Skip Header

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

Hematological and neurological expressed 1 protein

Gene

HN1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Names & Taxonomyi

Protein namesi
Recommended name:
Hematological and neurological expressed 1 protein
Alternative name(s):
Androgen-regulated protein 2
Cleaved into the following chain:
Gene namesi
Name:HN1
Synonyms:ARM2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 17

Organism-specific databases

HGNCiHGNC:14569. HN1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA29347.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 154154Hematological and neurological expressed 1 proteinPRO_0000424487Add
BLAST
Initiator methionineiRemoved; alternateCombined sources1 Publication
Chaini2 – 154153Hematological and neurological expressed 1 protein, N-terminally processedPRO_0000054918Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineCombined sources
Modified residuei2 – 21N-acetylthreonine; in Hematological and neurological expressed 1 protein, N-terminally processedCombined sources1 Publication
Modified residuei54 – 541PhosphothreonineCombined sources
Modified residuei80 – 801PhosphoserineCombined sources
Modified residuei87 – 871PhosphoserineCombined sources1 Publication
Modified residuei88 – 881PhosphoserineCombined sources
Modified residuei92 – 921PhosphoserineBy similarity
Modified residuei131 – 1311PhosphoserineCombined sources
Modified residuei148 – 1481N6-acetyllysineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ9UK76.
MaxQBiQ9UK76.
PaxDbiQ9UK76.
PRIDEiQ9UK76.
TopDownProteomicsiQ9UK76-1. [Q9UK76-1]
Q9UK76-2. [Q9UK76-2]
Q9UK76-3. [Q9UK76-3]

PTM databases

iPTMnetiQ9UK76.
PhosphoSiteiQ9UK76.

Expressioni

Tissue specificityi

Expressed in testis, skeletal muscle, thymus, prostate, colon, peripheral blood cells, brain and placenta.1 Publication

Gene expression databases

BgeeiQ9UK76.
CleanExiHS_HN1.
ExpressionAtlasiQ9UK76. baseline and differential.
GenevisibleiQ9UK76. HS.

Organism-specific databases

HPAiHPA059729.

Interactioni

Protein-protein interaction databases

BioGridi119338. 14 interactions.
IntActiQ9UK76. 2 interactions.
MINTiMINT-1390948.
STRINGi9606.ENSP00000348316.

Structurei

3D structure databases

ProteinModelPortaliQ9UK76.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the HN1 family.Curated

Phylogenomic databases

eggNOGiENOG410J50B. Eukaryota.
ENOG410YZCR. LUCA.
GeneTreeiENSGT00390000000756.
HOGENOMiHOG000231170.
HOVERGENiHBG055006.
InParanoidiQ9UK76.
OMAiCELHNLS.
PhylomeDBiQ9UK76.
TreeFamiTF327169.

Family and domain databases

InterProiIPR033335. JUPITER/HN1/HN1L.
[Graphical view]
PANTHERiPTHR34930. PTHR34930. 1 hit.
PfamiPF17054. JUPITER. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

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

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9UK76-1) [UniParc]FASTAAdd to basket

Also known as: HN1A

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
MTTTTTFKGV DPNSRNSSRV LRPPGGGSNF SLGFDEPTEQ PVRKNKMASN
60 70 80 90 100
IFGTPEENQA SWAKSAGAKS SGGREDLESS GLQRRNSSEA SSGDFLDLKG
110 120 130 140 150
EGDIHENVDT DLPGSLGQSE EKPVPAAPVP SPVAPAPVPS RRNPPGGKSS

LVLG
Length:154
Mass (Da):16,015
Last modified:January 23, 2007 - v3
Checksum:i1B443E4C7A28F093
GO
Isoform 2 (identifier: Q9UK76-2) [UniParc]FASTAAdd to basket

Also known as: HN1B

The sequence of this isoform differs from the canonical sequence as follows:
     100-154: GEGDIHENVD...PGGKSSLVLG → KMWTQTCQAA...LTVHLLDLFH

Show »
Length:181
Mass (Da):19,916
Checksum:iFF644A114DE28850
GO
Isoform 3 (identifier: Q9UK76-3) [UniParc]FASTAAdd to basket

Also known as: HN1C

The sequence of this isoform differs from the canonical sequence as follows:
     1-46: Missing.

