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Q15058

- KIF14_HUMAN

UniProt

Q15058 - KIF14_HUMAN

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Protein
Kinesin-like protein KIF14
Gene
KIF14, KIAA0042
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Plays an essential role in cytokinesis.2 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi447 – 4548ATP By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. PDZ domain binding Source: MGI
  3. microtubule motor activity Source: InterPro
  4. protein binding Source: UniProtKB

GO - Biological processi

  1. establishment of protein localization Source: MGI
  2. microtubule-based movement Source: InterPro
  3. negative regulation of integrin activation Source: MGI
  4. regulation of Rap protein signal transduction Source: MGI
  5. regulation of cell adhesion Source: MGI
  6. regulation of cell migration Source: MGI
  7. substrate adhesion-dependent cell spreading Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Motor protein

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Kinesin-like protein KIF14
Gene namesi
Name:KIF14
Synonyms:KIAA0042
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:19181. KIF14.

Subcellular locationi

Nucleus. Cytoplasm. Cytoplasmcytoskeletonspindle
Note: Nuclear localization observed during interphase in 1 Publication or triggered by entry into mitosis in 1 Publication. Cytoplasmic in interphase (1 Publication) and metaphase cells (1 Publication). From prophase to metaphase, accumulates at the developing spindle poles and their associated microtubules. During anaphase, accumulates at the spindle midzone. Localization to the central spindle and midbody during anaphase is dependent upon PRC1 and CIT presence. In cells ready to undergo abscission, concentrates at the contractile ring.2 Publications

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
  2. kinesin complex Source: InterPro
  3. microtubule Source: MGI
  4. nucleus Source: UniProtKB-SubCell
  5. spindle Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Microtubule, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA38820.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 16481648Kinesin-like protein KIF14
PRO_0000125449Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei12 – 121Phosphoserine1 Publication
Cross-linki275 – 275Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residuei1292 – 12921Phosphoserine1 Publication

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ15058.
PaxDbiQ15058.
PRIDEiQ15058.

PTM databases

PhosphoSiteiQ15058.

Expressioni

Developmental stagei

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

Gene expression databases

BgeeiQ15058.
CleanExiHS_KIF14.
GenevestigatoriQ15058.

Organism-specific databases

HPAiHPA038061.

Interactioni

Subunit structurei

Directly interacts with PRC1 within a complex also containing KIF4A, KIF20A and KIF23. Directly interacts with CIT depending on the activation state of the kinase (stronger interaction with the kinase-dead form). Interacts with ARRB2; the interaction is detected in the nucleus upon OR1D2 stimulation.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
SVILO463853EBI-1045252,EBI-6995105From a different organism.

Protein-protein interaction databases

BioGridi115256. 7 interactions.
IntActiQ15058. 3 interactions.
MINTiMINT-4989440.
STRINGi9606.ENSP00000356319.

Structurei

3D structure databases

ProteinModelPortaliQ15058.
SMRiQ15058. Positions 357-699, 777-906.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini358 – 701344Kinesin motor
Add
BLAST
Domaini825 – 89167FHA
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 356356Required for PRC1-binding
Add
BLAST
Regioni901 – 1648748Required for CIT-binding
Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili705 – 79187 Reviewed prediction
Add
BLAST
Coiled coili922 – 1079158 Reviewed prediction
Add
BLAST
Coiled coili1332 – 134817 Reviewed prediction
Add
BLAST
Coiled coili1468 – 150033 Reviewed prediction
Add
BLAST

Sequence similaritiesi

Contains 1 FHA domain.

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiCOG5059.
HOGENOMiHOG000113224.
HOVERGENiHBG052249.
InParanoidiQ15058.
KOiK17915.
OMAiFLQGCCS.
OrthoDBiEOG74TWXS.
PhylomeDBiQ15058.
TreeFamiTF105221.

Family and domain databases

Gene3Di2.60.200.20. 1 hit.
3.40.850.10. 1 hit.
InterProiIPR000253. FHA_dom.
IPR027640. Kinesin-like_fam.
IPR019821. Kinesin_motor_CS.
IPR001752. Kinesin_motor_dom.
IPR027417. P-loop_NTPase.
IPR008984. SMAD_FHA_domain.
[Graphical view]
PANTHERiPTHR24115. PTHR24115. 1 hit.
PfamiPF00498. FHA. 1 hit.
PF00225. Kinesin. 1 hit.
[Graphical view]
PRINTSiPR00380. KINESINHEAVY.
SMARTiSM00240. FHA. 1 hit.
SM00129. KISc. 1 hit.
[Graphical view]
SUPFAMiSSF49879. SSF49879. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEiPS00411. KINESIN_MOTOR_1. 1 hit.
PS50067. KINESIN_MOTOR_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q15058-1 [UniParc]FASTAAdd to Basket

