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Protein

Transformer-2 protein homolog alpha

Gene

TRA2A

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

Functioni

Sequence-specific RNA-binding protein which participates in the control of pre-mRNA splicing.1 Publication

GO - Molecular functioni

  • nucleotide binding Source: InterPro
  • poly(A) RNA binding Source: UniProtKB

GO - Biological processi

  • mRNA splicing, via spliceosome Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

mRNA processing, mRNA splicing

Keywords - Ligandi

RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Transformer-2 protein homolog alpha
Short name:
TRA-2 alpha
Short name:
TRA2-alpha
Alternative name(s):
Transformer-2 protein homolog A
Gene namesi
Name:TRA2A
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 7

Organism-specific databases

HGNCiHGNC:16645. TRA2A.

Subcellular locationi

  • Nucleus 1 Publication

GO - Cellular componenti

  • intracellular membrane-bounded organelle Source: HPA
  • nucleolus Source: HPA
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA164726707.

Polymorphism and mutation databases

DMDMi4033480.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 282281Transformer-2 protein homolog alphaPRO_0000081981Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineCombined sources
Modified residuei2 – 21PhosphoserineCombined sources
Modified residuei14 – 141PhosphoserineCombined sources
Modified residuei24 – 241PhosphothreonineCombined sources
Modified residuei30 – 301PhosphoserineBy similarity
Modified residuei84 – 841PhosphoserineCombined sources
Modified residuei86 – 861PhosphoserineCombined sources
Modified residuei88 – 881PhosphothreonineCombined sources
Modified residuei96 – 961PhosphoserineCombined sources
Modified residuei98 – 981PhosphoserineCombined sources
Modified residuei100 – 1001PhosphoserineBy similarity
Modified residuei202 – 2021PhosphothreonineCombined sources
Modified residuei204 – 2041PhosphothreonineCombined sources
Modified residuei255 – 2551Dimethylated arginineBy similarity

Post-translational modificationi

Phosphorylated in the RS domains.1 Publication

Keywords - PTMi

Acetylation, Methylation, Phosphoprotein

Proteomic databases

EPDiQ13595.
PaxDbiQ13595.
PRIDEiQ13595.

PTM databases

iPTMnetiQ13595.
PhosphoSiteiQ13595.

Expressioni

Gene expression databases

BgeeiQ13595.
ExpressionAtlasiQ13595. baseline and differential.
GenevisibleiQ13595. HS.

Organism-specific databases

HPAiHPA054018.

Interactioni

Subunit structurei

Binds to A3 enhancer proteins SRp75, SRp55, SRp40 and SRp30.

Protein-protein interaction databases

BioGridi118948. 152 interactions.
IntActiQ13595. 28 interactions.
MINTiMINT-1683046.
STRINGi9606.ENSP00000297071.

Structurei

3D structure databases

ProteinModelPortaliQ13595.
SMRiQ13595. Positions 110-202.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini119 – 19779RRMPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni198 – 22528LinkerAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi30 – 11283Arg/Ser-rich (RS1 domain)Add
BLAST
Compositional biasi226 – 28257Arg/Ser-rich (RS2 domain)Add
BLAST

Sequence similaritiesi

Belongs to the splicing factor SR family.Curated
Contains 1 RRM (RNA recognition motif) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG410IQWZ. Eukaryota.
ENOG4111HSX. LUCA.
GeneTreeiENSGT00710000106295.
HOGENOMiHOG000276232.
HOVERGENiHBG102125.
InParanoidiQ13595.
KOiK12897.
OMAiSKQSESH.
OrthoDBiEOG7SFHZZ.
PhylomeDBiQ13595.
TreeFamiTF106265.