Show »
Length:108
Mass (Da):11,023
Checksum:iC9E266E6180AB723
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti85 – 851R → G in BAD97041 (Ref. 5) Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 4646Missing in isoform 3. 2 PublicationsVSP_017132Add
BLAST
Alternative sequencei100 – 15455GEGDI…SLVLG → KMWTQTCQAAWGRVKRSPCL LRLCPARWPRPQCHPEEIPL AASPASSWVSSDCPERCRSV CFLHACELHNLSLTVHLLDL FH in isoform 2. 1 PublicationVSP_017133Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF086910 mRNA. Translation: AAP97140.1.
AY322169 mRNA. Translation: AAP83838.1.
AY322170 mRNA. Translation: AAP83839.1.
AF348672 Genomic DNA. Translation: AAL83903.1.
AF348672 Genomic DNA. Translation: AAP83962.1.
AF348672 Genomic DNA. Translation: AAP83963.1.
AF177862 mRNA. Translation: AAD53312.1.
AF266846 mRNA. Translation: AAQ14298.1.
AF266847 Genomic DNA. Translation: AAQ14299.1.
AK223321 mRNA. Translation: BAD97041.1.
AK312613 mRNA. Translation: BAG35500.1.
CH471099 Genomic DNA. Translation: EAW89244.1.
BC001420 mRNA. Translation: AAH01420.1.
BC039343 mRNA. Translation: AAH39343.1.
CCDSiCCDS32729.1. [Q9UK76-2]
CCDS45771.1. [Q9UK76-1]
CCDS45772.1. [Q9UK76-3]
RefSeqiNP_001002032.1. NM_001002032.2. [Q9UK76-2]
NP_001002033.1. NM_001002033.2. [Q9UK76-3]
NP_001275538.1. NM_001288609.1. [Q9UK76-3]
NP_001275539.1. NM_001288610.1. [Q9UK76-3]
NP_001275540.1. NM_001288611.1.
NP_057269.1. NM_016185.3. [Q9UK76-1]
UniGeneiHs.532803.

Genome annotation databases

EnsembliENST00000356033; ENSP00000348316; ENSG00000189159. [Q9UK76-2]
ENST00000409753; ENSP00000387059; ENSG00000189159. [Q9UK76-1]
ENST00000470924; ENSP00000462784; ENSG00000189159. [Q9UK76-3]
ENST00000476258; ENSP00000464266; ENSG00000189159. [Q9UK76-3]
ENST00000481647; ENSP00000462478; ENSG00000189159. [Q9UK76-3]
ENST00000482348; ENSP00000462834; ENSG00000189159. [Q9UK76-3]
GeneIDi51155.
KEGGihsa:51155.
UCSCiuc002jna.3. human. [Q9UK76-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF086910 mRNA. Translation: AAP97140.1.
AY322169 mRNA. Translation: AAP83838.1.
AY322170 mRNA. Translation: AAP83839.1.
AF348672 Genomic DNA. Translation: AAL83903.1.
AF348672 Genomic DNA. Translation: AAP83962.1.
AF348672 Genomic DNA. Translation: AAP83963.1.
AF177862 mRNA. Translation: AAD53312.1.
AF266846 mRNA. Translation: AAQ14298.1.
AF266847 Genomic DNA. Translation: AAQ14299.1.
AK223321 mRNA. Translation: BAD97041.1.
AK312613 mRNA. Translation: BAG35500.1.
CH471099 Genomic DNA. Translation: EAW89244.1.
BC001420 mRNA. Translation: AAH01420.1.
BC039343 mRNA. Translation: AAH39343.1.
CCDSiCCDS32729.1. [Q9UK76-2]
CCDS45771.1. [Q9UK76-1]
CCDS45772.1. [Q9UK76-3]
RefSeqiNP_001002032.1. NM_001002032.2. [Q9UK76-2]
NP_001002033.1. NM_001002033.2. [Q9UK76-3]
NP_001275538.1. NM_001288609.1. [Q9UK76-3]
NP_001275539.1. NM_001288610.1. [Q9UK76-3]
NP_001275540.1. NM_001288611.1.
NP_057269.1. NM_016185.3. [Q9UK76-1]
UniGeneiHs.532803.

3D structure databases

ProteinModelPortaliQ9UK76.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi119338. 14 interactions.
IntActiQ9UK76. 2 interactions.
MINTiMINT-1390948.
STRINGi9606.ENSP00000348316.

