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Protein

TBC1 domain family member 9B

Gene

TBC1D9B

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

Functioni

May act as a GTPase-activating protein for Rab family protein(s).

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei555 – 5551Arginine fingerBy similarity
Sitei594 – 5941Glutamine fingerBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

GTPase activation

Names & Taxonomyi

Protein namesi
Recommended name:
TBC1 domain family member 9B
Gene namesi
Name:TBC1D9B
Synonyms:KIAA0676
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 5

Organism-specific databases

HGNCiHGNC:29097. TBC1D9B.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei668 – 68821HelicalSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA145148062.

Polymorphism and mutation databases

BioMutaiTBC1D9B.
DMDMi296452939.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 12501250TBC1 domain family member 9BPRO_0000288501Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei397 – 3971PhosphothreonineCombined sources
Modified residuei411 – 4111PhosphoserineCombined sources
Modified residuei432 – 4321PhosphoserineCombined sources
Modified residuei435 – 4351PhosphoserineCombined sources
Modified residuei463 – 4631PhosphoserineCombined sources
Modified residuei1241 – 12411PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ66K14.
MaxQBiQ66K14.
PaxDbiQ66K14.
PeptideAtlasiQ66K14.
PRIDEiQ66K14.

PTM databases

iPTMnetiQ66K14.
PhosphoSiteiQ66K14.

Expressioni

Gene expression databases

BgeeiQ66K14.
CleanExiHS_TBC1D9B.
ExpressionAtlasiQ66K14. baseline and differential.
GenevisibleiQ66K14. HS.

Organism-specific databases

HPAiHPA038350.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
GABARAPL2P605203EBI-10217736,EBI-720116
L3MBTL2Q969R53EBI-10217736,EBI-739909

GO - Molecular functioni

Protein-protein interaction databases

BioGridi116696. 27 interactions.
IntActiQ66K14. 8 interactions.
STRINGi9606.ENSP00000349291.

Structurei

3D structure databases

ProteinModelPortaliQ66K14.
SMRiQ66K14. Positions 500-724, 859-926.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini142 – 20968GRAM 1Add
BLAST
Domaini288 – 35669GRAM 2Add
BLAST
Domaini508 – 695188Rab-GAP TBCPROSITE-ProRule annotationAdd
BLAST
Domaini879 – 91436EF-handPROSITE-ProRule annotationAdd
BLAST

Domaini

The arginine and glutamine fingers are critical for the GTPase-activating mechanism, they pull out Rab's 'switch 2' glutamine and insert in Rab's active site.By similarity

Sequence similaritiesi

Contains 1 EF-hand domain.PROSITE-ProRule annotation
Contains 2 GRAM domains.Curated
Contains 1 Rab-GAP TBC domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG4347. Eukaryota.
COG5210. LUCA.
GeneTreeiENSGT00760000119137.
HOVERGENiHBG054142.
InParanoidiQ66K14.
KOiK19951.
OMAiEGEAMTI.
OrthoDBiEOG7ZWD0Z.
PhylomeDBiQ66K14.
TreeFamiTF313145.

