Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P50995

- ANX11_HUMAN

UniProt

P50995 - ANX11_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Annexin A11

Gene

ANXA11

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

Functioni

Binds specifically to calcyclin in a calcium-dependent manner (By similarity). Required for midbody formation and completion of the terminal phase of cytokinesis.By similarity1 Publication

GO - Molecular functioni

  1. calcium-dependent phospholipid binding Source: UniProtKB-KW
  2. calcium-dependent protein binding Source: UniProtKB
  3. calcium ion binding Source: Ensembl
  4. MHC class II protein complex binding Source: UniProt
  5. phosphatidylethanolamine binding Source: Ensembl
  6. poly(A) RNA binding Source: UniProtKB
  7. S100 protein binding Source: UniProtKB

GO - Biological processi

  1. cytokinesis, completion of separation Source: UniProtKB
  2. phagocytosis Source: UniProtKB
  3. response to calcium ion Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division

Keywords - Ligandi

Calcium, Calcium/phospholipid-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Annexin A11
Alternative name(s):
56 kDa autoantigen
Annexin XI
Annexin-11
Calcyclin-associated annexin 50
Short name:
CAP-50
Gene namesi
Name:ANXA11
Synonyms:ANX11
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 10

Organism-specific databases

HGNCiHGNC:535. ANXA11.

Subcellular locationi

Cytoplasm. Melanosome. Nucleus envelope. Nucleusnucleoplasm. Cytoplasmcytoskeletonspindle
Note: Found throughout the nucleoplasm at interphase and during mitosis concentrates around the mitotic apparatus (By similarity). Elevation of intracellular calcium causes relocalization from the nucleoplasm to the nuclear envelope, with little effect on the cytoplasmic pool. Localization to the nuclear envelope is cell-cycle dependent.By similarity

GO - Cellular componenti

  1. azurophil granule Source: UniProtKB
  2. cytoplasm Source: UniProtKB
  3. extracellular vesicular exosome Source: UniProtKB
  4. membrane Source: UniProtKB
  5. midbody Source: UniProtKB
  6. nuclear envelope Source: UniProtKB
  7. nucleoplasm Source: UniProtKB
  8. nucleus Source: HPA
  9. phagocytic vesicle Source: UniProtKB
  10. specific granule Source: UniProtKB
  11. spindle Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA24825.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 505505Annexin A11PRO_0000067510Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei248 – 2481N6-acetyllysine1 Publication
Modified residuei255 – 2551N6-acetyllysine1 Publication
Modified residuei479 – 4791N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP50995.
PeptideAtlasiP50995.
PRIDEiP50995.

2D gel databases

REPRODUCTION-2DPAGEP50995.

PTM databases

PhosphoSiteiP50995.

Expressioni

Gene expression databases

BgeeiP50995.
CleanExiHS_ANXA11.
ExpressionAtlasiP50995. baseline and differential.
GenevestigatoriP50995.

Organism-specific databases

HPAiCAB004851.
HPA027545.

Interactioni

Subunit structurei

Interacts with S100A6 (By similarity). Interacts with PDCD6 in a calcium-dependent manner. Interacts with KIF23 during cytokinesis.By similarity3 Publications

Protein-protein interaction databases

BioGridi106808. 21 interactions.
IntActiP50995. 9 interactions.
MINTiMINT-4998941.
STRINGi9606.ENSP00000265447.

Structurei

3D structure databases

ProteinModelPortaliP50995.
SMRiP50995. Positions 197-505.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati209 – 26961Annexin 1Add
BLAST
Repeati281 – 34161Annexin 2Add
BLAST
Repeati365 – 42561Annexin 3Add
BLAST
Repeati440 – 50061Annexin 4Add
BLAST

Domaini

A pair of annexin repeats may form one binding site for calcium and phospholipid.

Sequence similaritiesi

Belongs to the annexin family.Curated
Contains 4 annexin repeats.Curated

Keywords - Domaini

Annexin, Repeat

Phylogenomic databases

eggNOGiNOG267770.
GeneTreeiENSGT00760000118972.
HOVERGENiHBG061815.
InParanoidiP50995.
KOiK17095.
OMAiNMYPGAP.
OrthoDBiEOG74XS72.
PhylomeDBiP50995.
TreeFamiTF105452.

