHOG000113224
HOVERGENiHBG052249
InParanoidiQ15058
KOiK17915
OMAiQEVSYHL
OrthoDBiEOG091G0159
PhylomeDBiQ15058
TreeFamiTF105221

Enzyme and pathway databases

ReactomeiR-HSA-5625900 RHO GTPases activate CIT

Miscellaneous databases

ChiTaRSiKIF14 human
GeneWikiiKIF14
GenomeRNAii9928
PROiPR:Q15058
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000118193 Expressed in 107 organ(s), highest expression level in bone marrow
CleanExiHS_KIF14
GenevisibleiQ15058 HS

Family and domain databases

CDDicd00060 FHA, 1 hit
Gene3Di3.40.850.10, 1 hit
InterProiView protein in InterPro
IPR000253 FHA_dom
IPR027640 Kinesin-like_fam
IPR032405 Kinesin_assoc
IPR019821 Kinesin_motor_CS
IPR001752 Kinesin_motor_dom
IPR036961 Kinesin_motor_dom_sf
IPR027417 P-loop_NTPase
IPR008984 SMAD_FHA_dom_sf
PANTHERiPTHR24115 PTHR24115, 1 hit
PfamiView protein in Pfam
PF00498 FHA, 1 hit
PF00225 Kinesin, 1 hit
PF16183 Kinesin_assoc, 1 hit
PRINTSiPR00380 KINESINHEAVY
SMARTiView protein in SMART
SM00240 FHA, 1 hit
SM00129 KISc, 1 hit
SUPFAMiSSF49879 SSF49879, 1 hit
SSF52540 SSF52540, 1 hit
PROSITEiView protein in PROSITE
PS00411 KINESIN_MOTOR_1, 1 hit
PS50067 KINESIN_MOTOR_2, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiKIF14_HUMAN
AccessioniPrimary (citable) accession number: Q15058
Secondary accession number(s): Q14CI8, Q4G0A5, Q5T1W3
Entry historyiIntegrated into UniProtKB/Swiss-Prot: September 19, 2002
Last sequence update: November 1, 1996
Last modified: November 7, 2018
This is version 169 of the entry and version 1 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

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  3. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
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