Family and domain databases

Gene3Di1.10.238.10. 1 hit.
InterProiIPR011992. EF-hand-dom_pair.
IPR002048. EF_hand_dom.
IPR004182. GRAM.
IPR000195. Rab-GTPase-TBC_dom.
[Graphical view]
PfamiPF02893. GRAM. 2 hits.
PF00566. RabGAP-TBC. 1 hit.
[Graphical view]
SMARTiSM00568. GRAM. 2 hits.
SM00164. TBC. 1 hit.
[Graphical view]
SUPFAMiSSF47473. SSF47473. 1 hit.
SSF47923. SSF47923. 2 hits.
PROSITEiPS50222. EF_HAND_2. 1 hit.
PS50086. TBC_RABGAP. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q66K14-1) [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
MWLSPEEVLV ANALWVTERA NPFFVLQRRR GHGRGGGLTG LLVGTLDVVL
60 70 80 90 100
DSSARVAPYR ILHQTQDSQV YWTVACGSSR KEITKHWEWL ENNLLQTLSI
110 120 130 140 150
FDSEEDITTF VKGKIHGIIA EENKNLQPQG DEDPGKFKEA ELKMRKQFGM
160 170 180 190 200
PEGEKLVNYY SCSYWKGRVP RQGWLYLTVN HLCFYSFLLG KEVSLVVQWV
210 220 230 240 250
DITRLEKNAT LLFPESIRVD TRDQELFFSM FLNIGETFKL MEQLANLAMR
260 270 280 290 300
QLLDSEGFLE DKALPRPIRP HRNISALKRD LDARAKNECY RATFRLPRDE
310 320 330 340 350
RLDGHTSCTL WTPFNKLHIP GQMFISNNYI CFASKEEDAC HLIIPLREVT
360 370 380 390 400
IVEKADSSSV LPSPLSISTK SKMTFLFANL KDRDFLVQRI SDFLQKTPSK
410 420 430 440 450
QPGSIGSRKA SVVDPSTESS PAPQEGSEQP ASPASPLSSR QSFCAQEAPT
460 470 480 490 500
ASQGLLKLFQ KNSPMEDLGA KGAKEKMKEE SWHIHFFEYG RGVCMYRTAK
510 520 530 540 550
TRALVLKGIP ESLRGELWLL FSGAWNEMVT HPGYYAELVE KSTGKYSLAT
560 570 580 590 600
EEIERDLHRS MPEHPAFQNE LGIAALRRVL TAYAFRNPTI GYCQAMNIVT
610 620 630 640 650
SVLLLYGSEE EAFWLLVALC ERMLPDYYNT RVVGALVDQG IFEELTRDFL
660 670 680 690 700
PQLSEKMQDL GVISSISLSW FLTLFLSVMP FESAVVIVDC FFYEGIKVIL
710 720 730 740 750
QVALAVLDAN MEQLLGCSDE GEAMTMLGRY LDNVVNKQSV SPPIPHLRAL
760 770 780 790 800
LSSSDDPPAE VDIFELLKVS YEKFSSLRAE DIEQMRFKQR LKVIQSLEDT
810 820 830 840 850
AKRSVVRAIP VDIGFSIEEL EDLYMVFKAK HLASQYWGCS RTMAGRRDPS
860 870 880 890 900
LPYLEQYRID ASQFRELFAS LTPWACGSHT PLLAGRMFRL LDENKDSLIN
910 920 930 940 950
FKEFVTGMSG MYHGDLTEKL KVLYKLHLPP ALSPEEAESA LEAAHYFTED
960 970 980 990 1000
SSSEASPLAS DLDLFLPWEA QEALPQEEQE GSGSEERGEE KGTSSPDYRH
1010 1020 1030 1040 1050
YLRMWAKEKE AQKETIKDLP KMNQEQFIEL CKTLYNMFSE DPMEQDLYHA
1060 1070 1080 1090 1100
IATVASLLLR IGEVGKKFSA RTGRKPRDCA TEEDEPPAPE LHQDAARELQ
1110 1120 1130 1140 1150
PPAAGDPQAK AGGDTHLGKA PQESQVVVEG GSGEGQGSPS QLLSDDETKD
1160 1170 1180 1190 1200
DMSMSSYSVV STGSLQCEDL ADDTVLVGGE ACSPTARIGG TVDTDWCISF
1210 1220 1230 1240 1250
EQILASILTE SVLVNFFEKR VDIGLKIKDQ KKVERQFSTA SDHEQPGVSG
Length:1,250
Mass (Da):140,525
Last modified:May 18, 2010 - v3
Checksum:i35D9E4914B1D8311
GO
Isoform 2 (identifier: Q66K14-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     955-971: Missing.

Show »
Length:1,233
Mass (Da):138,670
Checksum:i0CF4629B30598F6A
GO

Sequence cautioni

The sequence AAH08919.3 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti893 – 8931E → G in BAD97229 (Ref. 5) Curated
Sequence conflicti1231 – 12311K → R in CAE46050 (PubMed:17974005).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti240 – 2401L → P.
Corresponds to variant rs1057078 [ dbSNP | Ensembl ].
VAR_032440
Natural varianti706 – 7061V → I.
Corresponds to variant rs10037618 [ dbSNP | Ensembl ].
VAR_032441
Natural varianti1086 – 10861P → Q in a breast cancer sample; somatic mutation. 1 Publication
VAR_036196
Natural varianti1119 – 11191K → T.4 Publications
Corresponds to variant rs30386 [ dbSNP | Ensembl ].
VAR_032442

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei955 – 97117Missing in isoform 2. 2 PublicationsVSP_025699Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB014576 mRNA. Translation: BAA31651.1.
AC008393 Genomic DNA. No translation available.
AC010285 Genomic DNA. No translation available.
CH471165 Genomic DNA. Translation: EAW53780.1.
CH471165 Genomic DNA. Translation: EAW53782.1.
CH471165 Genomic DNA. Translation: EAW53777.1.
CH471165 Genomic DNA. Translation: EAW53779.1.
BC008919 mRNA. Translation: AAH08919.3. Different initiation.
BC080659 mRNA. Translation: AAH80659.1.
AK223509 mRNA. Translation: BAD97229.1.
BX641107 mRNA. Translation: CAE46050.1.
CCDSiCCDS43408.1. [Q66K14-1]
CCDS4450.1. [Q66K14-2]
RefSeqiNP_055858.2. NM_015043.3. [Q66K14-2]
NP_942568.2. NM_198868.2. [Q66K14-1]
UniGeneiHs.155829.

