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Protein

TBC1 domain family member 22B

Gene

TBC1D22B

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).By similarity

GO - Molecular functioni

  • 14-3-3 protein binding Source: UniProtKB
  • GTPase activator activity Source: GO_Central
  • Rab GTPase binding Source: GO_Central

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

GTPase activation

Names & Taxonomyi

Protein namesi
Recommended name:
TBC1 domain family member 22B
Gene namesi
Name:TBC1D22B
Synonyms:C6orf197
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 6

Organism-specific databases

HGNCiHGNC:21602. TBC1D22B.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi58 – 581S → E: No effect on ACBD3-binding. 1 Publication
Mutagenesisi88 – 903LNS → AAA: No effect on ACBD3-binding. 1 Publication
Mutagenesisi91 – 922KV → AA: No effect on ACBD3-binding. 1 Publication
Mutagenesisi94 – 963LAT → AAA: No effect on ACBD3-binding. 1 Publication
Mutagenesisi99 – 991Q → A: No effect on ACBD3-binding. 1 Publication
Mutagenesisi100 – 1012VL → AA: Almost complete loss of ACBD3-binding. 1 Publication
Mutagenesisi102 – 1043ENH → AAA: No effect on ACBD3-binding. 1 Publication
Mutagenesisi114 – 1141S → E: No effect on ACBD3-binding. 1 Publication
Mutagenesisi116 – 1194STTS → EEEE: No effect on ACBD3-binding. 1 Publication
Mutagenesisi140 – 1412SS → EE: No effect on ACBD3-binding. 1 Publication
Mutagenesisi143 – 1431T → E: No effect on ACBD3-binding. 1 Publication
Mutagenesisi168 – 1681S → E: No effect on ACBD3-binding. 1 Publication

Organism-specific databases

PharmGKBiPA134867087.

Polymorphism and mutation databases

BioMutaiTBC1D22B.
DMDMi47117913.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 505504TBC1 domain family member 22BPRO_0000208054Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Modified residuei58 – 581PhosphoserineCombined sources
Modified residuei116 – 1161PhosphoserineCombined sources
Modified residuei154 – 1541PhosphoserineCombined sources1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ9NU19.
MaxQBiQ9NU19.
PaxDbiQ9NU19.
PeptideAtlasiQ9NU19.
PRIDEiQ9NU19.

PTM databases

iPTMnetiQ9NU19.
PhosphoSiteiQ9NU19.

Expressioni

Gene expression databases

BgeeiQ9NU19.
CleanExiHS_TBC1D22B.
GenevisibleiQ9NU19. HS.

Organism-specific databases

HPAiHPA027908.
HPA027909.
HPA027910.

Interactioni

Subunit structurei

Interacts with ACBD3 and ARFGEF1. Interacts with YWHAB, YWHAE, YWHAG, YWHAH, YWHAQ and YWHAZ.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
CALCOCO2Q131373EBI-8787464,EBI-739580
CCDC57Q2TAC23EBI-8787464,EBI-2808286
CCDC67E9PJR53EBI-8787464,EBI-10177066
CDR2Q018503EBI-8787464,EBI-1181367
FXR2P511163EBI-8787464,EBI-740459
HSD17B14Q9BPX13EBI-8787464,EBI-742664
IKZF3Q9UKT93EBI-8787464,EBI-747204
KRT40Q6A1623EBI-8787464,EBI-10171697
PNMA5Q96PV43EBI-8787464,EBI-10171633
RBM10P981753EBI-8787464,EBI-721525
SIAH1Q8IUQ43EBI-8787464,EBI-747107
SORBS3O605043EBI-8787464,EBI-741237
TACC3Q9Y6A53EBI-8787464,EBI-2554984
TEX11Q8IYF33EBI-8787464,EBI-742397
TP53BP2Q13625-33EBI-8787464,EBI-10175039
TRIM23P364063EBI-8787464,EBI-740098
TRIM27P143733EBI-8787464,EBI-719493
TRIM54Q9BYV23EBI-8787464,EBI-2130429
VPS52Q8N1B43EBI-8787464,EBI-2799833

GO - Molecular functioni

  • 14-3-3 protein binding Source: UniProtKB
  • Rab GTPase binding Source: GO_Central

Protein-protein interaction databases

BioGridi120772. 102 interactions.
IntActiQ9NU19. 23 interactions.
STRINGi9606.ENSP00000362590.

