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P38432

- COIL_HUMAN

UniProt

P38432 - COIL_HUMAN

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Protein
Coilin
Gene
COIL, CLN80
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Component of nuclear coiled bodies, also known as Cajal bodies or CBs, which are involved in the modification and assembly of nucleoplasmic snRNPs.1 Publication

GO - Molecular functioni

  1. disulfide oxidoreductase activity Source: Ensembl
  2. identical protein binding Source: IntAct
  3. protein C-terminus binding Source: UniProtKB
  4. protein binding Source: IntAct
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Coilin
Alternative name(s):
p80-coilin
Gene namesi
Name:COIL
Synonyms:CLN80
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 17

Organism-specific databases

HGNCiHGNC:2184. COIL.

Subcellular locationi

Nucleus. NucleusCajal body 1 Publication

GO - Cellular componenti

  1. Cajal body Source: UniProtKB
  2. cytoplasm Source: HPA
  3. female germ cell nucleus Source: Ensembl
  4. nucleolus Source: UniProtKB
  5. nucleoplasm Source: UniProtKB
  6. nucleus Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi413 – 4197RGRGRGR → GGGGGGG: Impaired interaction with SMN. 1 Publication

Organism-specific databases

PharmGKBiPA26700.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 576576Coilin
PRO_0000058146Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei105 – 1051Phosphoserine1 Publication
Modified residuei122 – 1221Phosphothreonine4 Publications
Modified residuei184 – 1841Phosphoserine; by VRK1 and VRK21 Publication
Modified residuei271 – 2711Phosphoserine3 Publications
Modified residuei272 – 2721Phosphoserine1 Publication
Modified residuei290 – 2901Phosphothreonine1 Publication
Modified residuei301 – 3011Phosphoserine1 Publication
Modified residuei303 – 3031Phosphothreonine1 Publication
Modified residuei456 – 4561Phosphothreonine1 Publication
Modified residuei489 – 4891Phosphoserine3 Publications
Modified residuei566 – 5661Phosphoserine2 Publications

Post-translational modificationi

Symmetrical dimethylation of arginine residues within the RG repeat region enhances affinity for SMN, and thus localization of SMN complexes to CBs.
Phosphorylation during mitosis is associated with disassembly of CBs.

Keywords - PTMi

Methylation, Phosphoprotein

Proteomic databases

MaxQBiP38432.
PaxDbiP38432.
PeptideAtlasiP38432.
PRIDEiP38432.

PTM databases

PhosphoSiteiP38432.

Expressioni

Tissue specificityi

Found in all the cell types examined.

Gene expression databases

ArrayExpressiP38432.
BgeeiP38432.
CleanExiHS_COIL.
GenevestigatoriP38432.

Organism-specific databases

HPAiCAB017524.
HPA027884.

Interactioni

Subunit structurei

Interacts with ANKS1B. Interacts with SMN (via Tudor domain). Interacts (via C-terminus) with AK6.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself3EBI-945751,EBI-945751
AK6Q9Y3D85EBI-945751,EBI-2896123
ATXN1P542533EBI-945751,EBI-930964
ATXN1P54253-16EBI-945751,EBI-930975
CEP70Q8NHQ13EBI-945751,EBI-739624
LNX1Q8TBB12EBI-945751,EBI-739832
PICK1Q9NRD53EBI-945751,EBI-79165
PSME3P612893EBI-945751,EBI-355546
VRK1Q999869EBI-945751,EBI-1769146
XRCC5P130106EBI-945751,EBI-357997
XRCC6P129563EBI-945751,EBI-353208

Protein-protein interaction databases

BioGridi113815. 71 interactions.
DIPiDIP-38503N.
IntActiP38432. 62 interactions.
MINTiMINT-2855441.
STRINGi9606.ENSP00000240316.

Structurei

3D structure databases

ProteinModelPortaliP38432.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati223 – 22641-1
Repeati268 – 27141-2
Repeati386 – 38942-1
Repeati413 – 41423-1
Repeati415 – 41623-2
Repeati417 – 41823-3
Repeati419 – 42023-4
Domaini460 – 559100Tudor; atypical
Add
BLAST
Repeati517 – 52042-2

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni223 – 271492 X 4 AA repeats of A-R-N-S
Add
BLAST
Regioni386 – 5201352 X 4 AA repeats of S-L-P-A
Add
BLAST
Regioni392 – 42029Required for interaction with SMN
Add
BLAST
Regioni413 – 42084 X 2 AA tandem repeats of R-G

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi181 – 20121Lys-rich (basic)
Add
BLAST
Compositional biasi243 – 25210Ser/Thr-rich
Compositional biasi310 – 32011Ser/Thr-rich
Add
BLAST

Domaini

The atypical Tudor domain at the C-terminus contains two large unstructured loops, and does not bind methylated residues.1 Publication

Sequence similaritiesi

Belongs to the coilin family.
Contains 1 Tudor domain.