« Hide

MSLHSTHNRN NSGDILDIPS SQNSSSLNAL THSSRLKLHL KSDMSECEND     50
DPLLRSAGKV RDINRTYVIS ASRKTADMPL TPNPVGRLAL QRRTTRNKES 100
SLLVSELEDT TEKTAETRLT LQRRAKTDSA EKWKTAEIDS VKMTLNVGGE 150
TENNGVSKES RTNVRIVNNA KNSFVASSVP LDEDPQVIEM MADKKYKETF 200
SAPSRANENV ALKYSSNRPP IASLSQTEVV RSGHLTTKPT QSKLDIKVLG 250
TGNLYHRSIG KEIAKTSNKF GSLEKRTPTK CTTEHKLTTK CSLPQLKSPA 300
PSILKNRMSN LQVKQRPKSS FLANKQERSA ENTILPEEET VVQNTSAGKD 350
PLKVENSQVT VAVRVRPFTK REKIEKASQV VFMSGKEITV EHPDTKQVYN 400
FIYDVSFWSF DECHPHYASQ TTVYEKLAAP LLERAFEGFN TCLFAYGQTG 450
SGKSYTMMGF SEEPGIIPRF CEDLFSQVAR KQTQEVSYHI EMSFFEVYNE 500
KIHDLLVCKD ENGQRKQPLR VREHPVYGPY VEALSMNIVS SYADIQSWLE 550
LGNKQRATAA TGMNDKSSRS HSVFTLVMTQ TKTEFVEGEE HDHRITSRIN 600
LIDLAGSERC STAHTNGDRL KEGVSINKSL LTLGKVISAL SEQANQRSVF 650
IPYRESVLTW LLKESLGGNS KTAMIATISP AASNIEETLS TLRYANQARL 700
IVNIAKVNED MNAKLIRELK AEIAKLKAAQ RNSRNIDPER YRLCRQEITS 750
LRMKLHQQER DMAEMQRVWK EKFEQAEKRK LQETKELQKA GIMFQMDNHL 800
PNLVNLNEDP QLSEMLLYMI KEGTTTVGKY KPNSSHDIQL SGVLIADDHC 850
TIKNFGGTVS IIPVGEAKTY VNGKHILEIT VLRHGDRVIL GGDHYFRFNH 900
PVEVQKGKRP SGRDTPISEG PKDFEFAKNE LLMAQRSQLE AEIKEAQLKA 950
KEEMMQGIQI AKEMAQQELS SQKAAYESKI KALEAELREE SQRKKMQEIN 1000
NQKANHKIEE LEKAKQHLEQ EIYVNKKRLE METLATKQAL EDHSIRHARI 1050
LEALETEKQK IAKEVQILQQ NRNNRDKTFT VQTTWSSMKL SMMIQEANAI 1100
SSKLKTYYVF GRHDISDKSS SDTSIRVRNL KLGISTFWSL EKFESKLAAM 1150
KELYESNGSN RGEDAFCDPE DEWEPDITDA PVSSLSRRRS RSLMKNRRIS 1200
GCLHDIQVHP IKNLHSSHSS GLMDKSSTIY SNSAESFLPG ICKELIGSSL 1250
DFFGQSYDEE RTIADSLINS FLKIYNGLFA ISKAHEEQDE ESQDNLFSSD 1300
RAIQSLTIQT ACAFEQLVVL MKHWLSDLLP CTNIARLEDE LRQEVKKLGG 1350
YLQLFLQGCC LDISSMIKEA QKNAIQIVQQ AVKYVGQLAV LKGSKLHFLE 1400
NGNNKAASVQ EEFMDAVCDG VGLGMKILLD SGLEKAKELQ HELFRQCTKN 1450
EVTKEMKTNA MGLIRSLENI FAESKIKSFR RQVQEENFEY QDFKRMVNRA 1500
PEFLKLKHCL EKAIEIIISA LKGCHSDINL LQTCVESIRN LASDFYSDFS 1550
VPSTSVGSYE SRVTHIVHQE LESLAKSLLF CFESEESPDL LKPWETYNQN 1600
TKEEHQQSKS SGIDGSKNKG VPKRVYELHG SSPAVSSEEC TPSRIQWV 1648
Length:1,648
Mass (Da):186,492
Last modified:November 1, 1996 - v1
Checksum:iFB1423668A7B79D7
GO

Sequence cautioni

The sequence BAA05392.2 differs from that shown. Reason: Erroneous initiation.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti1633 – 16331P → A.1 Publication
Corresponds to variant rs12120084 [ dbSNP | Ensembl ].
VAR_037777

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti660 – 6601W → C in AAH98582. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D26361 mRNA. Translation: BAA05392.2. Different initiation.
AL445483 Genomic DNA. Translation: CAI17049.1.
CH471067 Genomic DNA. Translation: EAW91316.1.
BC098582 mRNA. Translation: AAH98582.1.
BC113742 mRNA. Translation: AAI13743.1.
CCDSiCCDS30963.1.
RefSeqiNP_055690.1. NM_014875.2.
UniGeneiHs.3104.

Genome annotation databases

EnsembliENST00000367350; ENSP00000356319; ENSG00000118193.
GeneIDi9928.
KEGGihsa:9928.
UCSCiuc010ppj.1. human.