Structurei

Secondary structure

1
505
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi185 – 1939Combined sources
Beta strandi195 – 1973Combined sources
Helixi200 – 2078Combined sources
Helixi213 – 2153Combined sources
Helixi216 – 2238Combined sources
Helixi238 – 25215Combined sources
Helixi285 – 30016Combined sources
Helixi313 – 3153Combined sources
Helixi316 – 32611Combined sources
Helixi331 – 3333Combined sources
Helixi336 – 3383Combined sources
Helixi341 – 36020Combined sources
Helixi361 – 3655Combined sources
Helixi371 – 38717Combined sources
Helixi389 – 3979Combined sources
Helixi403 – 4119Combined sources
Turni412 – 4143Combined sources
Helixi415 – 4173Combined sources
Helixi420 – 43213Combined sources
Helixi439 – 45113Combined sources
Helixi453 – 4575Combined sources
Helixi462 – 4709Combined sources
Helixi479 – 49618Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3DZXX-ray2.30A178-505[»]
ProteinModelPortaliQ9NU19.
SMRiQ9NU19. Positions 184-500.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9NU19.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini210 – 434225Rab-GAP TBCPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 Rab-GAP TBC domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG1092. Eukaryota.
ENOG410XQ68. LUCA.
GeneTreeiENSGT00840000129806.
HOVERGENiHBG057030.
InParanoidiQ9NU19.
OMAiIREIPFN.
OrthoDBiEOG7HHWSK.
PhylomeDBiQ9NU19.
TreeFamiTF314211.

Family and domain databases

InterProiIPR000195. Rab-GTPase-TBC_dom.
[Graphical view]
PfamiPF00566. RabGAP-TBC. 1 hit.
[Graphical view]
SMARTiSM00164. TBC. 1 hit.
[Graphical view]
SUPFAMiSSF47923. SSF47923. 2 hits.
PROSITEiPS50086. TBC_RABGAP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q9NU19-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAENSKQFW KRSAKLPGSI QPVYGAQHPP LDPRLTKNFI KERSKVNTVP
60 70 80 90 100
LKNKKASSFH EFARNTSDAW DIGDDEEEDF SSPSFQTLNS KVALATAAQV
110 120 130 140 150
LENHSKLRVK PERSQSTTSD VPANYKVIKS SSDAQLSRNS SDTCLRNPLH
160 170 180 190 200
KQQSLPLRPI IPLVARISDQ NASGAPPMTV REKTRLEKFR QLLSSQNTDL
210 220 230 240 250
DELRKCSWPG VPREVRPITW RLLSGYLPAN TERRKLTLQR KREEYFGFIE
260 270 280 290 300
QYYDSRNEEH HQDTYRQIHI DIPRTNPLIP LFQQPLVQEI FERILFIWAI
310 320 330 340 350
RHPASGYVQG INDLVTPFFV VFLSEYVEED VENFDVTNLS QDMLRSIEAD
360 370 380 390 400
SFWCMSKLLD GIQDNYTFAQ PGIQKKVKAL EELVSRIDEQ VHNHFRRYEV
410 420 430 440 450
EYLQFAFRWM NNLLMRELPL RCTIRLWDTY QSEPEGFSHF HLYVCAAFLI
460 470 480 490 500
KWRKEILDEE DFQGLLMLLQ NLPTIHWGNE EIGLLLAEAY RLKYMFADAP

NHYRR
Length:505
Mass (Da):59,081
Last modified:May 10, 2004 - v3
Checksum:iC0093770BE04AA4D
GO

Sequence cautioni

The sequence BAA91099.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti376 – 3783KVK → HEE in AAH00291 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB449909 mRNA. Translation: BAH16652.1.
AY313781 mRNA. Translation: AAQ72548.1.
AK000344 mRNA. Translation: BAA91099.1. Different initiation.
AK292893 mRNA. Translation: BAF85582.1.
AL096712, AL353579, AL589667 Genomic DNA. Translation: CAI22620.1.
AL353579, AL096712, AL589667 Genomic DNA. Translation: CAI20318.1.
AL589667, AL096712, AL353579 Genomic DNA. Translation: CAH71194.1.
CH471081 Genomic DNA. Translation: EAX03939.1.
BC000291 mRNA. Translation: AAH00291.2.
BC000743 mRNA. Translation: AAH00743.2.
BC001927 mRNA. Translation: AAH01927.1.
BC002720 mRNA. Translation: AAH02720.2.
BC063523 mRNA. Translation: AAH63523.1.
BC109026 mRNA. Translation: AAI09027.1.
BC109027 mRNA. Translation: AAI09028.1.
CCDSiCCDS4832.1.
RefSeqiNP_060242.2. NM_017772.3.
UniGeneiHs.731702.