Genome annotation databases

EnsembliENST00000355235; ENSP00000347375; ENSG00000197226. [Q66K14-2]
ENST00000356834; ENSP00000349291; ENSG00000197226. [Q66K14-1]
GeneIDi23061.
KEGGihsa:23061.
UCSCiuc003mlh.4. human. [Q66K14-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB014576 mRNA. Translation: BAA31651.1.
AC008393 Genomic DNA. No translation available.
AC010285 Genomic DNA. No translation available.
CH471165 Genomic DNA. Translation: EAW53780.1.
CH471165 Genomic DNA. Translation: EAW53782.1.
CH471165 Genomic DNA. Translation: EAW53777.1.
CH471165 Genomic DNA. Translation: EAW53779.1.
BC008919 mRNA. Translation: AAH08919.3. Different initiation.
BC080659 mRNA. Translation: AAH80659.1.
AK223509 mRNA. Translation: BAD97229.1.
BX641107 mRNA. Translation: CAE46050.1.
CCDSiCCDS43408.1. [Q66K14-1]
CCDS4450.1. [Q66K14-2]
RefSeqiNP_055858.2. NM_015043.3. [Q66K14-2]
NP_942568.2. NM_198868.2. [Q66K14-1]
UniGeneiHs.155829.

3D structure databases

ProteinModelPortaliQ66K14.
SMRiQ66K14. Positions 500-724, 859-926.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116696. 27 interactions.
IntActiQ66K14. 8 interactions.
STRINGi9606.ENSP00000349291.

PTM databases

iPTMnetiQ66K14.
PhosphoSiteiQ66K14.

Polymorphism and mutation databases

BioMutaiTBC1D9B.
DMDMi296452939.

Proteomic databases

EPDiQ66K14.
MaxQBiQ66K14.
PaxDbiQ66K14.
PeptideAtlasiQ66K14.
PRIDEiQ66K14.

Protocols and materials databases

DNASUi23061.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000355235; ENSP00000347375; ENSG00000197226. [Q66K14-2]
ENST00000356834; ENSP00000349291; ENSG00000197226. [Q66K14-1]
GeneIDi23061.
KEGGihsa:23061.
UCSCiuc003mlh.4. human. [Q66K14-1]

Organism-specific databases

CTDi23061.
GeneCardsiTBC1D9B.
HGNCiHGNC:29097. TBC1D9B.
HPAiHPA038350.
neXtProtiNX_Q66K14.
PharmGKBiPA145148062.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4347. Eukaryota.
COG5210. LUCA.
GeneTreeiENSGT00760000119137.
HOVERGENiHBG054142.
InParanoidiQ66K14.
KOiK19951.
OMAiEGEAMTI.
OrthoDBiEOG7ZWD0Z.
PhylomeDBiQ66K14.
TreeFamiTF313145.

Miscellaneous databases

ChiTaRSiTBC1D9B. human.
GenomeRNAii23061.
PROiQ66K14.

Gene expression databases

BgeeiQ66K14.
CleanExiHS_TBC1D9B.
ExpressionAtlasiQ66K14. baseline and differential.
GenevisibleiQ66K14. HS.

Family and domain databases

Gene3Di1.10.238.10. 1 hit.
InterProiIPR011992. EF-hand-dom_pair.
IPR002048. EF_hand_dom.
IPR004182. GRAM.
IPR000195. Rab-GTPase-TBC_dom.
[Graphical view]
PfamiPF02893. GRAM. 2 hits.
PF00566. RabGAP-TBC. 1 hit.
[Graphical view]
SMARTiSM00568. GRAM. 2 hits.
SM00164. TBC. 1 hit.
[Graphical view]
SUPFAMiSSF47473. SSF47473. 1 hit.
SSF47923. SSF47923. 2 hits.
PROSITEiPS50222. EF_HAND_2. 1 hit.
PS50086. TBC_RABGAP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Prediction of the coding sequences of unidentified human genes. X. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro."
    Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
    DNA Res. 5:169-176(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT THR-1119.
    Tissue: Brain.
  2. "The DNA sequence and comparative analysis of human chromosome 5."
    Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.
    , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
    Nature 431:268-274(2004) [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] OF 635-1250 (ISOFORM 2), VARIANT THR-1119.
    Tissue: Brain and Skin.
  5. 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] OF 805-1250 (ISOFORM 2), VARIANT THR-1119.
    Tissue: Colon.
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1004-1250, VARIANT THR-1119.
    Tissue: Uterus.
  7. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-432 AND SER-435, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-411; SER-432 AND SER-435, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "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].
  10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-435, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "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 SER-411; SER-432 AND SER-435, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  12. "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-432 AND SER-463, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "Toward a comprehensive characterization of a human cancer cell phosphoproteome."
    Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S.
    J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-397; SER-435 AND SER-463, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma and Erythroleukemia.
  15. "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-411 AND SER-1241, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  16. Cited for: VARIANT [LARGE SCALE ANALYSIS] GLN-1086.

Entry informationi

Entry nameiTBC9B_HUMAN
AccessioniPrimary (citable) accession number: Q66K14
Secondary accession number(s): D3DWQ5
, D3DWQ6, O75163, Q53EY0, Q6MZI2, Q96H49
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 29, 2007
Last sequence update: May 18, 2010
Last modified: July 6, 2016
This is version 106 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, Reference proteome

Documents

  1. Human chromosome 5
    Human chromosome 5: 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. 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.