Family and domain databases

Gene3Di3.30.70.330. 1 hit.
InterProiIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PfamiPF00076. RRM_1. 1 hit.
[Graphical view]
SMARTiSM00360. RRM. 1 hit.
[Graphical view]
SUPFAMiSSF54928. SSF54928. 1 hit.
PROSITEiPS50102. RRM. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

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

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform Long (identifier: Q13595-1) [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
MSDVEENNFE GRESRSQSKS PTGTPARVKS ESRSGSRSPS RVSKHSESHS
60 70 80 90 100
RSRSKSRSRS RRHSHRRYTR SRSHSHSHRR RSRSRSYTPE YRRRRSRSHS
110 120 130 140 150
PMSNRRRHTG SRANPDPNTC LGVFGLSLYT TERDLREVFS RYGPLSGVNV
160 170 180 190 200
VYDQRTGRSR GFAFVYFERI DDSKEAMERA NGMELDGRRI RVDYSITKRA
210 220 230 240 250
HTPTPGIYMG RPTHSGGGGG GGGGGGGGGG GRRRDSYYDR GYDRGYDRYE
260 270 280
DYDYRYRRRS PSPYYSRYRS RSRSRSYSPR RY
Length:282
Mass (Da):32,689
Last modified:November 1, 1996 - v1
Checksum:iEDB5ABE7BEA023FD
GO
Isoform Short (identifier: Q13595-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-101: Missing.
     214-214: H → Q
     215-282: Missing.

Show »
Length:113
Mass (Da):12,952
Checksum:iD7E4DDF02E52CEA0
GO
Isoform 3 (identifier: Q13595-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-101: Missing.

Note: No experimental confirmation available.
Show »
Length:181
Mass (Da):20,746
Checksum:i440524DD6FEC3910
GO
Isoform 4 (identifier: Q13595-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-101: Missing.
     257-257: Missing.

Note: No experimental confirmation available.
Show »
Length:180
Mass (Da):20,590
Checksum:i792DF54BE964E333
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 101101Missing in isoform Short, isoform 3 and isoform 4. 2 PublicationsVSP_005893Add
BLAST
Alternative sequencei214 – 2141H → Q in isoform Short. 1 PublicationVSP_005894
Alternative sequencei215 – 28268Missing in isoform Short. 1 PublicationVSP_005895Add
BLAST
Alternative sequencei257 – 2571Missing in isoform 4. 1 PublicationVSP_057405

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U53209 mRNA. Translation: AAC50658.1.
AK298815 mRNA. Translation: BAG60948.1.
AK300565 mRNA. Translation: BAG62271.1.
AK300741 mRNA. Translation: BAG62410.1.
AC023105 Genomic DNA. No translation available.
BC017094 mRNA. Translation: AAH17094.1.
CCDSiCCDS5383.1. [Q13595-1]
CCDS64609.1. [Q13595-3]
CCDS75569.1. [Q13595-4]
RefSeqiNP_001269686.1. NM_001282757.1. [Q13595-3]
NP_001269687.1. NM_001282758.1. [Q13595-3]
NP_001269688.1. NM_001282759.1. [Q13595-4]
NP_037425.1. NM_013293.4. [Q13595-1]
XP_005249782.1. XM_005249725.1. [Q13595-3]
XP_006715776.1. XM_006715713.1. [Q13595-3]
UniGeneiHs.445652.

Genome annotation databases

EnsembliENST00000297071; ENSP00000297071; ENSG00000164548. [Q13595-1]
ENST00000392502; ENSP00000376290; ENSG00000164548. [Q13595-4]
ENST00000538367; ENSP00000441116; ENSG00000164548. [Q13595-3]
ENST00000621813; ENSP00000480822; ENSG00000164548. [Q13595-3]
GeneIDi29896.
KEGGihsa:29896.
UCSCiuc011jzb.4. human.
uc011jzc.5. human. [Q13595-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U53209 mRNA. Translation: AAC50658.1.
AK298815 mRNA. Translation: BAG60948.1.
AK300565 mRNA. Translation: BAG62271.1.
AK300741 mRNA. Translation: BAG62410.1.
AC023105 Genomic DNA. No translation available.
BC017094 mRNA. Translation: AAH17094.1.
CCDSiCCDS5383.1. [Q13595-1]
CCDS64609.1. [Q13595-3]
CCDS75569.1. [Q13595-4]
RefSeqiNP_001269686.1. NM_001282757.1. [Q13595-3]
NP_001269687.1. NM_001282758.1. [Q13595-3]
NP_001269688.1. NM_001282759.1. [Q13595-4]
NP_037425.1. NM_013293.4. [Q13595-1]
XP_005249782.1. XM_005249725.1. [Q13595-3]
XP_006715776.1. XM_006715713.1. [Q13595-3]
UniGeneiHs.445652.