Genome annotation databases

EnsembliENST00000373491; ENSP00000362590; ENSG00000065491.
GeneIDi55633.
KEGGihsa:55633.
UCSCiuc003onn.3. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB449909 mRNA. Translation: BAH16652.1.
AY313781 mRNA. Translation: AAQ72548.1.
AK000344 mRNA. Translation: BAA91099.1. Different initiation.
AK292893 mRNA. Translation: BAF85582.1.
AL096712, AL353579, AL589667 Genomic DNA. Translation: CAI22620.1.
AL353579, AL096712, AL589667 Genomic DNA. Translation: CAI20318.1.
AL589667, AL096712, AL353579 Genomic DNA. Translation: CAH71194.1.
CH471081 Genomic DNA. Translation: EAX03939.1.
BC000291 mRNA. Translation: AAH00291.2.
BC000743 mRNA. Translation: AAH00743.2.
BC001927 mRNA. Translation: AAH01927.1.
BC002720 mRNA. Translation: AAH02720.2.
BC063523 mRNA. Translation: AAH63523.1.
BC109026 mRNA. Translation: AAI09027.1.
BC109027 mRNA. Translation: AAI09028.1.
CCDSiCCDS4832.1.
RefSeqiNP_060242.2. NM_017772.3.
UniGeneiHs.731702.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3DZXX-ray2.30A178-505[»]
ProteinModelPortaliQ9NU19.
SMRiQ9NU19. Positions 184-500.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi120772. 102 interactions.
IntActiQ9NU19. 23 interactions.
STRINGi9606.ENSP00000362590.

PTM databases

iPTMnetiQ9NU19.
PhosphoSiteiQ9NU19.

Polymorphism and mutation databases

BioMutaiTBC1D22B.
DMDMi47117913.

Proteomic databases

EPDiQ9NU19.
MaxQBiQ9NU19.
PaxDbiQ9NU19.
PeptideAtlasiQ9NU19.
PRIDEiQ9NU19.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000373491; ENSP00000362590; ENSG00000065491.
GeneIDi55633.
KEGGihsa:55633.
UCSCiuc003onn.3. human.

Organism-specific databases

CTDi55633.
GeneCardsiTBC1D22B.
HGNCiHGNC:21602. TBC1D22B.
HPAiHPA027908.
HPA027909.
HPA027910.
MIMi616880. gene.
neXtProtiNX_Q9NU19.
PharmGKBiPA134867087.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1092. Eukaryota.
ENOG410XQ68. LUCA.
GeneTreeiENSGT00840000129806.
HOVERGENiHBG057030.
InParanoidiQ9NU19.
OMAiIREIPFN.
OrthoDBiEOG7HHWSK.
PhylomeDBiQ9NU19.
TreeFamiTF314211.

Miscellaneous databases

EvolutionaryTraceiQ9NU19.
GenomeRNAii55633.
PROiQ9NU19.
SOURCEiSearch...

Gene expression databases

BgeeiQ9NU19.
CleanExiHS_TBC1D22B.
GenevisibleiQ9NU19. HS.

Family and domain databases

InterProiIPR000195. Rab-GTPase-TBC_dom.
[Graphical view]
PfamiPF00566. RabGAP-TBC. 1 hit.
[Graphical view]
SMARTiSM00164. TBC. 1 hit.
[Graphical view]
SUPFAMiSSF47923. SSF47923. 2 hits.
PROSITEiPS50086. TBC_RABGAP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification and characterization of a novel Tre-2/Bub2/Cdc16 (TBC) protein that possesses Rab3A-GAP activity."
    Ishibashi K., Kanno E., Itoh T., Fukuda M.
    Genes Cells 14:41-52(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain.
  2. Shan Y.X., Huang C.Q., Guo Z.K., Ye M.G., Yu L.
    Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  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].
    Tissue: Trachea.
  4. "The DNA sequence and analysis of human chromosome 6."
    Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
    Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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: Bone, Lung and Uterus.
  7. "ACBD3 interaction with TBC1 domain 22 protein is differentially affected by enteroviral and kobuviral 3A protein binding."
    Greninger A.L., Knudsen G.M., Betegon M., Burlingame A.L., DeRisi J.L.
    MBio 4:E00098-E00098(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-293; 346-421 AND 454-505, CLEAVAGE OF INITATOR METHIONINE, ACETYLATION AT ALA-2, PHOSPHORYLATION AT SER-154, INTERACTION WITH ACBD3; ARFGEF1; YWHAB; YWHAE; YWHAG; YWHAH; YWHAQ AND YWHAZ, MUTAGENESIS OF SER-58; 88-LEU--SER-90; 91-LYS-VAL-92; 94-LEU--THR-96; GLN-99; 100-VAL-LEU-101; 102-GLU--HIS-104; SER-114; 116-SER--SER-119; 140-SER-SER-141; THR-143 AND SER-168, MASS SPECTROMETRY.
  8. "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.
  9. "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 SER-58; SER-116 AND SER-154, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma and Erythroleukemia.
  10. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  11. "Crystal structure of the RabGAP domain of human TBC1D22B."
    Structural genomics consortium (SGC)
    Submitted (FEB-2009) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 178-505.

Entry informationi

Entry nameiTB22B_HUMAN
AccessioniPrimary (citable) accession number: Q9NU19
Secondary accession number(s): A8KA28
, Q32MQ8, Q5VUK9, Q6P4C3, Q7Z6P7, Q9BPV6, Q9BUT5, Q9NXB6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 8, 2002
Last sequence update: May 10, 2004
Last modified: July 6, 2016
This is version 121 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

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  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.