Family and domain databases

Gene3Di1.10.220.10. 4 hits.
InterProiIPR001464. Annexin.
IPR018502. Annexin_repeat.
IPR018252. Annexin_repeat_CS.
IPR008157. AnnexinXI.
[Graphical view]
PANTHERiPTHR10502:SF29. PTHR10502:SF29. 1 hit.
PfamiPF00191. Annexin. 4 hits.
[Graphical view]
PRINTSiPR00196. ANNEXIN.
PR01810. ANNEXINXI.
SMARTiSM00335. ANX. 4 hits.
[Graphical view]
PROSITEiPS00223. ANNEXIN. 4 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P50995-1) [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
MSYPGYPPPP GGYPPAAPGG GPWGGAAYPP PPSMPPIGLD NVATYAGQFN
60 70 80 90 100
QDYLSGMAAN MSGTFGGANM PNLYPGAPGA GYPPVPPGGF GQPPSAQQPV
110 120 130 140 150
PPYGMYPPPG GNPPSRMPSY PPYPGAPVPG QPMPPPGQQP PGAYPGQPPV
160 170 180 190 200
TYPGQPPVPL PGQQQPVPSY PGYPGSGTVT PAVPPTQFGS RGTITDAPGF
210 220 230 240 250
DPLRDAEVLR KAMKGFGTDE QAIIDCLGSR SNKQRQQILL SFKTAYGKDL
260 270 280 290 300
IKDLKSELSG NFEKTILALM KTPVLFDIYE IKEAIKGVGT DEACLIEILA
310 320 330 340 350
SRSNEHIREL NRAYKAEFKK TLEEAIRSDT SGHFQRLLIS LSQGNRDEST
360 370 380 390 400
NVDMSLAQRD AQELYAAGEN RLGTDESKFN AVLCSRSRAH LVAVFNEYQR
410 420 430 440 450
MTGRDIEKSI CREMSGDLEE GMLAVVKCLK NTPAFFAERL NKAMRGAGTK
460 470 480 490 500
DRTLIRIMVS RSETDLLDIR SEYKRMYGKS LYHDISGDTS GDYRKILLKI

CGGND
Length:505
Mass (Da):54,390
Last modified:October 1, 1996 - v1
Checksum:i4ADCAC8F270BFEE4
GO
Isoform 2 (identifier: P50995-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-33: Missing.

Note: No experimental confirmation available.

Show »
Length:472
Mass (Da):51,242
Checksum:i477704C7C6863AE0
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti191 – 1911R → Q.
Corresponds to variant rs2229554 [ dbSNP | Ensembl ].
VAR_048259
Natural varianti230 – 2301R → C.
Corresponds to variant rs1049550 [ dbSNP | Ensembl ].
VAR_012006
Natural varianti457 – 4571I → V.
Corresponds to variant rs1802932 [ dbSNP | Ensembl ].
VAR_012007

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 3333Missing in isoform 2. 1 PublicationVSP_054553Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L19605 mRNA. Translation: AAA19734.1.
AJ278463 mRNA. Translation: CAB94995.1.
AJ278464 mRNA. Translation: CAB94996.1.
AJ278465 mRNA. Translation: CAB94997.1.
AK301047 mRNA. Translation: BAG62659.1.
AL356095 Genomic DNA. No translation available.
AL513174 Genomic DNA. No translation available.
BC007564 mRNA. Translation: AAH07564.1.
CCDSiCCDS60576.1. [P50995-2]
CCDS7364.1. [P50995-1]
PIRiA53152.
RefSeqiNP_001148.1. NM_001157.2. [P50995-1]
NP_001265336.1. NM_001278407.1. [P50995-1]
NP_001265337.1. NM_001278408.1. [P50995-1]
NP_001265338.1. NM_001278409.1. [P50995-2]
NP_665875.1. NM_145868.1. [P50995-1]
NP_665876.1. NM_145869.1. [P50995-1]
UniGeneiHs.530291.

Genome annotation databases

EnsembliENST00000265447; ENSP00000265447; ENSG00000122359. [P50995-2]
ENST00000372231; ENSP00000361305; ENSG00000122359. [P50995-1]
ENST00000422982; ENSP00000404412; ENSG00000122359. [P50995-1]
ENST00000438331; ENSP00000398610; ENSG00000122359. [P50995-1]
GeneIDi311.
KEGGihsa:311.
UCSCiuc001kbq.1. human. [P50995-1]

Polymorphism databases

DMDMi1703322.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L19605 mRNA. Translation: AAA19734.1 .
AJ278463 mRNA. Translation: CAB94995.1 .
AJ278464 mRNA. Translation: CAB94996.1 .
AJ278465 mRNA. Translation: CAB94997.1 .
AK301047 mRNA. Translation: BAG62659.1 .
AL356095 Genomic DNA. No translation available.
AL513174 Genomic DNA. No translation available.
BC007564 mRNA. Translation: AAH07564.1 .
CCDSi CCDS60576.1. [P50995-2 ]
CCDS7364.1. [P50995-1 ]
PIRi A53152.
RefSeqi NP_001148.1. NM_001157.2. [P50995-1 ]
NP_001265336.1. NM_001278407.1. [P50995-1 ]
NP_001265337.1. NM_001278408.1. [P50995-1 ]
NP_001265338.1. NM_001278409.1. [P50995-2 ]
NP_665875.1. NM_145868.1. [P50995-1 ]
NP_665876.1. NM_145869.1. [P50995-1 ]
UniGenei Hs.530291.