PTM databases

iPTMnetiQ9UK76.
PhosphoSiteiQ9UK76.

Proteomic databases

EPDiQ9UK76.
MaxQBiQ9UK76.
PaxDbiQ9UK76.
PRIDEiQ9UK76.
TopDownProteomicsiQ9UK76-1. [Q9UK76-1]
Q9UK76-2. [Q9UK76-2]
Q9UK76-3. [Q9UK76-3]

Protocols and materials databases

DNASUi51155.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000356033; ENSP00000348316; ENSG00000189159. [Q9UK76-2]
ENST00000409753; ENSP00000387059; ENSG00000189159. [Q9UK76-1]
ENST00000470924; ENSP00000462784; ENSG00000189159. [Q9UK76-3]
ENST00000476258; ENSP00000464266; ENSG00000189159. [Q9UK76-3]
ENST00000481647; ENSP00000462478; ENSG00000189159. [Q9UK76-3]
ENST00000482348; ENSP00000462834; ENSG00000189159. [Q9UK76-3]
GeneIDi51155.
KEGGihsa:51155.
UCSCiuc002jna.3. human. [Q9UK76-1]

Organism-specific databases

CTDi51155.
GeneCardsiHN1.
H-InvDBHIX0173715.
HGNCiHGNC:14569. HN1.
HPAiHPA059729.
neXtProtiNX_Q9UK76.
PharmGKBiPA29347.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410J50B. Eukaryota.
ENOG410YZCR. LUCA.
GeneTreeiENSGT00390000000756.
HOGENOMiHOG000231170.
HOVERGENiHBG055006.
InParanoidiQ9UK76.
OMAiCELHNLS.
PhylomeDBiQ9UK76.
TreeFamiTF327169.

Miscellaneous databases

ChiTaRSiHN1. human.
GeneWikiiHN1_(gene).
GenomeRNAii51155.
NextBioi54053.
PROiQ9UK76.

Gene expression databases

BgeeiQ9UK76.
CleanExiHS_HN1.
ExpressionAtlasiQ9UK76. baseline and differential.
GenevisibleiQ9UK76. HS.

Family and domain databases

InterProiIPR033335. JUPITER/HN1/HN1L.
[Graphical view]
PANTHERiPTHR34930. PTHR34930. 1 hit.
PfamiPF17054. JUPITER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning, expression and subcellular localization of HN1 and HN1L genes, as well as characterization of their orthologs, defining an evolutionarily conserved gene family."
    Zhou G., Wang J., Zhang Y., Zhong C., Ni J., Wang L., Guo J., Zhang K., Yu L., Zhao S.
    Gene 331:115-123(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1; 2 AND 3), TISSUE SPECIFICITY.
  2. "Cloning of human homolog of Hn1 cDNA."
    Ji Y., Huang T., Johnson B.H., Thompson E.B.
    Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: T-cell.
  3. Korkmaz K.S., Korkmaz C.G., Saatcioglu F.
    Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
    Tissue: Prostatic carcinoma.
  4. "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 1).
    Tissue: Brain.
  5. Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
    Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Thymus.
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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] (ISOFORMS 1 AND 3).
    Tissue: Placenta and Testis.
  8. "Beyond linker histones and high mobility group proteins: global profiling of perchloric acid soluble proteins."
    Zougman A., Wisniewski J.R.
    J. Proteome Res. 5:925-934(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 85-99, ACETYLATION AT THR-2, PHOSPHORYLATION AT SER-87, IDENTIFICATION BY MASS SPECTROMETRY.
  9. "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-131, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."
    Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.
    J. Proteome Res. 6:4150-4162(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-54, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Platelet.
  12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-54; SER-80 AND SER-87, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. "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].
  14. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-54; SER-87 AND SER-88, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  15. "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-148, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "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 THR-54; SER-87; SER-88 AND SER-131, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "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 SER-87, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 AND THR-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  20. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-88, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiHN1_HUMAN
AccessioniPrimary (citable) accession number: Q9UK76
Secondary accession number(s): B2R6K3
, Q53FG7, Q7Z2D2, Q7Z2F0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 24, 2006
Last sequence update: January 23, 2007
Last modified: May 11, 2016
This is version 115 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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. 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.