3D structure databases

ProteinModelPortaliQ13595.
SMRiQ13595. Positions 110-202.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi118948. 152 interactions.
IntActiQ13595. 28 interactions.
MINTiMINT-1683046.
STRINGi9606.ENSP00000297071.

PTM databases

iPTMnetiQ13595.
PhosphoSiteiQ13595.

Polymorphism and mutation databases

DMDMi4033480.

Proteomic databases

EPDiQ13595.
PaxDbiQ13595.
PRIDEiQ13595.

Protocols and materials databases

DNASUi29896.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000297071; ENSP00000297071; ENSG00000164548. [Q13595-1]
ENST00000392502; ENSP00000376290; ENSG00000164548. [Q13595-4]
ENST00000538367; ENSP00000441116; ENSG00000164548. [Q13595-3]
ENST00000621813; ENSP00000480822; ENSG00000164548. [Q13595-3]
GeneIDi29896.
KEGGihsa:29896.
UCSCiuc011jzb.4. human.
uc011jzc.5. human. [Q13595-1]

Organism-specific databases

CTDi29896.
GeneCardsiTRA2A.
HGNCiHGNC:16645. TRA2A.
HPAiHPA054018.
MIMi602718. gene.
neXtProtiNX_Q13595.
PharmGKBiPA164726707.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IQWZ. Eukaryota.
ENOG4111HSX. LUCA.
GeneTreeiENSGT00710000106295.
HOGENOMiHOG000276232.
HOVERGENiHBG102125.
InParanoidiQ13595.
KOiK12897.
OMAiSKQSESH.
OrthoDBiEOG7SFHZZ.
PhylomeDBiQ13595.
TreeFamiTF106265.

Miscellaneous databases

ChiTaRSiTRA2A. human.
GeneWikiiTRA2A.
GenomeRNAii29896.
NextBioi35474147.
PROiQ13595.
SOURCEiSearch...

Gene expression databases

BgeeiQ13595.
ExpressionAtlasiQ13595. baseline and differential.
GenevisibleiQ13595. HS.

Family and domain databases

Gene3Di3.30.70.330. 1 hit.
InterProiIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PfamiPF00076. RRM_1. 1 hit.
[Graphical view]
SMARTiSM00360. RRM. 1 hit.
[Graphical view]
SUPFAMiSSF54928. SSF54928. 1 hit.
PROSITEiPS50102. RRM. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A human homologue of the Drosophila sex determination factor transformer-2 has conserved splicing regulatory functions."
    Dauwalder B., Amaya-Manzanares F., Mattox W.
    Proc. Natl. Acad. Sci. U.S.A. 93:9004-9009(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS LONG AND SHORT).
  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] (ISOFORMS 3 AND 4).
    Tissue: Prostate.
  3. "The DNA sequence of human chromosome 7."
    Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
    , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
    Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
    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].
    Tissue: Uterus.
  5. "Human Tra2 proteins are sequence-specific activators of pre-mRNA splicing."
    Tacke R., Tohyama M., Ogawa S., Manley J.L.
    Cell 93:139-148(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION.
    Tissue: Cervix carcinoma.
  6. "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-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-84; SER-86; THR-88; THR-202 AND THR-204, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2; SER-14; THR-202 AND THR-204, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2; SER-14; THR-24; SER-84; SER-86; THR-88; SER-96; SER-98 AND THR-204, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiTRA2A_HUMAN
AccessioniPrimary (citable) accession number: Q13595
Secondary accession number(s): B4DQI6, B4DUA9, E9PD75
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: November 1, 1996
Last modified: May 11, 2016
This is version 159 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 7
    Human chromosome 7: 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

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.