3D structure databases

ProteinModelPortali P50995.
SMRi P50995. Positions 197-505.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 106808. 21 interactions.
IntActi P50995. 9 interactions.
MINTi MINT-4998941.
STRINGi 9606.ENSP00000265447.

PTM databases

PhosphoSitei P50995.

Polymorphism databases

DMDMi 1703322.

2D gel databases

REPRODUCTION-2DPAGE P50995.

Proteomic databases

PaxDbi P50995.
PeptideAtlasi P50995.
PRIDEi P50995.

Protocols and materials databases

DNASUi 311.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000265447 ; ENSP00000265447 ; ENSG00000122359 . [P50995-2 ]
ENST00000372231 ; ENSP00000361305 ; ENSG00000122359 . [P50995-1 ]
ENST00000422982 ; ENSP00000404412 ; ENSG00000122359 . [P50995-1 ]
ENST00000438331 ; ENSP00000398610 ; ENSG00000122359 . [P50995-1 ]
GeneIDi 311.
KEGGi hsa:311.
UCSCi uc001kbq.1. human. [P50995-1 ]

Organism-specific databases

CTDi 311.
GeneCardsi GC10M081904.
HGNCi HGNC:535. ANXA11.
HPAi CAB004851.
HPA027545.
MIMi 602572. gene.
neXtProti NX_P50995.
PharmGKBi PA24825.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG267770.
GeneTreei ENSGT00760000118972.
HOVERGENi HBG061815.
InParanoidi P50995.
KOi K17095.
OMAi NMYPGAP.
OrthoDBi EOG74XS72.
PhylomeDBi P50995.
TreeFami TF105452.

Miscellaneous databases

ChiTaRSi ANXA11. human.
GeneWikii ANXA11.
GenomeRNAii 311.
NextBioi 1259.
PROi P50995.
SOURCEi Search...

Gene expression databases

Bgeei P50995.
CleanExi HS_ANXA11.
ExpressionAtlasi P50995. baseline and differential.
Genevestigatori P50995.

Family and domain databases

Gene3Di 1.10.220.10. 4 hits.
InterProi IPR001464. Annexin.
IPR018502. Annexin_repeat.
IPR018252. Annexin_repeat_CS.
IPR008157. AnnexinXI.
[Graphical view ]
PANTHERi PTHR10502:SF29. PTHR10502:SF29. 1 hit.
Pfami PF00191. Annexin. 4 hits.
[Graphical view ]
PRINTSi PR00196. ANNEXIN.
PR01810. ANNEXINXI.
SMARTi SM00335. ANX. 4 hits.
[Graphical view ]
PROSITEi PS00223. ANNEXIN. 4 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The 56K autoantigen is identical to human annexin XI."
    Misaki Y., Pruijn G.J.M., van der Kemp A.W., van Venrooij W.J.
    J. Biol. Chem. 269:4240-4246(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Teratocarcinoma.
  2. "Annexin A11 (ANXA11) gene structure as the progenitor of paralogous annexins and source of orthologous cDNA isoforms."
    Bances P., Fernandez M.R., Rodriguez-Garcia M.I., Morgan R.O., Fernandez M.-P.
    Genomics 69:95-103(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  3. "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] (ISOFORM 2).
    Tissue: Spleen.
  4. "The DNA sequence and comparative analysis of human chromosome 10."
    Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
    , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
    Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
    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] (ISOFORM 1).
    Tissue: Lymph.
  6. "ALG-2 interacts with the amino-terminal domain of annexin XI in a Ca(2+)-dependent manner."
    Satoh H., Shibata H., Nakano Y., Kitaura Y., Maki M.
    Biochem. Biophys. Res. Commun. 291:1166-1172(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PDCD6.
  7. "Calcium- and cell cycle-dependent association of annexin 11 with the nuclear envelope."
    Tomas A., Moss S.E.
    J. Biol. Chem. 278:20210-20216(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  8. "Dissecting the cellular functions of annexin XI using recombinant human annexin XI-specific autoantibodies cloned by phage display."
    Farnaes L., Ditzel H.J.
    J. Biol. Chem. 278:33120-33126(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  9. "Annexin 11 is required for midbody formation and completion of the terminal phase of cytokinesis."
    Tomas A., Futter C., Moss S.E.
    J. Cell Biol. 165:813-822(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH KIF23.
  10. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    Tissue: Melanoma.
  11. "Identification of Alix-type and non-Alix-type ALG-2-binding sites in human phospholipid scramblase 3: differential binding to an alternatively spliced isoform and amino acid-substituted mutants."
    Shibata H., Suzuki H., Kakiuchi T., Inuzuka T., Yoshida H., Mizuno T., Maki M.
    J. Biol. Chem. 283:9623-9632(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PDCD6.
  12. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-248; LYS-255 AND LYS-479, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiANX11_HUMAN
AccessioniPrimary (citable) accession number: P50995
Secondary accession number(s): B4DVE7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: October 29, 2014
This is version 133 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 10
    Human chromosome 10: 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