Polymorphism databases

DMDMi23396633.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D26361 mRNA. Translation: BAA05392.2 . Different initiation.
AL445483 Genomic DNA. Translation: CAI17049.1 .
CH471067 Genomic DNA. Translation: EAW91316.1 .
BC098582 mRNA. Translation: AAH98582.1 .
BC113742 mRNA. Translation: AAI13743.1 .
CCDSi CCDS30963.1.
RefSeqi NP_055690.1. NM_014875.2.
UniGenei Hs.3104.

3D structure databases

ProteinModelPortali Q15058.
SMRi Q15058. Positions 357-699, 777-906.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115256. 7 interactions.
IntActi Q15058. 3 interactions.
MINTi MINT-4989440.
STRINGi 9606.ENSP00000356319.

Chemistry

BindingDBi Q15058.
ChEMBLi CHEMBL5576.

PTM databases

PhosphoSitei Q15058.

Polymorphism databases

DMDMi 23396633.

Proteomic databases

MaxQBi Q15058.
PaxDbi Q15058.
PRIDEi Q15058.

Protocols and materials databases

DNASUi 9928.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000367350 ; ENSP00000356319 ; ENSG00000118193 .
GeneIDi 9928.
KEGGi hsa:9928.
UCSCi uc010ppj.1. human.

Organism-specific databases

CTDi 9928.
GeneCardsi GC01M200521.
HGNCi HGNC:19181. KIF14.
HPAi HPA038061.
MIMi 611279. gene.
neXtProti NX_Q15058.
PharmGKBi PA38820.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5059.
HOGENOMi HOG000113224.
HOVERGENi HBG052249.
InParanoidi Q15058.
KOi K17915.
OMAi FLQGCCS.
OrthoDBi EOG74TWXS.
PhylomeDBi Q15058.
TreeFami TF105221.

Miscellaneous databases

GeneWikii KIF14.
GenomeRNAii 9928.
NextBioi 37458.
PROi Q15058.
SOURCEi Search...

Gene expression databases

Bgeei Q15058.
CleanExi HS_KIF14.
Genevestigatori Q15058.

Family and domain databases

Gene3Di 2.60.200.20. 1 hit.
3.40.850.10. 1 hit.
InterProi IPR000253. FHA_dom.
IPR027640. Kinesin-like_fam.
IPR019821. Kinesin_motor_CS.
IPR001752. Kinesin_motor_dom.
IPR027417. P-loop_NTPase.
IPR008984. SMAD_FHA_domain.
[Graphical view ]
PANTHERi PTHR24115. PTHR24115. 1 hit.
Pfami PF00498. FHA. 1 hit.
PF00225. Kinesin. 1 hit.
[Graphical view ]
PRINTSi PR00380. KINESINHEAVY.
SMARTi SM00240. FHA. 1 hit.
SM00129. KISc. 1 hit.
[Graphical view ]
SUPFAMi SSF49879. SSF49879. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEi PS00411. KINESIN_MOTOR_1. 1 hit.
PS50067. KINESIN_MOTOR_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Prediction of the coding sequences of unidentified human genes. II. The coding sequences of 40 new genes (KIAA0041-KIAA0080) deduced by analysis of cDNA clones from human cell line KG-1."
    Nomura N., Nagase T., Miyajima N., Sazuka T., Tanaka A., Sato S., Seki N., Kawarabayasi Y., Ishikawa K., Tabata S.
    DNA Res. 1:223-229(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Bone marrow.
  2. "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.
    , 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].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  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], VARIANT ALA-1633.
    Tissue: Uterus.
  5. "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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1292, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  6. "KIF14 and citron kinase act together to promote efficient cytokinesis."
    Gruneberg U., Neef R., Li X., Chan E.H.Y., Chalamalasetty R.B., Nigg E.A., Barr F.A.
    J. Cell Biol. 172:363-372(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PRC1 AND CIT.
  7. "Novel function of beta-arrestin2 in the nucleus of mature spermatozoa."
    Neuhaus E.M., Mashukova A., Barbour J., Wolters D., Hatt H.
    J. Cell Sci. 119:3047-3056(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ARRB2.
  8. "RNA interference-mediated silencing of mitotic kinesin KIF14 disrupts cell cycle progression and induces cytokinesis failure."
    Carleton M., Mao M., Biery M., Warrener P., Kim S., Buser C., Marshall C.G., Fernandes C., Annis J., Linsley P.S.
    Mol. Cell. Biol. 26:3853-3863(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE.
  9. "The proteomic reactor facilitates the analysis of affinity-purified proteins by mass spectrometry: application for identifying ubiquitinated proteins in human cells."
    Vasilescu J., Zweitzig D.R., Denis N.J., Smith J.C., Ethier M., Haines D.S., Figeys D.
    J. Proteome Res. 6:298-305(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-275.
    Tissue: Lung adenocarcinoma.
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiKIF14_HUMAN
AccessioniPrimary (citable) accession number: Q15058
Secondary accession number(s): Q14CI8, Q4G0A5, Q5T1W3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 19, 2002
Last sequence update: November 1, 1996
Last modified: July 9, 2014
This is version 127 of the entry and version 1 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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