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG84544.
HOGENOMiHOG000059586.
HOVERGENiHBG007989.
InParanoidiP38432.
KOiK13150.
OMAiCRVVTDL.
OrthoDBiEOG712TX9.
PhylomeDBiP38432.
TreeFamiTF331811.

Family and domain databases

InterProiIPR024822. Coilin.
[Graphical view]
PANTHERiPTHR15197:SF0. PTHR15197:SF0. 1 hit.

Sequencei

Sequence statusi: Complete.

P38432-1 [UniParc]FASTAAdd to Basket

« Hide

MAASETVRLR LQFDYPPPAT PHCTAFWLLV DLNRCRVVTD LISLIRQRFG    50
FSSGAFLGLY LEGGLLPPAE SARLVRDNDC LRVKLEERGV AENSVVISNG 100
DINLSLRKAK KRAFQLEEGE ETEPDCKYSK KHWKSRENNN NNEKVLDLEP 150
KAVTDQTVSK KNKRKNKATC GTVGDDNEEA KRKSPKKKEK CEYKKKAKNP 200
KSPKVQAVKD WANQRCSSPK GSARNSLVKA KRKGSVSVCS KESPSSSSES 250
ESCDESISDG PSKVTLEARN SSEKLPTELS KEEPSTKNTT ADKLAIKLGF 300
SLTPSKGKTS GTTSSSSDSS AESDDQCLMS SSTPECAAGF LKTVGLFAGR 350
GRPGPGLSSQ TAGAAGWRRS GSNGGGQAPG ASPSVSLPAS LGRGWGREEN 400
LFSWKGAKGR GMRGRGRGRG HPVSCVVNRS TDNQRQQQLN DVVKNSSTII 450
QNPVETPKKD YSLLPLLAAA PQVGEKIAFK LLELTSSYSP DVSDYKEGRI 500
LSHNPETQQV DIEILSSLPA LREPGKFDLV YHNENGAEVV EYAVTQESKI 550
TVFWKELIDP RLIIESPSNT SSTEPA 576
Length:576
Mass (Da):62,608
Last modified:October 1, 1994 - v1
Checksum:i879702B590F16849
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M58411 mRNA. Translation: AAA36412.1.
AK313616 mRNA. Translation: BAG36378.1.
AC004584 Genomic DNA. No translation available.
CH471109 Genomic DNA. Translation: EAW94522.1.
BC010385 mRNA. Translation: AAH10385.1.
U06632 mRNA. Translation: AAB81550.1.
CCDSiCCDS11592.1.
PIRiS50113.
RefSeqiNP_004636.1. NM_004645.2.
UniGeneiHs.532795.

Genome annotation databases

EnsembliENST00000240316; ENSP00000240316; ENSG00000121058.
GeneIDi8161.
KEGGihsa:8161.
UCSCiuc002iuu.3. human.

Polymorphism databases

DMDMi585632.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M58411 mRNA. Translation: AAA36412.1 .
AK313616 mRNA. Translation: BAG36378.1 .
AC004584 Genomic DNA. No translation available.
CH471109 Genomic DNA. Translation: EAW94522.1 .
BC010385 mRNA. Translation: AAH10385.1 .
U06632 mRNA. Translation: AAB81550.1 .
CCDSi CCDS11592.1.
PIRi S50113.
RefSeqi NP_004636.1. NM_004645.2.
UniGenei Hs.532795.

3D structure databases

ProteinModelPortali P38432.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 113815. 71 interactions.
DIPi DIP-38503N.
IntActi P38432. 62 interactions.
MINTi MINT-2855441.
STRINGi 9606.ENSP00000240316.

PTM databases

PhosphoSitei P38432.

Polymorphism databases

DMDMi 585632.

Proteomic databases

MaxQBi P38432.
PaxDbi P38432.
PeptideAtlasi P38432.
PRIDEi P38432.

Protocols and materials databases

DNASUi 8161.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000240316 ; ENSP00000240316 ; ENSG00000121058 .
GeneIDi 8161.
KEGGi hsa:8161.
UCSCi uc002iuu.3. human.

Organism-specific databases

CTDi 8161.
GeneCardsi GC17M055015.
HGNCi HGNC:2184. COIL.
HPAi CAB017524.
HPA027884.
MIMi 600272. gene.
neXtProti NX_P38432.
PharmGKBi PA26700.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG84544.
HOGENOMi HOG000059586.
HOVERGENi HBG007989.
InParanoidi P38432.
KOi K13150.
OMAi CRVVTDL.
OrthoDBi EOG712TX9.
PhylomeDBi P38432.
TreeFami TF331811.

Miscellaneous databases

GeneWikii Coilin.
GenomeRNAii 8161.
NextBioi 30832.
PROi P38432.
SOURCEi Search...

Gene expression databases

ArrayExpressi P38432.
Bgeei P38432.
CleanExi HS_COIL.
Genevestigatori P38432.

Family and domain databases

InterProi IPR024822. Coilin.
[Graphical view ]
PANTHERi PTHR15197:SF0. PTHR15197:SF0. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Structure, expression and chromosomal localization of human p80-coilin gene."
    Chan E.K.L., Takano S., Andrade L.E.C., Hamel J.C., Matera A.G.
    Nucleic Acids Res. 22:4462-4469(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Liver.
  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.
    , 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].
    Tissue: Thymus.
  3. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
    Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
    , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
    Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. 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].
    Tissue: Brain.
  6. "Human autoantibody to a novel protein of the nuclear coiled body: immunological characterization and cDNA cloning of p80-coilin."
    Andrade L.E.C., Chan E.K.L., Raska I., Peebles C.L., Roos G., Tan E.M.
    J. Exp. Med. 173:1407-1419(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 172-576.
    Tissue: Liver.
  7. "Assembly of snRNP-containing coiled bodies is regulated in interphase and mitosis -- evidence that the coiled body is a kinetic nuclear structure."
    Carmo-Fonseca M., Ferreira J., Lamond A.I.
    J. Cell Biol. 120:841-852(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION.
  8. "Coilin forms the bridge between Cajal bodies and SMN, the spinal muscular atrophy protein."
    Hebert M.D., Szymczyk P.W., Shpargel K.B., Matera A.G.
    Genes Dev. 15:2720-2729(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SMN, MUTAGENESIS OF 413-ARG--ARG-419.
  9. "Coilin methylation regulates nuclear body formation."
    Hebert M.D., Shpargel K.B., Ospina J.K., Tucker K.E., Matera A.G.
    Dev. Cell 3:329-337(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: METHYLATION OF RG REPEATS.
  10. "A novel EB-1/AIDA-1 isoform, AIDA-1c, interacts with the Cajal body protein coilin."
    Xu H., Hebert M.D.
    BMC Cell Biol. 6:23-23(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ANKS1B.
  11. "Characterization of hCINAP, a novel coilin-interacting protein encoded by a transcript from the transcription factor TAFIID32 locus."
    Santama N., Ogg S.C., Malekkou A., Zographos S.E., Weis K., Lamond A.I.
    J. Biol. Chem. 280:36429-36441(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH AK6.
  12. "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 THR-122, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
    Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
    Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-122 AND SER-489, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-271; THR-290; SER-301; THR-303 AND SER-489, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  17. "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-105; THR-122; SER-271; SER-272; THR-456; SER-489 AND SER-566, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  18. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. "Substrate profiling of human vaccinia-related kinases identifies coilin, a Cajal body nuclear protein, as a phosphorylation target with neurological implications."
    Sanz-Garcia M., Vazquez-Cedeira M., Kellerman E., Renbaum P., Levy-Lahad E., Lazo P.A.
    J. Proteomics 75:548-560(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-184 BY VRK1 AND VRK2.
  20. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-122; SER-271 AND SER-566, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  21. "Solution structure of the carboxy-terminal Tudor domain from human Coilin."
    Shanbhag R., Kurabi A., Kwan J.J., Donaldson L.W.
    FEBS Lett. 584:4351-4356(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 460-576, DOMAIN TUDOR.

Entry informationi

Entry nameiCOIL_HUMAN
AccessioniPrimary (citable) accession number: P38432
Secondary accession number(s): B2R931
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: July 9, 2014
This is version 128 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 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi